Recombinant Human Serine--pyruvate aminotransferase (AGXT)

1. Mutations at the dimer interface of alanine-glyoxylate aminotransferase alter enzyme structure/activity, leading to primary hyperoxaluria type I and determine the cellular response to vitamin B6. PMID: 29110180
2. two novel AGXT missense mutations (p.M49L and p.N72I), which will enrich the AGXT mutation database and provide a better comprehension of PH1 pathogenesis, were identified in a big Chinese PH1 family. Significant morphological and structural difference of kidney stones from two siblings with the same genotype observed in this study displays the heterogeneity of genotype-phenotype correlation PMID: 27644547
3. AGXT mutational analysis was performed to confirm the diagnosis of PH1. PMID: 28161266
4. this study identifies a novel AGXT gene mutation in primary hyperoxaluria after kidney transplantation failure in Tunisian patient PMID: 27568336
5. AGXT gene sequencing is now the choice of diagnosis of Primary hyperoxaluria type 1 (PH1)due to its non-invasive nature compared to liver enzyme assay. Early diagnosis and accurate treatment in PH1 is important for better patient outcomes. PMID: 27915025
6. Caenorhabditis elegans AGXT-1 is a mitochondrial and temperature-adapted ortholog of peroxisomal human AGT1. PMID: 27179589
7. Novel AGXT mutations in a Tunisian population with primary hyperoxaluria type 1. PMID: 27935012
8. The novel p.Gln137Hisfs*19 AGXT mutation detected in this study extends the spectrum of known primary hyperoxaluria type I AGXT gene mutations in Tunisia. PMID: 27659337
9. Data show that onomeric minor allele of human alanine glyoxylate aminotransferase (AGT-Mi) binds pyridoxal 5-phosphate (PLP) but does not display catalytic activity. PMID: 27720751
10. Letter/Case Report: novel missense AGXT gene mutation in a Sri Lankan family with primary hyperoxaluria type 1. PMID: 26693850
11. Primary hyperoxaluria type 1 (PH1) is due to a defect in the AGXT gene. The aim of our study was to analyze the mutations causing PH1 in the Moroccan population PMID: 26383609
12. In conclusion, this study of an unprecedented number of primary hyperoxaluria type 1 patients showed geno-phenotype associations that have not been previously reported. PMID: 24988064
13. The pathogenic mutation G47R causes misfolding of alanine:glyoxylate aminotransferase. PMID: 26149463
14. A review of the current knowledge of the biochemical properties of liver peroxisomal alanine:glyoxylate aminotransferase and of the molecular defects caused by single point mutations associated with Primary Hyperoxaluria Type 1. PMID: 25620715
15. S81L and G170R mutations of AGT is associated with Primary Hyperoxaluria type I in homozygosis and heterozygosis. PMID: 24990153
16. AGT missense mutations associated with Primary Hyperoxaluria Type 1, were characterized. PMID: 24718375
17. Data suggest that dequalinium chloride (DECA) may be a pharmacologic strategy to treat primary hyperoxaluria 1 (PH1) patients with mutations in alanine:glyoxylate aminotransferase (AGT). PMID: 25237136
18. These are the first cases of primary hyperoxaluria type 1 to be diagnosed by clinical manifestations and AGXT gene mutations in mainland China. PMID: 24934730
19. data imply that the AGT Pro11Leu polymorphism is not directly responsible for the low incidence of stone formation in black South Africans. PMID: 24344980
20. Modeling of the mutations on a 1.9 A crystal structure suggests that Primary hyperoxaluria type I causing mutants perturb locally the native structure of AGT. PMID: 24205397
21. The view presented has important implications for the development of new therapeutic strategies based on targeting specific elements of alanine-glyoxylate aminotransferase homeostasis PMID: 23956997
22. Gly161 mutations in alanine:glyoxylate aminotransferase is associated with Primary Hyperoxaluria Type I. PMID: 24055001
23. Solved is the X-ray crystal structure of the S187F variant of AGT to a resolution of 2.9 A. PMID: 23589421
24. Identification of a double mutation c.32C>T (Pro11Leu) and c.731T>C (p.Ile244Thr) in AGXT gene in five unrelated Tunisian families with primary hyperoxaluria type 1 disease. PMID: 24012869
25. Three novel mutations detected in the AGXT gene associated with primary hyperoxaluria type 1 in a Tunisian patient population. PMID: 23810941
26. Four of the most common mutations in primary hyperoxaluria type 1 unmask the cryptic mitochondrial targeting sequence of alanine:glyoxylate aminotransferase encoded by the polymorphic minor allele PMID: 23229545
27. The molecular mechanism of recognition by the peroxisomal receptor Pex5p, in complex with alanine-glyoxylate aminotransferase revealed by X-ray crystallography. PMID: 22529745
28. These results suggest that the N-terminal extension plays an essential role in allowing AGT to attain its correct conformation and functional activity. PMID: 22198249
29. A side-by-side comparison was performed between normal AGT and nine purified recombinant pathogenic variants in terms of catalytic activity, coenzyme binding mode and affinity, spectroscopic features, oligomerization, and thermal stability. PMID: 22018727
30. selected aspects of the biochemical properties of the two allelic forms of AGXT and of some primary hyperoxaluria type 1-causing variants (review) PMID: 22201765
31. Partially unfolded states of AGXT strongly interact with Hsc70 and Hsp90 chaperones. PMID: 21103899
32. Selected AGXT gene mutations analysis provides a genetic diagnosis in 28% of Tunisian patients with primary hyperoxaluria. PMID: 21612638
33. Data show that P11L mutation is responsible for the urea sensitivity of AGT-Mi. PMID: 20713123
34. mutation of the AGXT gene, showing the patient to be compound heterozygous for the c.33_34InsC and c.508G > A mutations PMID: 20020206
35. Genotype-phenotype correlation in primary hypoxaluria type 1: the p. Gly170Arg AGXT mutation is associated with a better outcome. PMID: 20016466
36. Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I. PMID: 20133649
37. investigated occurrence of Pro11Leu polymorphism in both herder & agriculturalist populations from Central Asia; findings show distribution of variation observed in the AGXT gene could be due to demographic history, rather than local adaptation to diet PMID: 20059472
38. crystal structure of AGT consists of an intimate dimer in which an extended N-terminal segment of 21 amino acids from one subunit wraps as an elongated irregular coil around the outside of the crystallographic symmetry-related subunit. PMID: 20208150
39. 3D picture of an in vivo early ATP-dependent step of the folding reaction cycle of the chaperonin and supports a GroEL functional model in which the chaperonin promotes folding of the AGXT-LTM mutant protein through forced unfolding mechanism PMID: 20056599
40. serine:pyruvate aminotransferase expression is regulated by Sp1, AP-2 and PKA PMID: 12169688
41. crystal structure of normal human AGT complexed to the competitive inhibitor amino-oxyacetic acid to 2.5A PMID: 12899834
42. Early detection of Gly170Arg and Phe152Ile mutations in PH1 has important clinical implications because of their association with pyridoxine responsiveness and clinical outcome PMID: 15253729
43. report describing 3 AGXT gene mutations in Chinese patients with primary hyperoxaluria type 1 PMID: 15365967
44. mutations with serious consequences in vivo may not be inherently catalytically inactive and may be rescuable PMID: 15802217
45. human AGT interacts with human Pex5p in mammalian cells, but not yeast cells; type 1 peroxisomal targeting sequence(PTS1)is located entirely within the smaller C-terminal structural domain of 110 amino acids PMID: 15911627
46. Determination of crystal structure of AGT has enabled effects of some of most important missense mutations in AGXT gene to be rationalised in terms of AGT folding, dimerization and stability. New possibilities for design of pharmacological agents. PMID: 15961951
47. Presentation and role of transplantation [kidney and/or liver] in adult patients with type 1 primary hyperoxaluria and the 1244T AGXT mutation in a university hospital in Spain are presented. PMID: 16912707
48. The effects of missense mutations on enzyme activity, dimerization, aggregation, and turnover were investigated. PMID: 16971151
49. expressed wild-type human AGT1 was predominantly localized in mouse hepatocellular peroxisomes, whereas the most common mutant form of AGT1 (G170R) was localized predominantly in the mitochondria PMID: 17110443
50. AGXT is even more variable than formerly believed in the diagnosis of primary hyperoxaluria PMID: 17460142

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HGNC: 341

OMIM: 259900

KEGG: hsa:189

STRING: 9606.ENSP00000302620

UniGene: Hs.144567