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Literature summary extracted from

  • Cellini, B.; Bertoldi, M.; Montioli, R.; Paiardini, A.; Borri Voltattorni, C.
    Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications (2007), Biochem. J., 408, 39-50.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.44 expression in Escherichia coli Homo sapiens
2.6.1.44 wild-type and G82E mutant His-tagged enzyme expressed in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.44 G82E natural enzyme variant. Significant reduction in affinty for pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate. Mutant displays an altered conformational state of the bound pyridoxal 5'-phosphate and a decrease in overall catlytic activity to 0.1% of wild-type Homo sapiens
2.6.1.44 G82E naturally occuring variant. Like the wild-type, the G82E variant is able to bind 2 mol pyridoxal 5'-phosphate/dimer, it exhibits a significant reduced affinity for pyridoxal 5'-phosphate and even more for pyridoxamine 5'-phosphate compared with wild-type, and an altered conformational state of the bound pyridoxal 5'-phosphate. Dramatic decrease of the overall catalytic activity (about 0.1% of that of normal alanine:glyoxylate aminotransferase), appears to be related to the inability to undergo an efficient transaldimination of the pyridoxal 5'-phosphate form of the enzyme with amino acids as well as an efficient conversion of AGT-pyridoxamine 5'-phosphate into AGT-pyridoxal 5'-phosphate Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.44 D-alanine competitive inhibitor with L-alanine as varied substrate and glyoxylate as fixed substrate. Uncompetitive inhibitor with glyoxylate as varied substrate and L-alanine as fixed substrate; competitive with L-alanine, uncompetitive with glyoxylate Homo sapiens
2.6.1.44 pyruvate mixed type inhibition with L-alanine, competitive with glyoxylate; mixed type inhibitor with L-alanine as varied substrate and glyoxylate as fixed substrate. Competitive inhibitor with glyoxylate as varied substrate and L-alanine as fixed substrate Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.44 0.15
-
 glyoxylate mutant G82E, 25°C Homo sapiens
2.6.1.44 0.15
-
 glyoxylate pH 7.4, 25°C, mutant enzyme G82E Homo sapiens
2.6.1.44 0.21
-
 pyruvate pH 7.4, 25°C, wild-type enzyme Homo sapiens
2.6.1.44 0.21
-
 pyruvate wild-type, 25°C Homo sapiens
2.6.1.44 0.23
-
 glyoxylate pH 7.4, 25°C, wild-type enzyme Homo sapiens
2.6.1.44 0.23
-
 glyoxylate wild-type, 25°C Homo sapiens
2.6.1.44 15
-
 L-alanine mutant G82E, 25°C Homo sapiens
2.6.1.44 15
-
 L-alanine pH 7.4, 25°C, mutant enzyme G82E Homo sapiens
2.6.1.44 22
-
 glycine pH 7.4, 25°C, wild-type enzyme Homo sapiens
2.6.1.44 22
-
 glycine wild-type, 25°C Homo sapiens
2.6.1.44 31
-
 L-alanine pH 7.4, 25°C, wild-type enzyme Homo sapiens
2.6.1.44 31
-
 L-alanine wild-type, 25°C Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.44 L-alanine + glyoxylate Homo sapiens the enzyme is highly specific for catalysing glyoxylate to glycine processing, thereby playing a key role in glyoxylate detoxification pyruvate + glycine
-
 ?
2.6.1.44 additional information Homo sapiens enzyme is highly specific for catalyzing glyoxylate to glycine processing, playing a key role in glyoxylate detoxification ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.44 Homo sapiens
-
-
-
2.6.1.44 Homo sapiens A2V838
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.44 recombinant wild-type and G82E mutant His-tagged enzyme Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
2.6.1.44 L-alanine + glyoxylate = pyruvate + glycine pyridoxamine 5'-phosphate remains bound to the enzyme during the catalytic cycle. The enzyme-pyridoxamine 5'-phosphate complex displays a reactivity towards oxo acids higher than that of the apo-enzyme in presence of pyridoxamine Homo sapiens
a

Storage Stability

EC Number Storage Stability Organism
2.6.1.44 -20°C, wild-type and mutant enzyme G82E are stable for at least 1 month Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.44 glycine + pyruvate
-
 Homo sapiens L-alanine + glyoxylate
-
 ?
2.6.1.44 L-alanine + glyoxylate the enzyme is highly specific for catalysing glyoxylate to glycine processing, thereby playing a key role in glyoxylate detoxification Homo sapiens pyruvate + glycine
-
 ?
2.6.1.44 L-alanine + glyoxylate the enzyme is highly specific for catalysing glyoxylate to glycine processing Homo sapiens pyruvate + glycine
-
 ?
2.6.1.44 L-alanine + glyoxylate transamination half-reaction kinetic parameters Homo sapiens glycine + pyruvate
-
 r
2.6.1.44 L-arginine + pyruvate
-
 Homo sapiens 5-guanidino-2-oxopentanoate + L-alanine
-
 ?
2.6.1.44 L-asparagine + glyoxylate
-
 Homo sapiens 4-amino-2,4-dioxobutanoate + glycine
-
 ?
2.6.1.44 L-glutamate + glyoxylate
-
 Homo sapiens 2-oxoglutarate + glycine
-
 ?
2.6.1.44 L-phenylalanine + glyoxylate
-
 Homo sapiens phenylpyruvate + glycine
-
 ?
2.6.1.44 L-serine + glyoxylate
-
 Homo sapiens 3-hydroxy-2-oxopropanoate + glycine
-
 ?
2.6.1.44 additional information enzyme is highly specific for catalyzing glyoxylate to glycine processing, playing a key role in glyoxylate detoxification Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.6.1.44 AGT
-
 Homo sapiens
2.6.1.44 alanine:glyoxylate aminotransferase
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.44 0.068
-
 glyoxylate mutant G82E, 25°C Homo sapiens
2.6.1.44 0.068
-
 glyoxylate pH 7.4, 25°C, mutant enzyme G82E Homo sapiens
2.6.1.44 0.07
-
 L-alanine mutant G82E, 25°C Homo sapiens
2.6.1.44 0.07
-
 L-alanine pH 7.4, 25°C, mutant enzyme G82E Homo sapiens
2.6.1.44 0.33
-
 glycine pH 7.4, 25°C, wild-type enzyme Homo sapiens
2.6.1.44 0.33
-
 glycine wild-type, 25°C Homo sapiens
2.6.1.44 0.36
-
 pyruvate pH 7.4, 25°C, wild-type enzyme Homo sapiens
2.6.1.44 0.36
-
 pyruvate wild-type, 25°C Homo sapiens
2.6.1.44 45
-
 glyoxylate pH 7.4, 25°C, wild-type enzyme Homo sapiens
2.6.1.44 45
-
 L-alanine pH 7.4, 25°C, wild-type enzyme Homo sapiens
2.6.1.44 45
-
 glyoxylate wild-type, 25°C Homo sapiens
2.6.1.44 45
-
 L-alanine wild-type, 25°C Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.44 pyridoxal 5'-phosphate like the wild-type, the G82E variant is able to bind 2 mol pyridoxal 5'-phosphate/dimer, it exhibits a significant reduced affinity for pyridoxal 5'-phosphate and even more for pyridoxamine 5'-phosphate compared with wild-type, and an altered conformational state of the bound pyridoxal 5'-phosphate Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.6.1.44 2.3
-
 pyruvate glyoxylate as varied substrate and L-alanine as fixed substrate Homo sapiens
2.6.1.44 14.3
-
 D-alanine with L-alanine as varied substrate and glyoxylate as fixed substrate, Kis Homo sapiens
2.6.1.44 15.8
-
 pyruvate with L-alanine as varied substrate and glyoxylate as fixed substrate, Kis Homo sapiens
2.6.1.44 22.8
-
 pyruvate with L-alanine as varied substrate and glyoxylate as fixed substrate, Kii Homo sapiens
2.6.1.44 28.7
-
 D-alanine with glyoxylate as varied substrate and L-alanine as fixed substrate, Kii Homo sapiens