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Literature summary for 2.6.1.30 extracted from

  • Gilmer, P.J.; McIntire, W.S.; Kirsch, J.F.
    Pyridoxamine-pyruvate transaminase. 1. Determination of the active site stoichiometry and the pH dependence of the dissociation constant for 5-deoxypyridoxal (1977), Biochemistry, 16, 5241-5246.
    View publication on PubMed
Search for more literature for 2.6.1.30

General Stability

General Stability Organism
K+ stabilizes Pseudomonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics Pseudomonas sp.

Metals/Ions

Metals/Ions Comment Organism Structure
K+ activates Pseudomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas sp. enzyme is part of the degradative pathway for vitamin B6 compounds utilized by Pseudomonas sp. MA-1 ?
-
 ?
pyridoxamine + pyruvate Pseudomonas sp.
-
 pyridoxal + L-alanine
-
 r

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Storage Stability

Storage Stability Organism
loss of activity within 12 h at 25°C in sodium phosphate buffer, but is stable in potassium buffer under the same conditions Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information determination of the active site stoichiometry and the pH dependence of the dissociation constant for 5'-deoxypyridoxal Pseudomonas sp. ?
-
 ?
additional information enzyme is part of the degradative pathway for vitamin B6 compounds utilized by Pseudomonas sp. MA-1 Pseudomonas sp. ?
-
 ?
pyridoxamine + pyruvate
-
 Pseudomonas sp. pyridoxal + L-alanine
-
 r

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Pseudomonas sp.