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 4UVG
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Hitting the Target in More Than One Way: Novel, Direct Inhibitors of Mycobacterium Tuberculosis Enoyl Acp Reductase
Madhavapeddi, P., Kale, R.R., Cowen, S.D., Ghorpade, S.R., Davies, G., Bellale, E.V., Kale, M.G., Srivastava, A., Spadola, L., Kawatkar, A., Raichurkar, A.V., Tonge, M., Nandishaiah, R., Guptha, S., Narayan, A., Gingell, H., Plant, D., Landge, S., Menasinakai, S., Prabhakar, K.R., Achar, V., Ambady, A., Sambandamurthy, V.K., Ramachandran, V., Panduga, V., Reddy, J., Kumar, C.N.N., Kaur, P., Shandil, R., Iyer, P.S., Narayanan, S., Read, J.A.
To be Published
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