Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Moore, W.; Wiener, H.L.; Meister, A.
    Inactivation of gamma-glutamylcysteine synthetase, but not of glutamine synthetase, by S-sulfocysteine and S-sulfohomocysteine (1987), J. Biol. Chem., 262, 16771-16777.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.2 DL-2-Amino-4-phosphonobutanoate
-
 Rattus norvegicus
6.3.2.2 L-Homocysteate
-
 Rattus norvegicus
6.3.2.2 L-Homocysteine sulfinate
-
 Rattus norvegicus
6.3.2.2 S-sulfocysteine D-enantiomer and L-enantiomer, ATP is not required for inactivation, noncovalent binding of close to 1 mol of inactivator per mol of enzyme, competitive with respect to L-Glu, complete protection with L-gamma-glutamyl-L-2-aminobutanoate, L-Glu + ATP, and ADP Rattus norvegicus
6.3.2.2 S-sulfohomocysteine D-enantiomer and L-enantiomer, ATP is not required for inactivation, noncovalent binding of close to 1 mol of inactivator per mol of enzyme, mixed-type inhibition Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.2 0.3
-
 L-Cys
-
 Rattus norvegicus
6.3.2.2 1.6
-
 L-Glu
-
 Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.2 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.2.2 kidney
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.2 ATP + L-Glu + L-Cys
-
 Rattus norvegicus ADP + phosphate + gamma-L-Glu-L-Cys
-
 ?