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Literature summary for 2.6.1.44 extracted from

  • Lumb, M.J.; Danpure, C.J.
    Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations (2000), J. Biol. Chem., 275, 36415-36422.
    View publication on PubMed

Application

Application Comment Organism
medicine
-
Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
cloned and expressed in Escherichia coli JM109 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.23
-
glyoxylate pH 8.0, 37°C, recombinant His-AGT, L-alanine as amino donor Homo sapiens
0.39
-
glyoxylate pH 8.0, 37°C, recombinant AGT-His, L-alanine as amino donor Homo sapiens
9.1
-
L-alanine pH 8.0, 37°C, recombinant His-AGT, glyoxylate as amino acceptor Homo sapiens
9.4
-
L-alanine pH 8.0, 37°C, recombinant AGT-His, glyoxylate as amino acceptor Homo sapiens

Localization

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

Molecular Weight [Da]

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

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
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
51.8
-
purified recombinant enzyme Homo sapiens

Subunits

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8.5 recombinant enzyme Homo sapiens