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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing diphosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O-atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
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-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
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-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
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-
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
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an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
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(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop-2-enal + NADP+ + AMP + diphosphate
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
(R)-ibuprofen + NADPH + ATP
(2R)-2-(4-(2-methylpropyl)phenyl)propanal + NADP+ + AMP + H2O
2-methoxybenzoate + NADPH + H+ + ATP
2-methoxybenzaldehyde + NADP+ + AMP + diphosphate
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-
-
-
?
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
3-hydroxypropionate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
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-
-
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ir
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
4-hydroxybutyrate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
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-
-
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ir
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
4-nitrobenzoate + NADPH + H+ + ATP
4-nitrobenzaldehyde + NADP+ + AMP + diphosphate
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-
-
-
?
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
5-hydroxypentanoate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
-
-
-
ir
alpha-ketoglutaric acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
benzaldehyde + NADP+ + benzoyladenosine 5'-monophosphate + phosphate
benzoate + NADPH + ATP
-
-
-
-
r
benzoate + NADPH + ATP
benzaldehyde + NADP+ + AMP + phosphate
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
benzoic acid + ATP + NADPH + H+
benzaldehyde + AMP + diphosphate + NADP+
highest turnover number
-
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + benzyl alcohol + NADP+ + AMP + diphosphate
-
-
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
butyric acid + ATP + NADPH + H+
butyraldehyde + AMP + diphosphate + NADP+
-
highest Km value
-
?
caffeic acid + NADPH + ATP
3-(3,4-dihydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
capric acid + ATP + NADPH + H+
capraldehyde + AMP + diphosphate + NADP+
-
-
-
?
caproic acid + ATP + NADPH + H+
caproaldehyde + AMP + diphosphate + NADP+
-
-
-
?
caprylic acid + ATP + NADPH + H+
caprylaldehyde + AMP + diphosphate + NADP+
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
cinnamic acid + NADPH + ATP
3-phenyl-2-propen-1-al + NADP+ + AMP + H2O
cis-aconitic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
citric acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
coniferic acid + NADPH + ATP
coniferyl aldehyde + NADP+ + AMP + phosphate
-
-
-
?
D-malic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
DL-malic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
fatty acid + ATP + NADPH + H+
fatty aldehyde + AMP + diphosphate + NADP+
-
-
-
?
ferulic acid + NADPH + H+ + ATP
3-(4-hydroxy-3-methoxyphenyl)-2-propen-1-al + NADP+ + AMP + diphosphate
-
-
-
?
ferulic acid + NADPH + H+ + ATP
ferulic acid + coniferyl aldehyde + coniferyl alcohol + NADP+ + AMP + diphosphate
not completely reduced
-
-
?
furan-2-carboxylate + NADPH + H+ + ATP
furan-2-carbaldehyde + NADP+ + AMP + diphosphate
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
glutarate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
-
-
-
ir
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
ibuprofen + NADPH + ATP
2-(4-isobutylphenyl)propanal + NADP+ + AMP + H2O
L-malic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
lauric acid + ATP + NADPH + H+
lauraldehyde + AMP + diphosphate + NADP+
highest catalytic efficiency
-
-
?
m-coumaric acid + NADPH + ATP
3-(3-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
m-hydroxybenzoic acid + NADPH + ATP
m-hydroxybenzaldehyde + NADP+ + AMP + H2O
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
malonate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
-
-
-
ir
o-coumaric acid + NADPH + ATP
3-(2-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
p-anisic acid + NADPH + ATP
p-methoxybenzaldehyde + NADP+ + AMP + H2O
p-coumaric acid + NADPH + ATP
3-(4-hydroxphenyl)-2-propen-1-al + NADP+ + AMP + H2O
p-hydroxybenzoic acid + NADPH + ATP
p-hydroxybenzaldehyde + NADP+ + AMP + H2O
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
pyridine-2-carboxylate + NADPH + H+ + ATP
pyridine-2-carbaldehyde + NADP+ + AMP + diphosphate
salicylic acid + NADPH + ATP
salicyl aldehyde + NADP+ + AMP + H2O
sinapic acid + NADPH + ATP
3-(4-hydroxy-3,5-dimethoxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
succinate + NADPH + H+ + ATP
4-oxobutanoate + 1,4-butanedial + NADP+ + AMP + diphosphate
succinate + NADPH + H+ + ATP
? + NADP+ + AMP + diphosphate
-
-
-
-
ir
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
trans-aconitic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
vanillic acid + NADPH + H+ + ATP
4-hydroxy-3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
vanillic acid + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
vanillic acid + NADPH + H+ + ATP
vanillin + vanillyl alcohol + NADP+ + AMP + diphosphate
-
with Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.83, in which recombinant Npt is expressed along with recombinant car, vanillic acid is reduced to vanillin and vanillyl alcohol, with vanillin (80%) as the major product. Escherichia coli BL21-CodonPlus(DE3)-RP/pHAT305 (expressing only recombinant Car) reduce only 50% of the vanillic acid starting material, with vanillyl alcohol being the major metabolite. With Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.83, in which recombinant car is presumed to be in the fully active, phosphopantetheinylated holo form, the rate of reduction of vanillic acid is much faster than that of vanillin to vanillyl alcohol by endogenous Escherichia coli aldehyde dehydrogenase
-
-
?
additional information
?
-
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop-2-enal + NADP+ + AMP + diphosphate
-
-
-
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop-2-enal + NADP+ + AMP + diphosphate
-
-
-
-
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
-
-
-
-
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
-
-
-
-
?
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop2-enal + NADP+ + AMP + diphosphate
-
-
-
-
?
(R)-ibuprofen + NADPH + ATP
(2R)-2-(4-(2-methylpropyl)phenyl)propanal + NADP+ + AMP + H2O
Nocadia sp.
-
-
-
?
(R)-ibuprofen + NADPH + ATP
(2R)-2-(4-(2-methylpropyl)phenyl)propanal + NADP+ + AMP + H2O
Nocadia sp. NRRL 5646
-
-
-
?
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
-
-
-
ir
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
-
-
-
ir
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
-
-
-
?
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
-
-
-
ir
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
-
-
-
ir
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
-
-
-
ir
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
ir
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
ir
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
r
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
r
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Nocadia sp.
-
-
-
ir
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
Nocadia sp. NRRL 5646
-
-
-
ir
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic acids + NADPH + H+ + ATP
aromatic aldehydes + NADP+ + AMP + diphosphate + H2O
-
-
-
?
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + ATP
benzaldehyde + NADP+ + AMP + phosphate
-
-
-
-
?
benzoate + NADPH + ATP
benzaldehyde + NADP+ + AMP + phosphate
best substrate
-
-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
via an adenylated intermediate
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
via an adenylated intermediate
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
via an adenylated intermediate
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
rate relative to salycilate 286%
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
Nocadia sp.
-
the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
Nocadia sp. NRRL 5646
-
the reaction proceeds via benzoyladenosine 5'-monophosphate which is further reduced by NADPH to benzaldehyde
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
benzoic acid + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
-
-
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
cinnamate + NADPH + H+ + ATP
cinnamaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
cinnamic acid + NADPH + ATP
3-phenyl-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
cinnamic acid + NADPH + ATP
3-phenyl-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
cinnamic acid + NADPH + ATP
3-phenyl-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
furan-2-carboxylate + NADPH + H+ + ATP
furan-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
furan-2-carboxylate + NADPH + H+ + ATP
furan-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
-
-
-
ir
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
-
-
ir
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
-
-
-
ir
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
-
-
-
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
-
-
-
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
-
-
-
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
-
-
-
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
-
-
-
?
hexanoate + NADPH + H+ + ATP
hexanal + NADP+ + AMP + diphosphate
-
-
-
?
ibuprofen + NADPH + ATP
2-(4-isobutylphenyl)propanal + NADP+ + AMP + H2O
Nocadia sp.
-
-
-
?
ibuprofen + NADPH + ATP
2-(4-isobutylphenyl)propanal + NADP+ + AMP + H2O
Nocadia sp. NRRL 5646
-
-
-
?
m-coumaric acid + NADPH + ATP
3-(3-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
m-coumaric acid + NADPH + ATP
3-(3-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
m-hydroxybenzoic acid + NADPH + ATP
m-hydroxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
m-hydroxybenzoic acid + NADPH + ATP
m-hydroxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
-
low activity
-
-
ir
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
low activity
-
-
ir
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
-
low activity
-
-
ir
o-coumaric acid + NADPH + ATP
3-(2-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
o-coumaric acid + NADPH + ATP
3-(2-hydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
-
-
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
-
-
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
-
-
-
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
-
-
-
?
p-anisic acid + NADPH + ATP
p-methoxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
p-anisic acid + NADPH + ATP
p-methoxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
p-coumaric acid + NADPH + ATP
3-(4-hydroxphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
p-coumaric acid + NADPH + ATP
3-(4-hydroxphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
p-coumaric acid + NADPH + ATP
3-(4-hydroxphenyl)-2-propen-1-al + NADP+ + AMP + H2O
-
-
-
?
p-hydroxybenzoic acid + NADPH + ATP
p-hydroxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
p-hydroxybenzoic acid + NADPH + ATP
p-hydroxybenzaldehyde + NADP+ + AMP + H2O
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
piperonylate + NADPH + H+ + ATP
piperonylaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
pyridine-2-carboxylate + NADPH + H+ + ATP
pyridine-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
pyridine-2-carboxylate + NADPH + H+ + ATP
pyridine-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
salicylic acid + NADPH + ATP
salicyl aldehyde + NADP+ + AMP + H2O
-
-
-
?
salicylic acid + NADPH + ATP
salicyl aldehyde + NADP+ + AMP + H2O
-
rate relative to benzoate 9%
-
?
succinate + NADPH + H+ + ATP
4-oxobutanoate + 1,4-butanedial + NADP+ + AMP + diphosphate
-
-
-
ir
succinate + NADPH + H+ + ATP
4-oxobutanoate + 1,4-butanedial + NADP+ + AMP + diphosphate
-
-
-
-
ir
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
?
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillic acid + NADPH + H+ + ATP
4-hydroxy-3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
vanillic acid + NADPH + H+ + ATP
4-hydroxy-3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
vanillic acid + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
?
vanillic acid + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
?
additional information
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
-
no activity of the wild-type enzyme with succinate. Substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
-
substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
the enzyme is active against C2-C18 fatty acids. Enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
-
-
-
additional information
?
-
the enzyme is active against C2-C18 fatty acids. Enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
-
no activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, phenylpropynoate, butanoate, pyridine-2-carboxylate, 1H-pyrrole-2-carboxylate, and furan-2-carboxylate
-
-
-
additional information
?
-
-
enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity. No activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, phenylpropynoate, pyridine-2-carboxylate, and 1H-pyrrole-2-carboxylate
-
-
-
additional information
?
-
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
additional information
?
-
-
substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
additional information
?
-
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
additional information
?
-
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
additional information
?
-
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
additional information
?
-
NcCAR wild-type and mutants efficiently reduce aliphatic acids
-
-
-
additional information
?
-
Nocadia sp.
-
other substrates are phenyl-substituted aliphatic acids, heterocyclic carboxylic acids, polyaromatic ring carboxylic acids, ibuprofen and its (R)-(-) isomer
-
-
?
additional information
?
-
Nocadia sp. NRRL 5646
-
other substrates are phenyl-substituted aliphatic acids, heterocyclic carboxylic acids, polyaromatic ring carboxylic acids, ibuprofen and its (R)-(-) isomer
-
-
?
additional information
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
-
the enzyme prefers benzoates and aliphatic acids that are substituted with a phenyl group in the 3-position. No reaction of this CAR with simple aliphatic acids
-
-
-
additional information
?
-
-
the enzyme prefers benzoates and aliphatic acids that are substituted with a phenyl group in the 3-position. No reaction of this CAR with simple aliphatic acids
-
-
-
additional information
?
-
-
enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
-
-
-
additional information
?
-
pyruvic, isocitric acid, fumaric acid and maleic acid are not substrates for the enzyme
-
-
?
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
no activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, pyridine-2-carboxylate, 1H-pyrrole-2-carboxylate, and furan-2-carboxylate
-
-
-
additional information
?
-
-
substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
additional information
?
-
-
no activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, 1H-pyrrole-2-carboxylate and furan-2-carboxylate
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
-
-
-
additional information
?
-
-
the enzyme is active against C2-C18 fatty acids
-
-
-
additional information
?
-
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
-
-
-
additional information
?
-
-
the enzyme is active against C2-C18 fatty acids
-
-
-
additional information
?
-
-
no activity with 2-nitrobenzoate and 1H-pyrrole-2-carboxylate
-
-
-
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evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
evolution
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
evolution
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
evolution
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
evolution
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
evolution
analysis of highly conserved signature sequences of CARs, overview
evolution
-
CAR phylogenetic analysis and tree
evolution
-
CAR phylogenetic analysis and tree
evolution
-
CAR phylogenetic analysis and tree
evolution
-
CAR phylogenetic analysis and tree
evolution
-
CAR phylogenetic analysis and tree
evolution
CAR phylogenetic analysis and tree
evolution
-
CAR phylogenetic analysis and tree
evolution
CAR phylogenetic analysis and tree
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
CAR phylogenetic analysis and tree
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
analysis of highly conserved signature sequences of CARs, overview
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
analysis of highly conserved signature sequences of CARs, overview
-
evolution
-
analysis of highly conserved signature sequences of CARs, overview
-
evolution
-
analysis of highly conserved signature sequences of CARs, overview
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
analysis of highly conserved signature sequences of CARs, overview
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
evolution
-
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
-
malfunction
lack of posttranslational phosphopantetheinylation of a serine group in the recombinant CAR reduces the activity of recombinantly expressed enzyme
malfunction
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
malfunction
-
the purified CAR with a mutation to its conserved serine idue appears to degrade into separate A- and R-domains when incubated at room temperature
malfunction
-
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
-
malfunction
-
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
-
malfunction
-
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
-
malfunction
-
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
-
malfunction
-
replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity
-
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids
physiological function
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. Enzyme CAR from Mycobacterium marinum (mmCAR) reduces a number of aliphatic acids ranging from C3 to C18
physiological function
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. The purified enzyme from Nocardia iowensis reduces a broader range of substituted aromatic acids in addition to dicarboxylic acids of the citric acid cycle, resulting in a branding of the aryl-aldehyde oxidoreductase class more broadly as carboxylic acid reductases (CARs)
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. Whole cell reduction of aromatic carboxylic acids in the white-rot fungi Trametes versicolor
physiological function
requirement for the presence of a phosphopantetheine transferase for the loading of a phosphopantetheine group onto the CAR enzyme is shown for niCAR. Enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
physiological function
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
physiological function
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
physiological function
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
physiological function
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
-
physiological function
-
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. Enzyme CAR from Mycobacterium marinum (mmCAR) reduces a number of aliphatic acids ranging from C3 to C18
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
physiological function
-
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
-
additional information
structure homology modeling
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
additional information
-
structure-function analysis and structure comparisons
additional information
-
structure-function analysis and structure comparisons
additional information
-
structure-function analysis and structure comparisons
additional information
-
structure-function analysis and structure comparisons
additional information
-
structure-function analysis and structure comparisons
additional information
structure-function analysis and structure comparisons
additional information
-
structure-function analysis and structure comparisons
additional information
structure-function analysis and structure comparisons
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
-
additional information
-
structure-function analysis and structure comparisons
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
-
additional information
-
structure homology modeling
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
-
additional information
-
structure homology modeling
-
additional information
-
structure homology modeling
-
additional information
-
structure homology modeling
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
-
additional information
-
structure homology modeling
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
-
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E697Q
-
site-directed mutagenesis, the mutant enzyme retains 48.8% of wild-type activity with benzoate substrate
Q637E
-
site-directed mutagenesis, the mutant enzyme retains 47.1% of wild-type activity with benzoate substrate
A922G
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
E441A
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
F787A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G432A
-
site-directed mutagenesis, the mutant shows activity similar to wild-type
G457A
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
G592A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G691A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G694A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G697A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G755A
site-directed mutagenesis, the mutant has activity similar to wild-type
G843A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
G882A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
K190A
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
N885A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
P189A
-
site-directed mutagenesis, the mutant shows activity similar to wild-type
P198A
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
P285A
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
P904A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
S595A
site-directed mutagenesis, inactive mutant
T186A
-
site-directed mutagenesis, the mutant shows activity similar to wild-type
Y542A
site-directed mutagenesis, the enzyme shows reduced activity compared to wild-type
E433A
-
site-directed mutagenesis, inactive mutant
-
H237A
-
site-directed mutagenesis, inactive mutant
-
P285A
-
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
-
S595A
-
site-directed mutagenesis, inactive mutant
-
E433A
-
site-directed mutagenesis, inactive mutant
-
H237A
-
site-directed mutagenesis, inactive mutant
-
P285A
-
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
-
S595A
-
site-directed mutagenesis, inactive mutant
-
E433A
-
site-directed mutagenesis, inactive mutant
-
H237A
-
site-directed mutagenesis, inactive mutant
-
P285A
-
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
-
S595A
-
site-directed mutagenesis, inactive mutant
-
E433A
-
site-directed mutagenesis, inactive mutant
-
H237A
-
site-directed mutagenesis, inactive mutant
-
P285A
-
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
-
S595A
-
site-directed mutagenesis, inactive mutant
-
E433A
-
site-directed mutagenesis, inactive mutant
-
H237A
-
site-directed mutagenesis, inactive mutant
-
P285A
-
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
-
S595A
-
site-directed mutagenesis, inactive mutant
-
S689A
-
completely inactive
S691A
-
has 39% of the activity of recombinant car
S694A
-
has 50% of the activity of recombinant car
S696A
-
has 76% of the activity of recombinant car
E337A
site-directed mutagenesis, inactive mutant
E337A
-
site-directed mutagenesis, mutant shows decreased activity compared to wild-type
E433A
site-directed mutagenesis, inactive mutant
E433A
-
site-directed mutagenesis, mutant shows decreased activity compared to wild-type
H237A
site-directed mutagenesis, inactive mutant
H237A
-
site-directed mutagenesis, mutant shows decreased activity compared to wild-type
K848A
-
site-directed mutagenesis, inactive mutant
K848A
site-directed mutagenesis, inactive mutant
P234A
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
P234A
site-directed mutagenesis, the enzyme shows altered substrate specificity compared to wild-type
Y844A
-
site-directed mutagenesis, inactive mutant
Y844A
site-directed mutagenesis, inactive mutant
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
-
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Kutzneria albida (Ka) resulting in hybrid enzymes: Mav(A)-Ka(PR), Mav(AP)-Ka(R), Ka(A)-Mav(PR), and Ka(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes
additional information
-
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Mycobacterium marinum (Mm), Kutzneria albida (Ka), and Nocardia iowensis (Ni), and one fungal strain, Neurospora crassa (Nc), resulting in hybrid enzymes: Mav(A)-Mm(PR), Mav(AP)-Mm(R), Mm(A)-Mav(PR), Mm(AP)-Mav(R), Mav(A)-Ka(PR), Mav(AP)-Ka(R), Ka(A)-Mav(PR), Ka(AP)-Mav(R), Mav(A)-Ni(PR), Mav(AP)-Ni(R), Ni(A)-Mav(PR), and Ni(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs, overview. When mutations Q637E and E697Q are introduced into hybrid CAR, Mm(A)-Mav(PR), reduction in activities is also observed, albeit to a less extent. Analysis of substrate specificity of recombinant hybrid mutant enzymes
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
additional information
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Mycobacterium marinum (Mm) resulting in hybrid enzymes: Mav(A)-Mm(PR), Mav(AP)-Mm(R), Mm(A)-Mav(PR), and Mm(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
-
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Mycobacterium marinum (Mm) resulting in hybrid enzymes: Mav(A)-Mm(PR), Mav(AP)-Mm(R), Mm(A)-Mav(PR), and Mm(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
additional information
-
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from fungus Neurospora crassa (Nc), resulting in hybrid enzymes: Mav(A)-Nc(PR), Mav(AP)-Nc(R), Nc(A)-Mav(PR), and Nc(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes
additional information
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
additional information
-
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
-
additional information
-
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
-
additional information
-
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
-
additional information
-
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
-
additional information
-
the replacement of Gly184, Arg870, and Trp978 by alanine does not result in soluble expression. Pro904 is located close to Trp978, and its substitution by Ala yields significantly less soluble protein. Replacement of His237, Glu433, Ser595, Tyr844, and Lys848 by Ala abolishes CAR activity. Substitutions with alanine (P189A, P234A, P285A, E441A, and G457A) enhanced the specific activity toward hexanoic acid compared to the wild-type
-
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
additional information
-
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Nocardia iowensis (Ni) resulting in hybrid enzymes: Mav(A)-Ni(PR), Mav(AP)-Ni(R), Ni(A)-Mav(PR), and Ni(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
-
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
-
additional information
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analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
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additional information
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analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
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additional information
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analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
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industry
vanillic acid reduction in Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.85 cells containing car, npt and gdh is complete in 6 h, and is faster than in cells containing only car and/or npt. The availability of Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.85 expressing holo-Car and Gdh provides a means of generating a range of value-added aldehydes or alcohols of importance in pharmaceutical, food and agricultural industries. Uses of directed evolution and related mutant generating processes, may enable a Car-system with broader substrate specificities and one that is capable of achieving much higher product yields
synthesis
by combining the carboxylic acid reductase-dependent pathway with an exogenous fatty acid-generating lipase, natural oils (coconut oil, palm oil, and algal oil bodies) can be enzymatically converted into fatty alcohols across a broad chain length range (C8-C18)
synthesis
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carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Aldehydes as reactive intermediates in biosynthetic pathways, overview
synthesis
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carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Aldehydes as reactive intermediates in biosynthetic pathways, overview
synthesis
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carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Aldehydes as reactive intermediates in biosynthetic pathways, overview
synthesis
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carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Aldehydes as reactive intermediates in biosynthetic pathways, overview
synthesis
-
carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Aldehydes as reactive intermediates in biosynthetic pathways, overview
synthesis
carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Recombinant enzyme expression in Saccharomyces cerevisiae and Saccharomyces pombe and an engineered aldehyde-accumulating Escherichia coli strain for de novo production of vanillin from glucose. Aldehydes as reactive intermediates in biosynthetic pathways, overview
synthesis
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carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. The CAR from Mycobacterium marinum (mmCAR) reduces a number of aliphatic acids ranging from C3 to C18, expanding the potential of CARs in synthetic pathways. Aldehydes as reactive intermediates in biosynthetic pathways, overview
synthesis
carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. The CAR from Mycobacterium marinum (mmCAR) reduces a number of aliphatic acids ranging from C3 to C18, expanding the potential of CARs in synthetic pathways. Aldehydes as reactive intermediates in biosynthetic pathways, overview
synthesis
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carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts
synthesis
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carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts
synthesis
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carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts
synthesis
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carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts, application for the reduction of fatty acids to fatty alcohols
synthesis
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carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts, application for the reduction of fatty acids to fatty alcohols
synthesis
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carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts, application for the reduction of fatty acids to fatty alcohols
synthesis
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carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts, application for the reduction of fatty acids to fatty alcohols
synthesis
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carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts, application for the reduction of fatty acids to fatty alcohols
synthesis
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carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts, application for the reduction of fatty acids to fatty alcohols
synthesis
carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts, application for the reduction of fatty acids to fatty alcohols
synthesis
carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts. The reduction of racemic ibuprofen by whole Nocardia iowensis cells gives an enantiomeric excess (ee) of 61.2%, which is attributed to enantioselectivity by niCAR based on kinetic data for its reduction of (S)-(+)- and (R)-(-)-ibuprofen enantiomers
synthesis
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the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
synthesis
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
synthesis
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
synthesis
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
synthesis
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
synthesis
-
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
-
synthesis
-
carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts, application for the reduction of fatty acids to fatty alcohols
-
synthesis
-
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
-
synthesis
-
carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. The CAR from Mycobacterium marinum (mmCAR) reduces a number of aliphatic acids ranging from C3 to C18, expanding the potential of CARs in synthetic pathways. Aldehydes as reactive intermediates in biosynthetic pathways, overview
-
synthesis
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the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
-
synthesis
-
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
-
synthesis
-
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
-
synthesis
-
carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts
-
synthesis
-
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
-
synthesis
-
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
-
synthesis
-
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
-
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