Literature summary extracted from

Rozwarski, D.; Vilcheze, C.; Sugantino, M.; Bittman, R.; Sacchettini, J.
Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate (1999), J. Biol. Chem., 274, 15582-15598 .

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.3.1.118	the crystal structure of the enzyme in complex with NAD+ and trans-2-hexadecenoyl-(N-acetylcysteamine)-thioester reveals that the substrate binds in a general U-shaped conformation, with the trans double bond positioned directly adjacent to the nicotinamide ring of NAD+. The side chain of Tyr158 directly interacts with the thioester carbonyl oxygen of the C16 fatty acyl substrate and therefore can help stabilize the enolate intermediate, proposed to form during substrate catalysis. Hydrophobic residues, primarily from the substrate binding loop (residues 196-219), engulf the fatty acyl chain portion of the substrate. The substrate binding loop of InhA is longer than that of other enoyl-ACP reductases and creates a deeper substrate binding crevice, consistent with the ability of InhA to recognize longer chain fatty acyl substrates	Mycobacterium tuberculosis

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.3.1.118	Mycobacterium tuberculosis	P9WGR1	-	-
1.3.1.118	Mycobacterium tuberculosis ATCC 25618	P9WGR1	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
1.3.1.118	enoyl-ACP reductase	-	Mycobacterium tuberculosis
1.3.1.118	InhA	-	Mycobacterium tuberculosis

General Information

EC Number	General Information	Comment	Organism
1.3.1.118	metabolism	the enzyjme is a member of an FAS-II system that prefers longer chain fatty acylsubstrates for the purpose of synthesizing mycolic acids, a major component of mycobacterial cell walls	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)