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Literature summary for 2.6.1.29 extracted from

  • Kim, K.H.
    Purification and properties of a diamine alpha-ketoglutarate transaminase from Escherichia coli (1964), J. Biol. Chem., 239, 783-786.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.88
-
2-oxoglutarate pH 7.6, room temperature Escherichia coli
2.7
-
pyruvate pH 7.6, room temperature Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
putrescine + 2-oxoglutarate Escherichia coli
-
4-aminobutanal + L-glutamate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
precipitation with ammonium sulphate followed by column chromatography Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [Āµmol/min/mg] Specific Activity Maximum [Āµmol/min/mg] Comment Organism
1.63
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,7-diaminoheptane + 2-oxoglutarate 30% of the activity with putrescine Escherichia coli 7-aminoheptanal + L-glutamate
-
?
4-aminobutanoate + 2-oxoglutarate 11% of the activity with putrescine Escherichia coli 4-oxobutanoate + L-glutamate
-
?
cadaverine + 2-oxoglutarate equally active as putrescine Escherichia coli 5-aminopentanal + L-glutamate
-
?
additional information inactive with oxaloacetate Escherichia coli ?
-
?
additional information inactive with 1,3-diaminopropane, lysine, ornithine, spermidine Escherichia coli ?
-
?
putrescine + 2-oxoglutarate
-
Escherichia coli 4-aminobutanal + L-glutamate
-
?
putrescine + pyruvate
-
Escherichia coli 4-aminobutanal + L-alanine
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 10
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
8 10.5 almost completely inactive at pH 7, pH 8 about 40% of maximum activity, pH 10.5 about 20% of maximum activity Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate required Escherichia coli