|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 184.108.40.206
Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: enoyl-[acyl-carrier-protein] reductase (NADH)
Enzyme Commission Synonyms: 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), inhA (gene name)
Enzyme Commission Summary:
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 [Yu11]. The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12-24 carbons [Quemard95, Rozwarski99].
Instance reactions of [an acyl-[acyl-carrier protein] + NAD+ = a trans-2-enoyl-[acyl-carrier protein] + NADH + H+] (220.127.116.11):
i1: a dodecanoyl-[acp] + NAD+ ← a (2E)-dodec-2-enoyl-[acp] + NADH + H+ (18.104.22.168)
i2: a palmitoyl-[acp] + NAD+ ← a trans hexadecenoyl-[acp] + NADH + H+ (22.214.171.124)
i3: a myristoyl-[acp] + NAD+ ← a trans tetradec-2-enoyl-[acp] + NADH + H+ (126.96.36.199)
i4: a hexanoyl-[acyl-carrier-protein] + NAD+ ← a trans hex-2-enoyl-[acp] + NADH + H+ (188.8.131.52)
i5: a decanoyl-[acp] + NAD+ ← a (2E)-dec-2-enoyl-[acp] + NADH + H+ (184.108.40.206)
i6: an octanoyl-[acp] + NAD+ ← a trans oct-2-enoyl-[acp] + NADH + H+ (220.127.116.11)
i7: a butyryl-[acp] + NAD+ ← a crotonyl-[acp] + NADH + H+ (18.104.22.168)
Quemard95: Quemard A, Sacchettini JC, Dessen A, Vilcheze C, Bittman R, Jacobs WR, Blanchard JS (1995). "Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis." Biochemistry 34(26);8235-41. PMID: 7599116
Rozwarski99: Rozwarski DA, Vilcheze C, Sugantino M, Bittman R, Sacchettini JC (1999). "Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate." J Biol Chem 274(22);15582-9. PMID: 10336454
Shimakata82: Shimakata T, Stumpf PK (1982). "Purification and characterizations of beta-Ketoacyl-[acyl-carrier-protein] reductase, beta-hydroxyacyl-[acyl-carrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves." Arch Biochem Biophys 218(1);77-91. PMID: 6756317
Weeks68: Weeks G, Wakil SJ (1968). "Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli." J Biol Chem 1968;243(6);1180-9. PMID: 4384650
Yu11: Yu X, Liu T, Zhu F, Khosla C (2011). "In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli." Proc Natl Acad Sci U S A 108(46);18643-8. PMID: 22042840
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