Literature summary for 2.6.1.44 extracted from

Coulter-Mackie, M.B.; Lian, Q.; Wong, S.G.
Overexpression of human alanine:glyoxylate aminotransferase in Escherichia coli: renaturation from guanidine-HCl and affinity for pyridoxal phosphate co-factor (2005), Protein Expr. Purif., 41, 18-26.

Search for more literature for 2.6.1.44

Protein Variants

Protein Variants	Comment	Organism
G170R	mutation associated with primary hyperoxaluria type I, no effect on affinity for pyridoxal 5-phosphate	Homo sapiens
G41R	mutation associated with primary hyperoxaluria type I, enhanced activity after re-folding	Homo sapiens
G41V	mutation associated with primary hyperoxaluria type I, enhanced activity after re-folding	Homo sapiens
I340M	polymorphism associated with enzyme from minor allele, significantly higher Km-value than that for major allele, 90% of activity of enzyme from major allele	Homo sapiens
P11L	50% of activity of enzyme from major allele	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
peroxisome	-	Homo sapiens	5777	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	overexpression in Escherichia coli	-

Renatured (Commentary)

Renatured (Comment)	Organism
denaturation of enzyme with guanidine-HCl and re-folding, complete renaturation. Mutations G41V and G41R, associated with primary hyperoxaluria type I, show enhanced activity after re-folding. Pyridoxal 5-phosphate is not required for proper re-folding	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Homo sapiens	-

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Homo sapiens

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Release 2023.1 (January 2023)