IntEnz

EC 1.3.1.9 - Enoyl-[acyl-carrier-protein] reductase (NADH)

IntEnz Enzyme Nomenclature
EC 1.3.1.9

Names

Reaction

• 10240 [IUBMB]
  a 2,3-saturated acyl-[ACP]

  a 2,3-saturated acyl-[ACP]

  GENERIC:9926

  Is ROOT: no
  ROOT compound: GENERIC:9620

  Number of residues: 1

  O-(S-(2,3-saturated)-acylpantetheine-4ʼ-phosphoryl)-L-serine residue O-(S-(2,3-saturated)-acylpantetheine-4'-phosphoryl)-L-serine residue Name origin: UniProt - CHECKED (C) CHEBI:78785 Formula: C17H28N3O9PSR Charge: -1 Position: undefined ChEBI compound status: CHECKED (C)

  +

  NAD⁺

  NAD(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:57540

  Formula: C21H26N7O14P2
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  =

  a (2E)-enoyl-[ACP]

  a (2E)-enoyl-[ACP]

  GENERIC:9925

  Is ROOT: no
  ROOT compound: GENERIC:9620

  Number of residues: 1

  O-(S-(2E)-enoylpantetheine-4ʼ-phosphoryl)-L-serine residue O-(S-(2E)-enoylpantetheine-4'-phosphoryl)-L-serine residue Name origin: UniProt - CHECKED (C) CHEBI:78784 Formula: C17H26N3O9PSR Charge: -1 Position: undefined ChEBI compound status: CHECKED (C)

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  NADH

  NADH

  Name origin: UniProt - CHECKED (C)

  CHEBI:57945

  Formula: C21H27N7O14P2
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

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 [3]. The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.

Links to other databases

References

1. Shimakata, T. and Stumpf, P.K.
   Purification and characterizations of β-ketoacyl-[acyl-carrier-protein] reductase, β-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves.
   Arch. Biochem. Biophys. 218: 77-91 (1982). [PMID: 6756317]
2. Weeks, G. and Wakil, S.J.
   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. 243: 1180-1189 (1968). [PMID: 4384650]
3. Yu, X., Liu, T., Zhu, F., Khosla, C.
   In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli.
   Proc. Natl. Acad. Sci. U.S.A. 108: 18643-18648 (2011). [PMID: 22042840]

[EC 1.3.1.9 created 1972, modified 2013]