Alanine Glyoxylate Aminotransferase (AGXT)

AGT; AGT1; AGXT1; PH1; SPAT; SPT; TLH6; Oxalosis I; Hyperoxaluria I; Glycolicaciduria; Serine-Pyruvate Aminotransferase

SPN	U558
HGNC	341
MGI	1329033
PubMed	11562405
RGD	2073
UniProt	P21549
Wiki	AGXT

Serine--pyruvate aminotransferase is an enzyme expressed only in the liver and the protein is localized mostly in the peroxisomes, where it is involved in glyoxylate detoxification. Mutations in this gene, some of which alter subcellular targeting, have been associated with type I primary hyperoxaluria.The human peroxisomal AGT showed about 78% amino acid sequence identity with rat mitochondrial AGT. The putative pyridoxal phosphate-binding lysine residue at position 209 is conserved. A comparison of the 5-prime sequences indicated that the N-terminal 22 amino acids of the rat translation product are absent from the human protein. The loss of this mitochondrial targeting sequence (MTS) signal during evolution may partly explain the species differences in intracellular localization of AGT.

Reference

"Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase."
Eur. J. Biochem. 194:9-18(1990) [PubMed] [Europe PMC] [Abstract]

"Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1."
J. Cell Biol. 111:2341-2351(1990) [PubMed] [Europe PMC] [Abstract]

"Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon."
Biochem. J. 268:517-520(1990) [PubMed] [Europe PMC] [Abstract]

"Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase."
Genomics 10:34-42(1991) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1."
J. Mol. Biol. 331:643-652(2003) [PubMed] [Europe PMC] [Abstract]

"Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene."
Biochem. Biophys. Res. Commun. 176:1093-1099(1991) [PubMed] [Europe PMC] [Abstract]

"A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1."
Genomics 13:215-218(1992) [PubMed] [Europe PMC] [Abstract]

"A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1."
Hum. Mol. Genet. 1:643-644(1992) [PubMed] [Europe PMC] [Abstract]

"Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation."
Am. J. Hum. Genet. 53:417-432(1993) [PubMed] [Europe PMC] [Abstract]

"Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase."
Biochimie 75:309-315(1993) [PubMed] [Europe PMC] [Abstract]

"Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene."
J. Med. Genet. 34:489-492(1997) [PubMed] [Europe PMC] [Abstract]

"Identification of new mutations in primary hyperoxaluria type 1 (PH1)."
J. Nephrol. 11:15-17(1998) [PubMed] [Europe PMC] [Abstract]

"Gene symbol: AGXT. Disease: primary hyperoxaluria type I."
Hum. Genet. 104:441-441(1999) [PubMed] [Europe PMC] [Abstract]

"Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene."
Hum. Genet. 104:523-525(1999) [PubMed] [Europe PMC] [Abstract]

"Primary hyperoxaluria type I: a model for multiple mutations in a monogenic disease within a distinct ethnic group."
J. Am. Soc. Nephrol. 10:2352-2358(1999) [PubMed] [Europe PMC] [Abstract]

"Identification of 5 novel mutations in the AGXT gene."
Hum. Mutat. 15:577-577(2000) [PubMed] [Europe PMC] [Abstract]

"Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations."
J. Biol. Chem. 275:36415-36422(2000) [PubMed] [Europe PMC] [Abstract]

"The AGT gene in Africa: a distinctive minor allele haplotype, a polymorphism (V326I), and a novel PH1 mutation (A112D) in Black Africans."
Mol. Genet. Metab. 78:44-50(2003) [PubMed] [Europe PMC] [Abstract]

"Primary hyperoxaluria type 1 in the Canary Islands: a conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase."
Proc. Natl. Acad. Sci. U.S.A. 100:7277-7282(2003) [PubMed] [Europe PMC] [Abstract]

"Clinical implications of mutation analysis in primary hyperoxaluria type 1."
Kidney Int. 66:746-752(2004) [PubMed] [Europe PMC] [Abstract]

"Implications of genotype and enzyme phenotype in pyridoxine response of patients with type I primary hyperoxaluria."
Am. J. Nephrol. 25:183-188(2005) [PubMed] [Europe PMC] [Abstract]

"Intra-familial clinical heterogeneity: absence of genotype-phenotype correlation in primary hyperoxaluria type 1 in Israel."
Am. J. Nephrol. 25:269-275(2005) [PubMed] [Europe PMC] [Abstract]

"The major allele of the alanine:glyoxylate aminotransferase gene: nine novel mutations and polymorphisms associated with primary hyperoxaluria type 1."
Mol. Genet. Metab. 86:172-178(2005) [PubMed] [Europe PMC] [Abstract]