Literature summary for 1.3.1.118 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 .

Search for more literature for 1.3.1.118

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WGR1	-	-
Mycobacterium tuberculosis ATCC 25618	P9WGR1	-	-

Synonyms

Synonyms	Comment	Organism
enoyl-ACP reductase	-	Mycobacterium tuberculosis
InhA	-	Mycobacterium tuberculosis

General Information

General Information	Comment	Organism
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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)