Biology:Alanine—glyoxylate transaminase

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alanine-glyoxylate transaminase
5luc.jpg
Alanine-glyoxylate transaminase dimer, Human
Identifiers
EC number2.6.1.44
CAS number9015-67-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, an alanine-glyoxylate transaminase (EC 2.6.1.44) is an enzyme that catalyzes the chemical reaction

L-alanine + glyoxylate [math]\displaystyle{ \rightleftharpoons }[/math] pyruvate + glycine

Thus, the two substrates of this enzyme are L-alanine and glyoxylate, whereas its two products are pyruvate and glycine.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-alanine:glyoxylate aminotransferase. Other names in common use include AGT, alanine-glyoxylate aminotransferase, alanine-glyoxylic aminotransferase, and L-alanine-glycine transaminase. This enzyme participates in alanine and aspartate metabolism and glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1H0C, 1J04, 1VJO, 2BKW, 2HUF, 2HUI, and 2HUU.

References