Alanine-glyoxylate transaminase (AGXT) catalyzes the irreversible reaction of glyoxylate and alanine to form glycine and pyruvate (Danpure and Jennings 1988). The active form of the enzyme is a homodimer (Zhang et al. 2003) with one molecule of pyridoxal phosphate bound to each subunit (Coulter-Mackie et al. 2005). Mutations in this enzyme are associated with primary hyperoxaluria type I. Mutant alleles encode both catalytically inactive proteins and active ones that are mis-localized to mitochondria (Purdue et al. 1990; Takada et al. 1990).
Roe, SM, Bartlam, M, Pearl, LH, Danpure, CJ, Rao, Z, Zhang, X, Hou, Y
Takada, Y, Kaneko, N, Danpure, CJ, Purdue, PE, Esumi, H
Lian, Q, Coulter-Mackie, MB, Wong, SG
Takada, Y, Danpure, CJ, Purdue, PE
Jennings, PR, Danpure, CJ
alanine-glyoxylate transaminase activity of AGXT dimer [peroxisomal matrix]
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