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

BRENDA support

Literature summary for 6.3.5.5 extracted from

  • Rishavy, M.A.; Cleland, W.W.; Lusty, C.J.
    15N isotope effects in glutamine hydrolysis catalyzed by carbamyl phosphate synthetase: evidence for a tetrahedral intermediate in the mechanism (2000), Biochemistry, 39, 7309-7315.
    View publication on PubMed
Search for more literature for 6.3.5.5

Protein Variants

Protein Variants Comment Organism
E841K comparison of 15N-isotope effects in mutant and wild-type enzyme on the hydrolysis of glutamine, the rate of glutamine hydrolysis in the mutant is not affected by MgATP2 and HCO3-, with the wild-type enzyme in the absence of MgATP2 and HCO3- the isotope effect id reduced Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.15
-
 L-glutamine pH 7.6, 37°C, L-glutamine hydrolysis Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ATP + L-Gln + HCO3- Escherichia coli
-
 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ir

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2 ATP + L-glutamine + hydrogencarbonate + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate An ordered uni bi mechanism for glutamine hydrolysis that is consistent with the isotope effects and with the catalytic properties of the enzyme is proposed Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ATP + L-Gln + HCO3-
-
 Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ir

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2
-
 wild-type enzyme Escherichia coli
6.6
-
 mutant enzyme E841K Escherichia coli
9.3
-
 wild-type enzyme Escherichia coli