EC Number   |
General Information |
Reference |
|---|
    2.6.1.44 | evolution |
AGT is a homodimer and belongs to the fold type I family of PLP-dependent enzymes. Enzyme AGT is present in the human population in two allelic forms, the major allele encoding AGT-Ma and the minor allele encoding AGT-Mi, the latter characterized by the Pro11 to Leu and Ile340 to Met amino acid substitutions |
759584 |
| 2.6.1.44 | evolution |
AGT is homodimeric and belongs to the fold type I family of PLP-dependent enzymes |
758763 |
| 2.6.1.44 | evolution |
aminotransferase enzymes function via a bimolecular double displacement ping-pong mechanism where an amino acid usually serves as the amino donor and an alpha-keto acid serves as the amino acceptor. Aminotransferases are ubiquitous in the three domains of life and are involved in a variety of metabolic pathways including amino acid metabolism, nitrogen assimilation, gluconeogenesis, responses to a number of biotic/abiotic stresses, and among other pathways. The aminotransferase gene family in the model plant Arabidopsis thaliana consists of 44 genes, eight of which are suggested to be alanine aminotransferases. One of the putative alanine aminotransferases genes, At3g08860, is attributed the function of alanine:glyoxylate aminotransferase/beta-alanine:pyruvate aminotransferase based on the analysis of gene expression networks and homology to other beta-alanine aminotransferases in plants |
759951 |
| 2.6.1.44 | evolution |
enzyme AGT is present in the human population in two allelic forms, the major allele encoding AGT-Ma and the minor allele encoding AGT-Mi, the latter characterized by the Pro11 to Leu and Ile340 to Met amino acid substitutions |
758860, 759779 |
| 2.6.1.44 | malfunction |
alanine:glyoxylate aminotransferase deficiency causes primary hyperoxaluria type 1 |
704634 |
| 2.6.1.44 | malfunction |
causes the hereditary kidney stone disease primary hyperoxaluria type 1 |
722393 |
| 2.6.1.44 | malfunction |
critical role of AGXT deletion during HCC progression, loss of AGXT expression is correlated with a poor prognosis and differentiation of HCC. Loss of AGXT expression promotes the malignant phenotypes of HCC cell lines |
759686 |
| 2.6.1.44 | malfunction |
deficiency is responsible for Primary Hyperoxaluria Type 1, an autosomal recessive disorder |
721718 |
| 2.6.1.44 | malfunction |
deficit of AGT causes primary hyperoxaluria type I (PH1) (OMIM 259900), a rare metabolic recessive disease due to inborn errors affecting the metabolism of glyoxylate in liver peroxisomes. Molecular dynamics simulations of F152I-Mi and I244T-Mi variants associated with PH1 and implications in their pathogenicity |
758860 |
| 2.6.1.44 | malfunction |
deficit of AGT leads to primary hyperoxaluria type I (PH1), a rare disease characterized by calcium oxalate stones deposition in the urinary tract as a consequence of glyoxylate accumulation. Most missense mutations cause AGT misfolding, as in the case of the G41R, which induces aggregation and proteolytic degradation |
758763 |
