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Information on EC 1.3.1.39 - enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and Organism(s) Bacillus subtilis and UniProt Accession P71079

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IUBMB Comments
This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is one of the activities of EC 2.3.1.85, fatty-acid synthase system. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH).
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Bacillus subtilis
UNIPROT: P71079
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
acyl-ACP dehydrogenase, enoyl-ACP reductase, enoyl-ACP reductase III, enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase, FabI, FabK, FabL, NADPH 2-enoyl Co A reductase, PG1416, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
enoyl-ACP reductase III
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acyl-ACP dehydrogenase
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enoyl-ACP reductase
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enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase
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NADPH 2-enoyl Co A reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Re-specific)
This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is one of the activities of EC 2.3.1.85, fatty-acid synthase system. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH).
CAS REGISTRY NUMBER
COMMENTARY hide
37251-09-5
not distinguished from EC 1.3.1.10
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform FabL
UniProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme and in complex with NADPH and inhibitor triclosan, to 2.8 A and 1.8 A resolution, respectively
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, K.H.; Ha, B.H.; Kim, S.J.; Hong, S.K.; Hwang, K.Y.; Kim, E.E.
Crystal structures of enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis
J. Mol. Biol.
406
403-415
2011
Bacillus subtilis (P71079), Bacillus subtilis 168 (P71079)
Manually annotated by BRENDA team