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2.6.1.44 |
Description |
Alanine--glyoxylate aminotransferase |
Alternative names |
L-alanine-glyoxylate transaminase;
L-alanine-glycine transaminase;
AGT;
AGXT;
serine-glyoxylate aminotransferase (ambiguous);
3-hydroxykynurenine transaminase (ambiguous);
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Catalyzed reaction |
L-alanine + glyoxylate = pyruvate + glycine. |
Cofactor |
Pyridoxal-phosphate. |
Comments |
-!- With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyzes the reaction of EC 2.6.1.51. |
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The eukariotic sequences included in family a are close homologs of alanine:glyoxylate aminotransferase 1 from rat liver organelles, which in turn is identical to serine-pyruvate aminotransferase (2.6.1.51) and asparagine-oxo-acid aminotransferase (2.6.1.14)[Noguchi & Fujiwara (1988) JBC 263, 182].
The so-called alanine:glyoxylate aminotransferase 2 (AGXT2) from rat liver appears to be identical to (D)-3-amino-2-methylpropanoate aminotransferase (2.6.1.40) and aminolevulinate aminotransferase (2.6.1.43). Sequences of AGXT2 close homologs (which are very different from those in family a) are listed under 2.6.1.40.
The archaeal sequences included in family b are not closely related to the eukariotic enzymes with alanine-glyoxylate aminotransferase activity. |
Diseases |
Primary hyperoxaluria type 1 |
Prosite |
PROSITE; PS00600; |
PDB |
1H0C; 2YOB; 3ZRR; 2ZC0; |
Organisms |
-Eubacteria -Archea -Plants -Fungi -Metazoa -Human |
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Links |
Enzyme (activities) 2.6.1.44
BRENDA (activities) 2.6.1.44
KEGG (pathways) 2.6.1.44
PLPMDB (PLP mutants) 2.6.1.44
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References |
Articles on 2.6.1.44 |
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last changed |
2019/09/19 12:23 |
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