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 4COD
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Encoded Library Technology as a Source of Hits for the Discovery and Lead Optimization of a Potent and Selective Class of Bactericidal Direct Inhibitors of Mycobacterium Tuberculosis Inha.
Encinas, L., O'Keefe, H., Neu, M., Remuinan, M.J., Patel, A.M., Guardia, A., Davie, C.P., Perez-Macias, N., Yang, H., Convery, M.A., Messer, J.A., Perez-Herran, E., Centrella, P.A., Alvarez-Gomez, D., Clark, M.A., Huss, S., O'Donovan, G.K., Ortega-Muro, F., Mcdowell, W., Castaneda, P., Arico-Muendel, C.C., Pajk, S., Rullas, J., Angulo-Barturen, I., Alvarez-Ruiz, E., Mendoza-Losana, A., Pages, L.B., Castro-Pichel, J., Evindar, G.
J.Med.Chem.