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Literature summary for 2.6.1.44 extracted from

  • Zhang, X.; Roe, S.M.; Pearl, L.H.; Danpure, C.J.
    Crystallization and preliminary crystallographic analysis of human alanine:glyoxylate aminotransferase and its polymorphic variants (2001), Acta Crystallogr. Sect. D, 57, 1936-1937.
    View publication on PubMed
Search for more literature for 2.6.1.44

Application

Application Comment Organism
medicine hereditary disease primary hyperoxaluria type 1 is caused by a deficiency of the liver-specific peroxisomal enzyme alanine:glyoxylate aminotransferase, diagnosis with selective inhibitors and enzyme assays Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
human AGT expressed in Escherichia coli B834(DE3) Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals belong to space group P4(1)2(1)2 or its enantiomorph with uni-cell parameters a = b = 90.81, c = 142.62 A Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
 2 * 43000, SDS-PAGE Homo sapiens
43000
-
 2 * 43000, homodimer Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-alanine + glyoxylate Homo sapiens
-
 pyruvate + glycine
-
 ir

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 human
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme 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
-
 ir

Subunits

Subunits Comment Organism
dimer 2 * 43000, SDS-PAGE Homo sapiens
dimer 2 * 43000, homodimer Homo sapiens

Cofactor

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