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 5JFO
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Antitubercular drugs for an old target: GSK693 as a promising InhA direct inhibitor.
Martinez-Hoyos, M., Perez-Herran, E., Gulten, G., Encinas, L., Alvarez-Gomez, D., Alvarez, E., Ferrer-Bazaga, S., Garcia-Perez, A., Ortega, F., Angulo-Barturen, I., Rullas-Trincado, J., Blanco Ruano, D., Torres, P., Castaneda, P., Huss, S., Fernandez Menendez, R., Gonzalez Del Valle, S., Ballell, L., Barros, D., Modha, S., Dhar, N., Signorino-Gelo, F., McKinney, J.D., Garcia-Bustos, J.F., Lavandera, J.L., Sacchettini, J.C., Jimenez, M.S., Martin-Casabona, N., Castro-Pichel, J., Mendoza-Losana, A.
Ebiomedicine