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Literature summary 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)

EC Number Cloned (Comment) Organism
3.5.1.54 recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Pseudomonas syringae pv. tomato

Protein Variants

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.54 additional information the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC Pseudomonas syringae pv. tomato

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.54 additional information
-
 additional information Michaelis-Menten kinetics Saccharomyces cerevisiae
3.5.1.54 additional information
-
 additional information Michaelis-Menten kinetics Granulibacter bethesdensis
3.5.1.54 additional information
-
 additional information Michaelis-Menten kinetics Pseudomonas syringae pv. tomato
3.5.1.54 additional information
-
 additional information Michaelis-Menten kinetics Candida albicans
3.5.1.54 0.1
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, urea amidolyase Granulibacter bethesdensis
3.5.1.54 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
3.5.1.54 0.21
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, allophanate hydrolase Granulibacter bethesdensis
3.5.1.54 0.22
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, allophanate hydrolase Pseudomonas syringae pv. tomato
3.5.1.54 0.23
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, urea amidolyase Saccharomyces cerevisiae
3.5.1.54 0.23
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, urea amidolyase Candida albicans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.54 urea-1-carboxylate + H2O Saccharomyces cerevisiae
-
 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O Granulibacter bethesdensis
-
 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O Pseudomonas syringae pv. tomato
-
 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O Candida albicans
-
 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O Pseudomonas syringae pv. tomato DC3000
-
 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O Pseudomonas syringae pv. tomato ATCC BAA-871D-5
-
 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O Pseudomonas syringae pv. tomato ATCC BAA-871
-
 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O Candida albicans ATCC MYA-2876
-
 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O Granulibacter bethesdensis ATCC BAA-1260
-
 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O Saccharomyces cerevisiae ATCC 204508
-
 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O Granulibacter bethesdensis CGDN1H1
-
 2 CO2 + 2 NH3
-
 r

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.54 Candida albicans A0A1D8PDC6
-
-
3.5.1.54 Candida albicans ATCC MYA-2876 A0A1D8PDC6
-
-
3.5.1.54 Granulibacter bethesdensis Q0BRB0
-
-
3.5.1.54 Granulibacter bethesdensis ATCC BAA-1260 Q0BRB0
-
-
3.5.1.54 Granulibacter bethesdensis CGDN1H1 Q0BRB0
-
-
3.5.1.54 Pseudomonas syringae pv. tomato
-
-
-
3.5.1.54 Pseudomonas syringae pv. tomato ATCC BAA-871D-5
-
-
-
3.5.1.54 Pseudomonas syringae pv. tomato DC3000
-
-
-
3.5.1.54 Saccharomyces cerevisiae P32528
-
-
3.5.1.54 Saccharomyces cerevisiae ATCC 204508 P32528
-
-
6.3.4.6 Pseudomonas syringae pv. tomato
-
-
-
6.3.4.6 Pseudomonas syringae pv. tomato ATCC BAA-871
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.54 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.54 urea-1-carboxylate + H2O
-
 Saccharomyces cerevisiae 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O
-
 Granulibacter bethesdensis 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O
-
 Pseudomonas syringae pv. tomato 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O
-
 Candida albicans 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O
-
 Pseudomonas syringae pv. tomato DC3000 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O
-
 Pseudomonas syringae pv. tomato ATCC BAA-871D-5 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O
-
 Pseudomonas syringae pv. tomato ATCC BAA-871 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O
-
 Candida albicans ATCC MYA-2876 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O
-
 Granulibacter bethesdensis ATCC BAA-1260 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O
-
 Saccharomyces cerevisiae ATCC 204508 2 CO2 + 2 NH3
-
 r
3.5.1.54 urea-1-carboxylate + H2O
-
 Granulibacter bethesdensis CGDN1H1 2 CO2 + 2 NH3
-
 r

Synonyms

EC Number Synonyms Comment Organism
3.5.1.54 DUR1,2
-
 Saccharomyces cerevisiae
3.5.1.54 PsAH
-
 Pseudomonas syringae pv. tomato
3.5.1.54 UAL
-
 Saccharomyces cerevisiae
3.5.1.54 UAL
-
 Granulibacter bethesdensis
3.5.1.54 UAL
-
 Pseudomonas syringae pv. tomato
3.5.1.54 UAL
-
 Candida albicans
3.5.1.54 urea amidolyase
-
 Saccharomyces cerevisiae
3.5.1.54 urea amidolyase
-
 Granulibacter bethesdensis
3.5.1.54 urea amidolyase
-
 Pseudomonas syringae pv. tomato
3.5.1.54 urea amidolyase
-
 Candida albicans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.54 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
3.5.1.54 12
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, allophanate hydrolase Pseudomonas syringae pv. tomato
3.5.1.54 15
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, allophanate hydrolase Granulibacter bethesdensis
3.5.1.54 18
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, urea amidolyase Granulibacter bethesdensis
3.5.1.54 24
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, urea amidolyase Candida albicans
3.5.1.54 32
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, urea amidolyase Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.54 7.3
-
 assay at Saccharomyces cerevisiae
3.5.1.54 7.3
-
 assay at Granulibacter bethesdensis
3.5.1.54 7.3
-
 assay at Pseudomonas syringae pv. tomato
3.5.1.54 7.3
-
 assay at Candida albicans

General Information

EC Number General Information Comment Organism
3.5.1.54 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
3.5.1.54 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
3.5.1.54 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
3.5.1.54 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
3.5.1.54 malfunction the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC Pseudomonas syringae pv. tomato
3.5.1.54 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
3.5.1.54 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
3.5.1.54 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
3.5.1.54 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
3.5.1.54 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
3.5.1.54 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
3.5.1.54 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
3.5.1.54 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
6.3.4.6 physiological function urea amidolyase is comprised of two enzymatic components: urea carboxylase and allophanate hydrolase. There is no substrate channeling or interdomain/intersubunit communication between urea carboxylase and allophanate hydrolase. Neither stable nor transient interactions can be detected between urea carboxylase and allophanate hydrolase and the catalytic efficiencies are independent of one another. An artificial fusion of urea carboxylase and allophanate hydrolase does not significantly alter the allophanate hydrolase enzyme activity or catalytic efficiency Pseudomonas syringae pv. tomato

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.1.54 54.54
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, allophanate hydrolase Pseudomonas syringae pv. tomato
3.5.1.54 71.4
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, allophanate hydrolase Granulibacter bethesdensis
3.5.1.54 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
3.5.1.54 104.35
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, urea amidolyase Candida albicans
3.5.1.54 139.13
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, urea amidolyase Saccharomyces cerevisiae
3.5.1.54 180
-
 urea-1-carboxylate pH 7.3, temperature not specified in the publication, urea amidolyase Granulibacter bethesdensis