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Literature summary for 2.6.1.44 extracted from

  • Rodionov, R.N.; Murry, D.J.; Vaulman, S.F.; Stevens, J.W.; Lentz, S.R.
    Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide production (2010), J. Biol. Chem., 285, 5385-5391.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.44

Cloned(Commentary)

Cloned (Comment) Organism
expressed in COS-7 cells and human umbilical vein endothelial cells with a C-terminal FLAG epitope tag Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
 FLAG-tagged enzyme, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney expressed primarily in the kidney Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine + glyoxylate
-
 Homo sapiens pyruvate + glycine
-
 ?
additional information mitochondrially localized human AGXT2 is able to effectively metabolize asymmetric dimethylarginine in vivo Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
AGXT2
-
 Homo sapiens
alanine-glyoxylate aminotransferase 2
-
 Homo sapiens

Cofactor

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

General Information

General Information Comment Organism
physiological function overexpression of human AGXT2 protects from asymmetric dimethylarginine-induced inhibition in nitric oxide production Homo sapiens