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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.9
-
 Mycobacterium tuberculosis

Protein Variants

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

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.9 Mycobacterium tuberculosis P9WGR1
-
-
1.3.1.9 Mycobacterium tuberculosis H37Rv P9WGR1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.9
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.3.1.9 4
-
 stable for 3 months Mycobacterium tuberculosis