Activating Compound | Comment | Organism | Structure |
---|---|---|---|
aminooxyacetic acid | presence significantly stabilizes enzyme | Homo sapiens |
Application | Comment | Organism |
---|---|---|
medicine | primary hyperoxaluria type I is a severe kidney stone disease caused by mutations in the protein alanine:glyoxylate aminotransferase | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
human AGT can substitute for function of yeast Agx1 (yeast alanine:glyoxylate aminotransferase) and that mutations associated with disease in humans show reduced growth in yeast. The reduced growth of minor allele mutants reflects reduced protein levels, indicating that these proteins are less stable than wild-type AGT in yeast | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
F152I | natural mutation in enzyme minor allele, decreased activity | Homo sapiens |
G170R | natural mutation in enzyme minor allele, 40-57% of the activity of major allele, in vitro | Homo sapiens |
I244T | natural mutation in enzyme minor allele, 8-26% of the activity of major allele, in vitro | Homo sapiens |
additional information | human enzyme can substitute for function of yeast Agx1. Mutations associated with disease in humans show reduced growth in yeast, refecting reduced protein levels | Homo sapiens |
R233C | natural mutation in enzyme major allele, 14% of the activity of wild-type tmajor allele, in vitro | Homo sapiens |
R233C | natural mutation in enzyme minor allele, no in vitro enzymic activity | Homo sapiens |
S158L | natural mutation in enzyme major allele, no in vitro enzymic activity | Homo sapiens |
S205P | natural mutation in enzyme major allele, decreased activity | Homo sapiens |
General Stability | Organism |
---|---|
human AGT can substitute for function of yeast Agx1 (Yeast alanine:glyoxylate aminotransferase) and that mutations associated with disease in humans show reduced growth in yeast. The reduced growth of minor allele mutants reflects reduced protein levels, indicating that these proteins are less stable than wild-type AGT in yeast | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Homo sapiens | - |
patients with primary hyperoxaluria type I | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-alanine + glyoxylate | - |
Homo sapiens | pyruvate + glycine | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the two allelic forms consist of a wild-type major allele, AGTma, and a minor allele, AGTmi. Wild-type minor allele displays about 46-50% of the activity of the major allele | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
AGT | - |
Homo sapiens |
alanine:glyoxylate aminotransferase | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | presence significantly stabilizes enzyme | Homo sapiens |