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Literature summary for 2.6.1.44 extracted from

  • Montioli, R.; Fargue, S.; Lewin, J.; Zamparelli, C.; Danpure, C.J.; Borri Voltattorni, C.; Cellini, B.
    The N-terminal extension is essential for the formation of the active dimeric structure of liver peroxisomal alanine:glyoxylate aminotransferase (2012), Int. J. Biochem. Cell Biol., 44, 536-546.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
His-tagged protein expressed in Escherichia coli JM109, expressed in CHO cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
DELTA 1-21 purified protein does not show bound PLP (affinity is about 80fold lower than wild type protein), catalytic activity about 1000fold lower than wild type protein, expressed in Escherichia coli in an insoluble form, peroxisomal localization, expressed in CHO cells the mutant protein forms large stable but catalytically inactive aggregates in the peroxisomes Homo sapiens
P10L/P11L Kcat value 56% of wild type protein, aggregation occuring at a slower rate than that of DELTA 1-21 protein Homo sapiens

Localization

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine + glyoxylate
-
Homo sapiens pyruvate + glycine
-
?

Subunits

Subunits Comment Organism
homodimer gel filtration Homo sapiens

Synonyms

Synonyms Comment Organism
alanine:glyoxylate aminotransferase
-
Homo sapiens

Cofactor

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

General Information

General Information Comment Organism
malfunction causes the hereditary kidney stone disease primary hyperoxaluria type 1 Homo sapiens