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Literature summary for 6.3.5.5 extracted from

  • Eroglu, B.; Powers-Lee, S.G.
    Unmasking a functional allosteric domain in an allosterically nonresponsive carbamoyl-phosphate synthetase (2002), J. Biol. Chem., 277, 45466-45472.
    View publication on PubMed
Search for more literature for 6.3.5.5

Activating Compound

Activating Compound Comment Organism Structure
IMP allosteric effect on Escherichia coli enzyme in dependence of temperature, no response to chimeric enzyme Escherichia coli
IMP the nonresponsive enzyme can bind UMP at domain D and allosteric effect on chimeric enzyme Saccharomyces cerevisiae
L-ornithine allosteric effect on chimeric enzyme and Escherichia coli enzyme Escherichia coli
L-ornithine allosteric effect on chimeric enzyme, no effect on Saccharomyces cerevisae enzyme Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
Escherichia coli and chimeric enzyme are expressed in Escherichia coli L673 Escherichia coli
expression in Saccharomyces pombe Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
UMP effect on chimeric enzyme and Escherichia coli enzyme Escherichia coli
UMP the nonresponsive enzyme can bind UMP at domain D and allosteric effect on chimeric enzyme Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.361
-
 L-glutamine chimeric enzyme, in presence of ornithine and absence of UMP Escherichia coli
0.89
-
 L-glutamine Escherichia coli enzyme, in presence of ornithine and absence of UMP Escherichia coli
0.91
-
 L-glutamine Escherichia coli enzyme, in absence of ornithine and UMP Escherichia coli
1.075
-
 L-glutamine chimeric enzyme, in absence of ornithine and UMP Escherichia coli
1.49
-
 L-glutamine Escherichia coli enzyme, in absence of ornithine and presence of UMP Escherichia coli
1.86
-
 L-glutamine chimeric enzyme, in absence of ornithine and presence of UMP 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 the product carbamoyl phosphate is utilized for the arginine biosynthesis 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
2 ATP + L-Gln + HCO3- Saccharomyces cerevisiae the product carbamoyl phosphate is utilized for the arginine biosynthesis 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
2 ATP + L-Gln + HCO3- Saccharomyces cerevisiae LPL26 the product carbamoyl phosphate is utilized for the arginine biosynthesis 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 and construction of a chimeric enzyme, in which the C-terminal 136 residues of Escherichia coli enzyme are replaced by the corresponding residues of Saccharomyces cerevisiae enzyme
-
Saccharomyces cerevisiae
-
 construction of a chimeric enzyme, in which the C-terminal 136 residues of Escherichia coli enzyme are replaced by the corresponding residues of Saccharomyces cerevisae enzyme
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification construction of a chimeric enzyme, in which the C-terminal 136 residues of Escherichia coli enzyme are replaced by the corresponding residues of Saccharomyces cerevisae enzyme Escherichia coli
side-chain modification construction of a chimeric enzyme, in which the C-terminal 136 residues of Escherichia coli enzyme are replaced by the corresponding residues of Saccharomyces cerevisae enzyme Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae
Escherichia coli and chimeric enzyme Escherichia coli

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
-
 ?
2 ATP + L-Gln + HCO3-
-
 Saccharomyces cerevisiae 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
2 ATP + L-Gln + HCO3- the product carbamoyl phosphate is utilized for the arginine biosynthesis Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
2 ATP + L-Gln + HCO3- the product carbamoyl phosphate is utilized for the arginine biosynthesis Saccharomyces cerevisiae 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
2 ATP + L-Gln + HCO3-
-
 Saccharomyces cerevisiae LPL26 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
2 ATP + L-Gln + HCO3- the product carbamoyl phosphate is utilized for the arginine biosynthesis Saccharomyces cerevisiae LPL26 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
2 ATP + NH4+ + HCO3-
-
 Escherichia coli 2 ADP + phosphate + carbamoyl phosphate
-
 ?
2 ATP + NH4+ + HCO3-
-
 Saccharomyces cerevisiae 2 ADP + phosphate + carbamoyl phosphate
-
 ?
2 ATP + NH4+ + HCO3-
-
 Saccharomyces cerevisiae LPL26 2 ADP + phosphate + carbamoyl phosphate
-
 ?