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Literature summary for 1.1.1.385 extracted from

  • Parker, J.B.; Walsh, C.T.
    Action and timing of BacC and BacD in the late stages of biosynthesis of the dipeptide antibiotic bacilysin (2013), Biochemistry, 52, 889-901.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.385

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli with an N-terminal His6tag Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(1R,2S,5R,6S)-dihydroanticapsin + NAD+ Bacillus subtilis (1R,2S,5R,6S)-dihydroanticapsin i.e. 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine. The enzyme is involved in the biosynthesis of the dipeptide antibiotic bacilysin (1R,2S,6R)-anticapsin + NADH + H+ (1R,2S,6R)-anticapsin i.e. 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine ?
(1R,2S,5R,6S)-dihydroanticapsin + NAD+ Bacillus subtilis 168 (1R,2S,5R,6S)-dihydroanticapsin i.e. 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine. The enzyme is involved in the biosynthesis of the dipeptide antibiotic bacilysin (1R,2S,6R)-anticapsin + NADH + H+ (1R,2S,6R)-anticapsin i.e. 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P39640
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-
Bacillus subtilis 168 P39640
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1R,2S,5R,6S)-dihydroanticapsin + NAD+ (1R,2S,5R,6S)-dihydroanticapsin i.e. 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine. The enzyme is involved in the biosynthesis of the dipeptide antibiotic bacilysin Bacillus subtilis (1R,2S,6R)-anticapsin + NADH + H+ (1R,2S,6R)-anticapsin i.e. 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine ?
(1R,2S,5R,6S)-dihydroanticapsin + NAD+ (1R,2S,5R,6S)-dihydroanticapsin i.e. 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine. Exogenous enzyme is added into crude DELTAbacC extracts and dihydroanticapsin transformation is analyzed by LC-MS. Wild-type extract contains a significant amount of bacilysin and a minor amount of anticapsin, but the DELTA extract does not possess a detectable amount of either. However, the DELTAbacC extract contains accumulated amounts of masses corresponding to dihydroanticapsin and dihydrobacilysin, which contain the intact epoxide but possess a C7-hydroxyl moiety in place of the C7-ketone found in mature anticapsin and bacilysin. This finding is consistent with the assignment of the enzyme (BacC) as the dehydrogenase used to oxidize the C7-hydroxyl and strongly suggests that the enzyme (BacC) oxidation occurs sometime after the epoxidation of the cyclohexenol double bond. When the DELTAbacC extract is exposed to the enzyme (BacC) the C7-hydroxyl of hydroanticapsin is oxidized to generate anticapsin. The enzyme (BacC) has no oxidation activity on the dihydrobacilysin dipeptide Bacillus subtilis (1R,2S,6R)-anticapsin + NADH + H+ (1R,2S,6R)-anticapsin i.e. 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine ?
(1R,2S,5R,6S)-dihydroanticapsin + NAD+ (1R,2S,5R,6S)-dihydroanticapsin i.e. 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine. The enzyme is involved in the biosynthesis of the dipeptide antibiotic bacilysin Bacillus subtilis 168 (1R,2S,6R)-anticapsin + NADH + H+ (1R,2S,6R)-anticapsin i.e. 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine ?
(1R,2S,5R,6S)-dihydroanticapsin + NAD+ (1R,2S,5R,6S)-dihydroanticapsin i.e. 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine. Exogenous enzyme is added into crude DELTAbacC extracts and dihydroanticapsin transformation is analyzed by LC-MS. Wild-type extract contains a significant amount of bacilysin and a minor amount of anticapsin, but the DELTA extract does not possess a detectable amount of either. However, the DELTAbacC extract contains accumulated amounts of masses corresponding to dihydroanticapsin and dihydrobacilysin, which contain the intact epoxide but possess a C7-hydroxyl moiety in place of the C7-ketone found in mature anticapsin and bacilysin. This finding is consistent with the assignment of the enzyme (BacC) as the dehydrogenase used to oxidize the C7-hydroxyl and strongly suggests that the enzyme (BacC) oxidation occurs sometime after the epoxidation of the cyclohexenol double bond. When the DELTAbacC extract is exposed to the enzyme (BacC) the C7-hydroxyl of hydroanticapsin is oxidized to generate anticapsin. The enzyme (BacC) has no oxidation activity on the dihydrobacilysin dipeptide Bacillus subtilis 168 (1R,2S,6R)-anticapsin + NADH + H+ (1R,2S,6R)-anticapsin i.e. 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine ?
(2S,4S,7R)-tetrahydrotyrosine + NAD+ (2S,4S,7R)-tetrahydrotyrosine is a surrogate substrate for the enzyme, because currently there is no route for purifying dihydroanticapsin (with the epoxide intact) from DELTAbacC strain extracts. No activity with (2S,4R,7R)-tetrahydrotyrosine Bacillus subtilis 3-[(1S)-4-oxocyclohex-2-en-1-yl]-L-alanine + NADH + H+
-
 ?
(2S,4S,7R)-tetrahydrotyrosine + NAD+ (2S,4S,7R)-tetrahydrotyrosine is a surrogate substrate for the enzyme, because currently there is no route for purifying dihydroanticapsin (with the epoxide intact) from DELTAbacC strain extracts. No activity with (2S,4R,7R)-tetrahydrotyrosine Bacillus subtilis 168 3-[(1S)-4-oxocyclohex-2-en-1-yl]-L-alanine + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
BacC
-
 Bacillus subtilis
BSU37720 locus name Bacillus subtilis
ywfD
-
 Bacillus subtilis

General Information

General Information Comment Organism
malfunction dihydroanticapsin and dihydrobacilysin accumulate in extracts of a DELTAbacC strain and are processed to anticapsin and then bacilysin upon addition of BacC and BacD, respectively Bacillus subtilis
metabolism the enzyme is involved in the biosynthesis of the dipeptide antibiotic bacilysin Bacillus subtilis