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Literature summary for 3.5.1.54 extracted from

  • Lin, Y.; Boese, C.; St. Maurice, M.
    The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent (2016), Protein Sci., 25, 1812-1824 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Protein Variants Comment Organism
S179A site-directed mutagenesis Pseudomonas syringae pv. tomato

Inhibitors

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 [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/ Products (Substrates)

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

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 (Commentary)

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 and Products (Substrate)

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

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 [1/s]

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

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

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 [mM/s]

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