Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Pseudomonas syringae pv. tomato |
Protein Variants | Comment | Organism |
---|---|---|
S179A | site-directed mutagenesis | Pseudomonas syringae pv. tomato |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC | Pseudomonas syringae pv. tomato |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Saccharomyces cerevisiae | |
additional information | - |
additional information | Michaelis-Menten kinetics | Granulibacter bethesdensis | |
additional information | - |
additional information | Michaelis-Menten kinetics | Pseudomonas syringae pv. tomato | |
additional information | - |
additional information | Michaelis-Menten kinetics | Candida albicans | |
0.1 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, urea amidolyase | Granulibacter bethesdensis | |
0.15 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, allophanate hydrolase with urea carboxylase in a 1:1 molar ratio | Pseudomonas syringae pv. tomato | |
0.21 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, allophanate hydrolase | Granulibacter bethesdensis | |
0.22 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, allophanate hydrolase | Pseudomonas syringae pv. tomato | |
0.23 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, urea amidolyase | Saccharomyces cerevisiae | |
0.23 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, urea amidolyase | Candida albicans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
urea-1-carboxylate + H2O | Saccharomyces cerevisiae | - |
2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | Granulibacter bethesdensis | - |
2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | Pseudomonas syringae pv. tomato | - |
2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | Candida albicans | - |
2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | Pseudomonas syringae pv. tomato DC3000 | - |
2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | Pseudomonas syringae pv. tomato ATCC BAA-871D-5 | - |
2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | Pseudomonas syringae pv. tomato ATCC BAA-871 | - |
2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | Candida albicans ATCC MYA-2876 | - |
2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | Granulibacter bethesdensis ATCC BAA-1260 | - |
2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | Saccharomyces cerevisiae ATCC 204508 | - |
2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | Granulibacter bethesdensis CGDN1H1 | - |
2 CO2 + 2 NH3 | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Candida albicans | A0A1D8PDC6 | - |
- |
Candida albicans ATCC MYA-2876 | A0A1D8PDC6 | - |
- |
Granulibacter bethesdensis | Q0BRB0 | - |
- |
Granulibacter bethesdensis ATCC BAA-1260 | Q0BRB0 | - |
- |
Granulibacter bethesdensis CGDN1H1 | Q0BRB0 | - |
- |
Pseudomonas syringae pv. tomato | - |
- |
- |
Pseudomonas syringae pv. tomato ATCC BAA-871D-5 | - |
- |
- |
Pseudomonas syringae pv. tomato DC3000 | - |
- |
- |
Saccharomyces cerevisiae | P32528 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | P32528 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, untagged PsAH does not copurify with His-tagged PsUC, nor does untagged PsUC co-purify with His-tagged PsAH | Pseudomonas syringae pv. tomato |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
urea-1-carboxylate + H2O | - |
Saccharomyces cerevisiae | 2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | - |
Granulibacter bethesdensis | 2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | - |
Pseudomonas syringae pv. tomato | 2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | - |
Candida albicans | 2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | - |
Pseudomonas syringae pv. tomato DC3000 | 2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | - |
Pseudomonas syringae pv. tomato ATCC BAA-871D-5 | 2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | - |
Pseudomonas syringae pv. tomato ATCC BAA-871 | 2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | - |
Candida albicans ATCC MYA-2876 | 2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | - |
Granulibacter bethesdensis ATCC BAA-1260 | 2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | 2 CO2 + 2 NH3 | - |
r | |
urea-1-carboxylate + H2O | - |
Granulibacter bethesdensis CGDN1H1 | 2 CO2 + 2 NH3 | - |
r |
Synonyms | Comment | Organism |
---|---|---|
DUR1,2 | - |
Saccharomyces cerevisiae |
PsAH | - |
Pseudomonas syringae pv. tomato |
UAL | - |
Saccharomyces cerevisiae |
UAL | - |
Granulibacter bethesdensis |
UAL | - |
Pseudomonas syringae pv. tomato |
UAL | - |
Candida albicans |
urea amidolyase | - |
Saccharomyces cerevisiae |
urea amidolyase | - |
Granulibacter bethesdensis |
urea amidolyase | - |
Pseudomonas syringae pv. tomato |
urea amidolyase | - |
Candida albicans |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
11 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, allophanate hydrolase with urea carboxylase in a 1:1 molar ratio | Pseudomonas syringae pv. tomato | |
12 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, allophanate hydrolase | Pseudomonas syringae pv. tomato | |
15 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, allophanate hydrolase | Granulibacter bethesdensis | |
18 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, urea amidolyase | Granulibacter bethesdensis | |
24 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, urea amidolyase | Candida albicans | |
32 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, urea amidolyase | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.3 | - |
assay at | Saccharomyces cerevisiae |
7.3 | - |
assay at | Granulibacter bethesdensis |
7.3 | - |
assay at | Pseudomonas syringae pv. tomato |
7.3 | - |
assay at | Candida albicans |
General Information | Comment | Organism |
---|---|---|
evolution | urea carboxylase (UC) and allophanate hydrolase (A) display a close evolutionary and functional association. The inter-domain coupling efficiency is low in both bacterial and yeast UAL | Saccharomyces cerevisiae |
evolution | urea carboxylase (UC) and allophanate hydrolase (A) display a close evolutionary and functional association. The inter-domain coupling efficiency is low in both bacterial and yeast UAL | Granulibacter bethesdensis |
evolution | urea carboxylase (UC) and allophanate hydrolase (A) display a close evolutionary and functional association. The inter-domain coupling efficiency is low in both bacterial and yeast UAL | Pseudomonas syringae pv. tomato |
evolution | urea carboxylase (UC) and allophanate hydrolase (A) display a close evolutionary and functional association. The inter-domain coupling efficiency is low in both bacterial and yeast UAL | Candida albicans |
malfunction | the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC | Pseudomonas syringae pv. tomato |
additional information | urea amidolyase (UAL) comprised of two enzymatic components: urea carboxylase (UC) and allophanate hydrolase. The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent. Allophanate is not directly channeled from PsUC to PsAH | Candida albicans |
additional information | urea amidolyase (UAL) comprises two enzymatic components: urea carboxylase (UC) and allophanate hydrolase. The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent. Allophanate is not directly channeled from PsUC to PsAH | Saccharomyces cerevisiae |
additional information | urea amidolyase (UAL) comprises two enzymatic components: urea carboxylase (UC) and allophanate hydrolase. The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent. Allophanate is not directly channeled from PsUC to PsAH | Granulibacter bethesdensis |
additional information | urea amidolyase (UAL) comprises two enzymatic components: urea carboxylase (UC) and allophanate hydrolase. The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent. PsAH and PsUC do not influence each other's enzyme activities. Allophanate is not directly channeled from PsUC to PsAH | Pseudomonas syringae pv. tomato |
physiological function | urea amidolyase (UAL) is a multifunctional biotin-dependent enzyme that contributes to both bacterial and fungal pathogenicity by catalyzing the ATP-dependent cleavage of urea into ammonia and CO2. Urea amidolyase is comprised of two enzymatic components: urea carboxylase (UC) and allophanate hydrolase (A) | Saccharomyces cerevisiae |
physiological function | urea amidolyase (UAL) is a multifunctional biotin-dependent enzyme that contributes to both bacterial and fungal pathogenicity by catalyzing the ATP-dependent cleavage of urea into ammonia and CO2. Urea amidolyase is comprised of two enzymatic components: urea carboxylase (UC) and allophanate hydrolase (A) | Granulibacter bethesdensis |
physiological function | urea amidolyase (UAL) is a multifunctional biotin-dependent enzyme that contributes to both bacterial and fungal pathogenicity by catalyzing the ATP-dependent cleavage of urea into ammonia and CO2. Urea amidolyase is comprised of two enzymatic components: urea carboxylase (UC) and allophanate hydrolase (A) | Pseudomonas syringae pv. tomato |
physiological function | urea amidolyase (UAL) is a multifunctional biotin-dependent enzyme that contributes to both bacterial and fungal pathogenicity by catalyzing the ATP-dependent cleavage of urea into ammonia and CO2. Urea amidolyase is comprised of two enzymatic components: urea carboxylase (UC) and allophanate hydrolase (A) | Candida albicans |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
54.54 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, allophanate hydrolase | Pseudomonas syringae pv. tomato | |
71.4 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, allophanate hydrolase | Granulibacter bethesdensis | |
73.3 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, allophanate hydrolase with urea carboxylase in a 1:1 molar ratio | Pseudomonas syringae pv. tomato | |
104.35 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, urea amidolyase | Candida albicans | |
139.13 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, urea amidolyase | Saccharomyces cerevisiae | |
180 | - |
urea-1-carboxylate | pH 7.3, temperature not specified in the publication, urea amidolyase | Granulibacter bethesdensis |