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Information on EC 1.3.1.9 - enoyl-[acyl-carrier-protein] reductase (NADH) and Organism(s) Bacillus cereus and UniProt Accession Q81GI3

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IUBMB Comments
The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18 . The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
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Bacillus cereus
UNIPROT: Q81GI3
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Word Map
The taxonomic range for the selected organisms is: Bacillus cereus
The enzyme appears in selected viruses and cellular organisms
Synonyms
pfenr, enoyl-acyl carrier protein, enoyl acyl carrier protein reductase, mtinha, enoyl acp reductase, nadh-dependent enoyl-acp reductase, enoyl-reductase, fabi1, fabi2, nadh-dependent enoyl-acyl carrier protein reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cold-shock induced protein 15
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CSI15
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enoyl-ACP reductase
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NADH-dependent enoyl-ACP reductase
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NADH-enoyl acyl carrier protein reductase
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NADH-specific enoyl-ACP reductase
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reductase, enoyl-[acyl carrier protein]
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VEG241
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vegetative protein 241
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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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]:NAD+ oxidoreductase
The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18 [3]. The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
CAS REGISTRY NUMBER
COMMENTARY hide
37251-08-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo form and in the ternary complex with NADP+ and an indole naphthyridinone inhibitor, to 3.0 and 2.2 A resolution, respectively. The two structures are almost identical, except for the three stretches that are disordered in the apo form. The apo form exists as a homo-dimer in both crystal and solution, while the ternary complex forms a homo-tetramer. The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, S.J.; Ha, B.H.; Kim, K.H.; Hong, S.K.; Shin, K.J.; Suh, S.W.; Kim, E.E.
Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus
Biochem. Biophys. Res. Commun.
400
517-522
2010
Bacillus cereus (Q81GI3), Bacillus cereus DSM 31 (Q81GI3)
Manually annotated by BRENDA team