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Literature summary for 1.1.1.298 extracted from

  • Rathnasingh, C.; Raj, S.M.; Lee, Y.; Catherine, C.; Ashok, S.; Park, S.
    Production of 3-hydroxypropionic acid via malonyl-CoA pathway using recombinant Escherichia coli strains (2012), J. Biotechnol., 157, 633-640.
    View publication on PubMed
Search for more literature for 1.1.1.298

Cloned(Commentary)

Cloned (Comment) Organism
gene mcr, functional expression in Escherichia coli under the T5 promoter control leading to production of 3-hydroxypropionate, coexpression with the nicotinamide nucleotide transhydrogenase that converts NADH to NADPH, required by MCR Chloroflexus aurantiacus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Chloroflexus aurantiacus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
malonate semialdehyde + NADPH + H+ Chloroflexus aurantiacus
-
 3-hydroxypropionate + NADP+
-
 ?
malonate semialdehyde + NADPH + H+ Chloroflexus aurantiacus DSM 635
-
 3-hydroxypropionate + NADP+
-
 ?
additional information Chloroflexus aurantiacus the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298 ?
-
 ?
additional information Chloroflexus aurantiacus DSM 635 the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Chloroflexus aurantiacus Q6QQP7 gene mcr
-
Chloroflexus aurantiacus DSM 635 Q6QQP7 gene mcr
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli Chloroflexus aurantiacus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
10
-
 purified recombinant enzyme, pH 7.8, 55°C Chloroflexus aurantiacus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
malonate semialdehyde + NADPH + H+
-
 Chloroflexus aurantiacus 3-hydroxypropionate + NADP+
-
 ?
malonate semialdehyde + NADPH + H+
-
 Chloroflexus aurantiacus DSM 635 3-hydroxypropionate + NADP+
-
 ?
additional information the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298 Chloroflexus aurantiacus ?
-
 ?
additional information the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298 Chloroflexus aurantiacus DSM 635 ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50 57
-
 Chloroflexus aurantiacus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
37 60 63% of maximal activity at 60°C, maximal activity at 50°C, about 30% at 37°C Chloroflexus aurantiacus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
-
 Chloroflexus aurantiacus

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5 half-maximal activity at pH 6.5 and pH 8.5 Chloroflexus aurantiacus

Cofactor

Cofactor Comment Organism Structure
NADPH dependent on Chloroflexus aurantiacus

General Information

General Information Comment Organism
physiological function the organism assimilates CO2 by the 3-hydroxypropionate cycle, and malonyl-CoA reductase is an essential enzyme for the cycle Chloroflexus aurantiacus