CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family Enoyl-[acyl-carrier-protein] reductase [NADH]

Enzyme Information

1.3.1.9
Enoyl-[acyl-carrier-protein] reductase (NADH).
based on mapping to UniProt P9WGR1
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH.
-!- The enzyme catalyzes 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.

UniProtKB Entries (1)

P9WGR1
INHA_MYCTU
Mycobacterium tuberculosis H37Rv
Enoyl-[acyl-carrier-protein] reductase [NADH]

PDB Structure

PDB 4BGI
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Pyridomycin bridges the NADH- and substrate-binding pockets of the enoyl reductase InhA.
Hartkoorn, R.C., Pojer, F., Read, J.A., Gingell, H., Neres, J., Horlacher, O.P., Altmann, K.H., Cole, S.T.
Nat. Chem. Biol.