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Literature summary 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

General Stability

EC Number General Stability Organism
2.6.1.30 K+ stabilizes Pseudomonas sp.

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.30 Pseudomonas sp.
-
-
-

Storage Stability

EC Number Storage Stability Organism
2.6.1.30 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)

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.30 37
-
assay at Pseudomonas sp.