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Literature summary for 2.6.1.44 extracted from

  • Hopper, E.D.; Pittman, A.M.; Fitzgerald, M.C.; Tucker, C.L.
    In vivo and in vitro examination of stability of primary hyperoxaluria-associated human alanine:glyoxylate aminotransferase (2008), J. Biol. Chem., 283, 30493-30502.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
aminooxyacetic acid presence significantly stabilizes enzyme Homo sapiens

Application

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(Commentary)

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

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

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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Homo sapiens
-
patients with primary hyperoxaluria type I
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine + glyoxylate
-
Homo sapiens pyruvate + glycine
-
?

Subunits

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

Synonyms Comment Organism
AGT
-
Homo sapiens
alanine:glyoxylate aminotransferase
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate presence significantly stabilizes enzyme Homo sapiens