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Literature summary for 1.3.1.9 extracted from

  • Parikh, S.; Moynihan, D.P.; Xiao, G.; Tonge, P.J.
    Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis (1999), Biochemistry, 38, 13623-13634.
    View publication on PubMed
Search for more literature for 1.3.1.9

Cloned(Commentary)

Cloned (Comment) Organism
-
 Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
K165A mutant enzyme is unable to bind NADH Mycobacterium tuberculosis
K165M mutant enzyme is unable to bind NADH Mycobacterium tuberculosis
K165Q wild type activity Mycobacterium tuberculosis
Y158A decreased Kcat, unaffected Km for trans-2-dodecenoyl-CoA, lower Km for NADH Mycobacterium tuberculosis
Y158F decreased Kcat, unaffected Km for trans-2-dodecenoyl-CoA, lower Km for NADH Mycobacterium tuberculosis
Y158S wild type activity Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WGR1
-
-
Mycobacterium tuberculosis H37Rv P9WGR1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trans-2-decenoyl-CoA + NADH
-
 Mycobacterium tuberculosis decanoyl-CoA + NAD+
-
 ?
trans-2-decenoyl-CoA + NADH
-
 Mycobacterium tuberculosis H37Rv decanoyl-CoA + NAD+
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4
-
 stable for 3 months Mycobacterium tuberculosis