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Literature summary for 3.5.1.2 extracted from

  • Snodgrass, P.J.; Lund, P.
    Allosteric properties of phosphate-activated glutaminase of human liver mitochondria (1984), Biochim. Biophys. Acta, 798, 21-27.
    View publication on PubMed
Search for more literature for 3.5.1.2

Activating Compound

Activating Compound Comment Organism Structure
NH4+ activates Homo sapiens
phosphate activates Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
glutamate no inhibition Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1
-
 Gln in presence of 100 mM phosphate Homo sapiens

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-Gln + H2O Homo sapiens enzyme plays a key role in urea synthesis by regulating provision of glutamate for synthesis of N-acetylglutamate, the obligatory cofactor of carbamoylphosphate synthetase L-Glu + NH3
-
 ?

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.
Gln + H2O
-
 Homo sapiens Glu + NH3
-
 ?
L-Gln + H2O enzyme plays a key role in urea synthesis by regulating provision of glutamate for synthesis of N-acetylglutamate, the obligatory cofactor of carbamoylphosphate synthetase Homo sapiens L-Glu + NH3
-
 ?