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Literature summary for 1.1.1.51 extracted from

  • Schultz, R.M.; Groman, E.V.; Engel, L.L.
    3(17)beta-Hydroxysteroid dehydrogenase of Pseudomonas testosteroni. Ligand binding properties (1977), J. Biol. Chem., 252, 3784-3790.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.063
-
3-pyridinealdehyde adenine dinucleotide testosterone as substrate Comamonas testosteroni
0.083
-
NAD+ testosterone as substrate Comamonas testosteroni
0.083
-
Thionicotinamide adenine dinucleotide testosterone as substrate Comamonas testosteroni
0.685
-
3-acetylpyridine adenine dinucleotide testosterone as substrate Comamonas testosteroni

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
testosterone + 3-acetylpyridine adenine dinucleotide
-
Comamonas testosteroni ?
-
?
testosterone + 3-pyridinealdehyde adenine dinucleotide
-
Comamonas testosteroni ?
-
?
testosterone + NAD+
-
Comamonas testosteroni androstenedione + NADH + H+
-
r
testosterone + thionicotinamide adenine dinucleotide
-
Comamonas testosteroni ?
-
?

Cofactor

Cofactor Comment Organism Structure
3-acetylpyridine adenine dinucleotide
-
Comamonas testosteroni
3-pyridinealdehyde adenine dinucleotide
-
Comamonas testosteroni
NAD+
-
Comamonas testosteroni
NADH
-
Comamonas testosteroni
thio-NAD+
-
Comamonas testosteroni