| Entry |
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| Name |
enoyl-[acyl-carrier-protein] reductase (NADH);
enoyl-[acyl carrier protein] reductase;
enoyl-ACP reductase;
NADH-enoyl acyl carrier protein reductase;
NADH-specific enoyl-ACP reductase;
acyl-[acyl-carrier-protein]:NAD+ oxidoreductase;
fabI (gene name)
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| Class |
Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor
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| Sysname |
acyl-[acyl-carrier protein]:NAD+ oxidoreductase
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| Reaction(IUBMB) |
an acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+ [RN: R01403]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
trans-2,3-dehydroacyl-[acyl-carrier protein] [CPD: C00693];
NADH [CPD: C00004];
H+ [CPD: C00080]
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| Comment |
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.
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| History |
EC 1.3.1.9 created 1972, modified 2013
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| Pathway |
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| Orthology |
| K00208 | enoyl-[acyl-carrier protein] reductase I |
| K00209 | enoyl-[acyl-carrier protein] reductase / trans-2-enoyl-CoA reductase (NAD+) |
| K02371 | enoyl-[acyl-carrier protein] reductase II |
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| Genes |
» show all
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| Reference |
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| Authors |
Shimakata T, Stumpf PK. |
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| Title |
Purification and characterizations of beta-Ketoacyl-[acyl-carrier-protein] reductase, beta-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves. |
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| Journal |
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| Reference |
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| Authors |
Weeks G, Wakil SJ. |
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| Title |
Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli. |
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| Journal |
J Biol Chem 243:1180-9 (1968) |
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| Reference |
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| Authors |
Yu X, Liu T, Zhu F, Khosla C |
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| Title |
In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli. |
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| Journal |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 1.3.1.9 |
| ExPASy - ENZYME nomenclature database: | 1.3.1.9 |
| BRENDA, the Enzyme Database: | 1.3.1.9 |
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