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Literature summary for 2.6.1.44 extracted from

  • Cellini, B.; Montioli, R.; Paiardini, A.; Lorenzetto, A.; Maset, F.; Bellini, T.; Oppici, E.; Voltattorni, C.B.
    Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I (2010), Proc. Natl. Acad. Sci. USA, 107, 2896-2901.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.44

Protein Variants

Protein Variants Comment Organism
G41R the mutation on the minor and major alleles causes hyperoxaluria type 1, the variant under physiological conditions forms insoluble inactive high-order aggregates through intermolecular electrostatic interactions, the mutation decreases resistance to thermal denaturation and inactivation Homo sapiens
G41V the mutation on the major alle causes hyperoxaluria type 1, the variant under physiological conditions forms insoluble inactive high-order aggregates through intermolecular electrostatic interactions, the mutation decreases resistance to thermal denaturation and inactivation Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42700
-
 about 42700 Da, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Homo sapiens