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Literature summary for 2.6.1.19 extracted from

  • Kim, D.W.; Yoon, C.S.; Eum, W.S.; Lee, B.R.; An, J.J.; Lee, S.H.; Lee, S.R.; Ahn, J.Y.; Kwon, O.S.; Kang, T.C.; Won, M.H.; Cho, S.W.; Lee, K.S.; Park, J.; Choi, S.Y.
    Site-directed mutagenesis of human brain GABA transaminase: lysine-357 is involved in cofactor binding at the active site (2004), Mol. Cells, 18, 314-319.
    View publication on PubMed
Search for more literature for 2.6.1.19

Protein Variants

Protein Variants Comment Organism
K357A no enzymic activity, even not by addition of exogenous pyridoxal 5’-phosphate Homo sapiens
K357B no enzymic activity, even not by addition of exogenous pyridoxal 5’-phosphate Homo sapiens
K357N no enzymic activity, even not by addition of exogenous pyridoxal 5’-phosphate Homo sapiens
K357Q no enzymic activity, even not by addition of exogenous pyridoxal 5’-phosphate Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 x * 50000, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
apoenzyme reconstituted with exogenous pyridoxal 5’-phosphate almost completely regains catalytic activity Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
17.5
-
 pH 8.4, 25°C Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-aminobutanoate + 2-oxoglutarate
-
 Homo sapiens 4-oxobutanoate + L-glutamate
-
 ?

Subunits

Subunits Comment Organism
? x * 50000, SDS-PAGE Homo sapiens

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate K357 is involved in binding Homo sapiens