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Literature summary for 6.3.5.5 extracted from

  • Fang, H.; Liu, H.; Chen, N.; Zhang, C.; Xie, X.; Xu, Q.
    Site-directed mutagenesis studies on the uridine monophosphate binding sites of feedback inhibition in carbamoyl phosphate synthetase and effects on cytidine production by Bacillus amyloliquefaciens (2013), Can. J. Microbiol., 59, 374-379.
    View publication on PubMed
Search for more literature for 6.3.5.5

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 (DE3) cells Bacillus amyloliquefaciens

Protein Variants

Protein Variants Comment Organism
K986I the substrate kinetics (Km for L-glutamine) increases nearly 1.3fold compared to the wild type enzyme Bacillus amyloliquefaciens
T941F the substrate kinetics (Km for L-glutamine) increases nearly 1.2fold compared to the wild type enzyme Bacillus amyloliquefaciens
T941F/K986I the substrate kinetics (Km for L-glutamine) increases nearly 1.96fold compared to the wild type enzyme Bacillus amyloliquefaciens
T941F/T970A/K986I the substrate kinetics (Km for L-glutamine) increases nearly 2.17fold compared to the wild type enzyme Bacillus amyloliquefaciens
T970A the substrate kinetics (Km for L-glutamine) increases nearly 1.1fold compared to the wild type enzyme Bacillus amyloliquefaciens

Inhibitors

Inhibitors Comment Organism Structure
UMP
-
 Bacillus amyloliquefaciens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.23
-
 L-glutamine wild type enzyme, in 50 mM HEPES (pH 7.5), at 37°C Bacillus amyloliquefaciens
0.26
-
 L-glutamine mutant enzyme T970A, in 50 mM HEPES (pH 7.5), at 37°C Bacillus amyloliquefaciens
0.28
-
 L-glutamine mutant enzyme T941F, in 50 mM HEPES (pH 7.5), at 37°C Bacillus amyloliquefaciens
0.3
-
 L-glutamine mutant enzyme K986I, in 50 mM HEPES (pH 7.5), at 37°C Bacillus amyloliquefaciens
0.45
-
 L-glutamine mutant enzyme T941F/K986I, in 50 mM HEPES (pH 7.5), at 37°C Bacillus amyloliquefaciens
0.5
-
 L-glutamine mutant enzyme T941F/T970A/K986I, in 50 mM HEPE (pH 7.5), at 37°C Bacillus amyloliquefaciens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 2 * 40000, SDS-PAGE Bacillus amyloliquefaciens
120000
-
 gel filtration Bacillus amyloliquefaciens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamine + HCO3- + H2O Bacillus amyloliquefaciens
-
 ADP + phosphate + L-glutamate + carbamoyl phosphate
-
 ?
ATP + L-glutamine + HCO3- + H2O Bacillus amyloliquefaciens CYT1
-
 ADP + phosphate + L-glutamate + carbamoyl phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
-
-
-
Bacillus amyloliquefaciens CYT1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-charged HisTrap column column chromatography Bacillus amyloliquefaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamine + HCO3- + H2O
-
 Bacillus amyloliquefaciens ADP + phosphate + L-glutamate + carbamoyl phosphate
-
 ?
ATP + L-glutamine + HCO3- + H2O
-
 Bacillus amyloliquefaciens CYT1 ADP + phosphate + L-glutamate + carbamoyl phosphate
-
 ?

Subunits

Subunits Comment Organism
homotrimer 2 * 40000, SDS-PAGE Bacillus amyloliquefaciens

Synonyms

Synonyms Comment Organism
carbamoyl phosphate synthetase
-
 Bacillus amyloliquefaciens
CPS
-
 Bacillus amyloliquefaciens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Bacillus amyloliquefaciens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.004
-
 wild type enzyme, in 50 mM HEPES (pH 7.5), at 37°C Bacillus amyloliquefaciens UMP
0.0907
-
 mutant enzyme T941F, in 50 mM HEPES (pH 7.5), at 37°C Bacillus amyloliquefaciens UMP
0.1504
-
 mutant enzyme T970A, in 50 mM HEPES (pH 7.5), at 37°C Bacillus amyloliquefaciens UMP
0.2
-
 mutant enzyme K986I, in 50 mM HEPES (pH 7.5), at 37°C Bacillus amyloliquefaciens UMP