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allophanate + H2O
2 CO2 + 2 NH3
allophanate + H2O
CO2 + NH3
allophanate + H2O
NH3 + CO2
malonamic acid + hydroxylamine
malonohydroxamate + ?
hydroxylamine trapping activity
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
additional information
?
-
allophanate + H2O
2 CO2 + 2 NH3
-
-
-
?
allophanate + H2O
2 CO2 + 2 NH3
the enzyme exhibits high specificity for allophanate
-
-
?
allophanate + H2O
2 CO2 + 2 NH3
-
-
-
?
allophanate + H2O
2 CO2 + 2 NH3
the enzyme exhibits high specificity for allophanate
-
-
?
allophanate + H2O
2 CO2 + 2 NH3
-
-
-
?
allophanate + H2O
2 CO2 + 2 NH3
-
-
-
ir
allophanate + H2O
2 CO2 + 2 NH3
the reverse reaction is catalyzed by urea carboxylase
-
-
ir
allophanate + H2O
2 CO2 + 2 NH3
the N-terminal domain of allophanate hydrolase deaminates allophanate to produce ammonia and N-carboxycarbamate, while the smaller C-terminal domain seems not to be required for cataytic activity, overview
-
-
?
allophanate + H2O
CO2 + NH3
-
-
-
-
ir
allophanate + H2O
CO2 + NH3
-
2nd step in the degradation of urea
-
-
ir
allophanate + H2O
CO2 + NH3
-
-
-
ir
allophanate + H2O
CO2 + NH3
-
-
-
ir
allophanate + H2O
CO2 + NH3
-
2nd step in the degradation of urea
-
ir
allophanate + H2O
CO2 + NH3
-
2nd step in the degradation of urea
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
-
ir
allophanate + H2O
NH3 + CO2
-
the enzyme is involved in bacterial cyanuric acid metabolism
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
-
ir
allophanate + H2O
NH3 + CO2
-
the enzyme is involved in bacterial cyanuric acid metabolism
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
?
allophanate + H2O
NH3 + CO2
-
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
-
ir
allophanate + H2O
NH3 + CO2
the enzyme is involved in bacterial cyanuric acid metabolism
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
ir
allophanate + H2O
NH3 + CO2
the enzyme is involved in bacterial cyanuric acid metabolism
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
?, ir
allophanate + H2O
NH3 + CO2
-
-
-
-
ir
allophanate + H2O
NH3 + CO2
-
the enzyme is involved in bacterial cyanuric acid metabolism
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
-
ir
allophanate + H2O
NH3 + CO2
-
the enzyme is involved in bacterial cyanuric acid metabolism
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
-
ir
allophanate + H2O
NH3 + CO2
-
the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
-
ir
allophanate + H2O
NH3 + CO2
-
the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
?
allophanate + H2O
NH3 + CO2
-
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
-
ir
allophanate + H2O
NH3 + CO2
the enzyme is involved in bacterial cyanuric acid metabolism
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
-
ir
allophanate + H2O
NH3 + CO2
-
the enzyme is involved in bacterial cyanuric acid metabolism
-
-
ir
allophanate + H2O
NH3 + CO2
-
-
-
-
ir
allophanate + H2O
NH3 + CO2
-
the enzyme is involved in bacterial cyanuric acid metabolism
-
-
ir
biuret + H2O
?
-
-
-
?
malonamic acid + H2O
?
-
-
-
?
malonamic acid + H2O
?
-
-
-
?
malonamic acid + H2O
?
-
-
-
?
malonamide + H2O
?
-
-
-
?
malonamide + H2O
?
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
r
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
r
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
r
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
r
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
r
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
?
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
-
r
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
-
r
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
-
r
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
-
r
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
r
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
-
-
-
r
additional information
?
-
binding process of allophanate to allophanate hydrolase, computational analysis, enzyme-substrate interaction, overview
-
-
?
additional information
?
-
binding process of allophanate to allophanate hydrolase, computational analysis, enzyme-substrate interaction, overview
-
-
?
additional information
?
-
binding process of allophanate to allophanate hydrolase, computational analysis, enzyme-substrate interaction, overview
-
-
?
additional information
?
-
allophanate is produced at the active site of the UC C-terminal domain and is translocated to that of the AH N-domain for subsequent reaction. Allophanate is translocated from the active site of UC C-terminal domain to that of the AH N-domain via diffusion through solvent, instead of being channeled through the dimer
-
-
?
additional information
?
-
allophanate is produced at the active site of the UC C-terminal domain and is translocated to that of the AH N-domain for subsequent reaction. Allophanate is translocated from the active site of UC C-terminal domain to that of the AH N-domain via diffusion through solvent, instead of being channeled through the dimer
-
-
?
additional information
?
-
allophanate is produced at the active site of the UC C-terminal domain and is translocated to that of the AH N-domain for subsequent reaction. Allophanate is translocated from the active site of UC C-terminal domain to that of the AH N-domain via diffusion through solvent, instead of being channeled through the dimer
-
-
?
additional information
?
-
allophanate is produced at the active site of the UC C-terminal domain and is translocated to that of the AH N-domain for subsequent reaction. Allophanate is translocated from the active site of UC C-terminal domain to that of the AH N-domain via diffusion through solvent, instead of being channeled through the dimer
-
-
?
additional information
?
-
allophanate is produced at the active site of the UC C-terminal domain and is translocated to that of the AH N-domain for subsequent reaction. Allophanate is translocated from the active site of UC C-terminal domain to that of the AH N-domain via diffusion through solvent, instead of being channeled through the dimer
-
-
?
additional information
?
-
allophanate is produced at the active site of the UC C-terminal domain and is translocated to that of the AH N-domain for subsequent reaction. Allophanate is translocated from the active site of UC C-terminal domain to that of the AH N-domain via diffusion through solvent, instead of being channeled through the dimer
-
-
?
additional information
?
-
allophanate is produced at the active site of the UC C-terminal domain and is translocated to that of the AH N-domain for subsequent reaction. Allophanate is translocated from the active site of UC C-terminal domain to that of the AH N-domain via diffusion through solvent, instead of being channeled through the dimer
-
-
?
additional information
?
-
allophanate also shows nonenzymatic decomposition, half-life at pH 8.0 is 50 h
-
-
?
additional information
?
-
substrate specificity, no activity with methyl allophanate, hydantoic acid, oxamic acid, hydroxyurea, methyl carbamate, N-methylurea, acetylurea, 1-acetyl-2-thiourea, and semicarbazide, no activity with rhodanine, rhodanine-3-acetic acid, 3-aminorhodanine, (4R)-(-)-2-thioxo-4-thiazolidinecarboxylic acid, (-)-2-oxo-4-thiazolinecarboxylic acid, and 2-amino-5-bromothiazol
-
-
?
additional information
?
-
-
substrate specificity, no activity with methyl allophanate, hydantoic acid, oxamic acid, hydroxyurea, methyl carbamate, N-methylurea, acetylurea, 1-acetyl-2-thiourea, and semicarbazide, no activity with rhodanine, rhodanine-3-acetic acid, 3-aminorhodanine, (4R)-(-)-2-thioxo-4-thiazolidinecarboxylic acid, (-)-2-oxo-4-thiazolinecarboxylic acid, and 2-amino-5-bromothiazol
-
-
?
additional information
?
-
the catalytic reaction is catalyzed by either the full-length AtzF or the amidase domain of AtzF, AtzF467. There is no catalytic advantage conferred by the C terminus of AtzF in vitro
-
-
?
additional information
?
-
-
the catalytic reaction is catalyzed by either the full-length AtzF or the amidase domain of AtzF, AtzF467. There is no catalytic advantage conferred by the C terminus of AtzF in vitro
-
-
?
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evolution
allophanate hydrolase is a member of the amidase family of enzymes that possess a conserved serine- and glycine-rich motif, the so-called amidase signature sequence
evolution
the enzyme belongs to the amidase signature family, which is characterized by a conserved block of 130 amino acids rich in Gly and Ser and a Ser-cisSer-Lys catalytic triad
evolution
the positions of the amino acids essential for catalysis (Ser165, Ser189, and Lys91) and substrate binding (Tyr320 and Arg328), are highly conserved
evolution
allophanate hydrolase (AH) is a member of the AS family
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
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
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
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
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
-
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
-
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
-
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
-
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
-
evolution
-
allophanate hydrolase (AH) is a member of the AS family
-
evolution
-
the enzyme belongs to the amidase signature family, which is characterized by a conserved block of 130 amino acids rich in Gly and Ser and a Ser-cisSer-Lys catalytic triad
-
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
-
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
-
evolution
-
allophanate hydrolase (AH) is a member of the AS family
-
malfunction
-
the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC
malfunction
-
the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC
-
malfunction
-
the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC
-
malfunction
-
the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC
-
metabolism
allophanate hydrolase also participates in the cyanuric acid mineralization pathway, in which the cyanuric acid ring is hydrolytically opened by cyanuric acid hydrolase (AtzD or TrzD, EC 3.5.2.15) forming the unstable metabolite carboxybiuret, which spontaneously decarboxylates to form biuret. Allophanate is produced from biuret by AtzE (biuret hydrolase; EC 3.5.1.84) via a single deamination. Hydrolysis of allophanate is then carried out by allophanate hydrolase. Both pathways, cyanuric acid mineralization pathway and urea carboxylase pathway, depend upon allophanate deamination by allophanate hydrolase to avoid spontaneous decarboxylation (and urea formation)
metabolism
allophanate hydrolase catalyzes the hydrolysis of allophanate, an intermediate in atrazine degradation and urea catabolism pathways, to NH3 and CO2
metabolism
urea amidolyase catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source
metabolism
-
urea amidolyase catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source
-
metabolism
-
urea amidolyase catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source
-
metabolism
-
urea amidolyase catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source
-
metabolism
-
urea amidolyase catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source
-
metabolism
-
allophanate hydrolase catalyzes the hydrolysis of allophanate, an intermediate in atrazine degradation and urea catabolism pathways, to NH3 and CO2
-
metabolism
-
urea amidolyase catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source
-
metabolism
-
urea amidolyase catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source
-
physiological function
allophanate hydrolase is essential for urea utilization. The enzyme also has important functions in the eukaryotic pyrimidine nucleic acid precursor degradation pathway, the yeast-hypha transition that several pathogens utilize to escape the host defense, and an s-triazine herbicide degradation pathway in soil bacteria
physiological function
allophanate hydrolase catalyzes the hydrolysis reaction of allophanate, an intermediate in Atrazine degradation and urea catabolism pathways, to produce ammonia and carbon dioxide
physiological function
the activity of the allophanate hydrolase from Pseudomonas sp. strain ADP, AtzF, provides the final hydrolytic step for the mineralization of s-triazines, such as atrazine and cyanuric acid. The action of AtzF provides metabolic access to two of the three nitrogens in each triazine ring
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)
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)
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)
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)
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)
-
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)
-
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)
-
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)
-
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)
-
physiological function
-
allophanate hydrolase catalyzes the hydrolysis reaction of allophanate, an intermediate in Atrazine degradation and urea catabolism pathways, to produce ammonia and carbon dioxide
-
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)
-
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)
-
physiological function
-
allophanate hydrolase catalyzes the hydrolysis reaction of allophanate, an intermediate in Atrazine degradation and urea catabolism pathways, to produce ammonia and carbon dioxide
-
additional information
the enzyme's N and C domains catalyze sequential reactions, overview
additional information
-
the enzyme's N and C domains catalyze sequential reactions, overview
additional information
the N-terminal amidase domain of the enzyme reveals that it is highly homologous to allophanate hydrolases involved in a different catabolic process in other organisms (i.e., the mineralization of urea), structure analysis, overview. The smaller C-terminal domain does not appear to have a physiologically relevant catalytic function. AtzF forms a large, ca. 660-kDa, multienzyme complex with AtzD and AtzE that is capable of mineralizing cyanuric acid. The function of this complex may be to channel substrates from one active site to the next, effectively protecting unstable metabolites, such as allophanate, from solvent-mediated decarboxylation to a dead-end metabolic product. The positions of the amino acids essential for catalysis (Ser165, Ser189, and Lys91) and substrate binding (Tyr320 and Arg328), are highly conserved
additional information
Tyr299 and Arg307 seem to serve to anchor and orient the substrate for attack by the catalytic nucleophile, Ser172, nucleophilic attack by serine results in a covalent tetrahedral intermediate that is stabilized by an oxyanion hole. After displacement of ammonia, the covalent intermediate is hydrolyzed to release the product. The unique C-terminal domain is conserved, but it does not contribute to catalysis or to the structural integrity of the core domain, suggesting that it may play a role in mediating transient and specific interactions with the urea carboxylase component of urea amidolyase. Active site architecture and structure-function analysis, overview
additional information
-
Tyr299 and Arg307 seem to serve to anchor and orient the substrate for attack by the catalytic nucleophile, Ser172, nucleophilic attack by serine results in a covalent tetrahedral intermediate that is stabilized by an oxyanion hole. After displacement of ammonia, the covalent intermediate is hydrolyzed to release the product. The unique C-terminal domain is conserved, but it does not contribute to catalysis or to the structural integrity of the core domain, suggesting that it may play a role in mediating transient and specific interactions with the urea carboxylase component of urea amidolyase. Active site architecture and structure-function analysis, overview
additional information
binding process of allophanate to allophanate hydrolase, computational analysis using the three-dimensional structure of AH, PDB ID 4GYS, quantum chemistry calculations and molecular dynamics simulation, overview. The optimal enzyme-substrate complex conformation demonstrates that along with Arg307 and Tyr299, Gly124 is also one of the key anchor residues in the stable complex. The energetic calculation suggests the existence of an intermediate state in the enzyme-substrate binding process. The further atomic-level investigation illuminates that Tyr299, Arg307 and Ser172 can stabilize the substrate in the intermediate state. By this token, the residues Arg307 and Tyr299 function in both binding process and getting stable state. Active site structure with docked allophanate, overview
additional information
structure analysis of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex, overview. AtzF forms a large, about 660-kDa, multienzyme complex with cyanuric acid amidohydrolase AtzD and biuret amidohydrolase AtzE that is capable of mineralizing cyanuric acid. The function of this complex may be to channel substrates from one active site to the next, effectively protecting unstable metabolites, such as allophanate, from solvent-mediated decarboxylation to a dead-end metabolic product. There is no catalytic advantage conferred by the C terminus of AtzF in vitro
additional information
-
structure analysis of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex, overview. AtzF forms a large, about 660-kDa, multienzyme complex with cyanuric acid amidohydrolase AtzD and biuret amidohydrolase AtzE that is capable of mineralizing cyanuric acid. The function of this complex may be to channel substrates from one active site to the next, effectively protecting unstable metabolites, such as allophanate, from solvent-mediated decarboxylation to a dead-end metabolic product. There is no catalytic advantage conferred by the C terminus of AtzF in vitro
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
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
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
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
additional information
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. UC converts urea to allophanate, and AH subsequently converts it to ammonium. The AH domain is composed of N- and C-domains, which catalyze sequential reactions in the allophanate to ammonium conversion
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. UC converts urea to allophanate, and AH subsequently converts it to ammonium. The AH domain is composed of N- and C-domains, which catalyze sequential reactions in the allophanate to ammonium conversion
-
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. UC converts urea to allophanate, and AH subsequently converts it to ammonium. The AH domain is composed of N- and C-domains, which catalyze sequential reactions in the allophanate to ammonium conversion
-
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
-
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
-
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
-
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
-
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. UC converts urea to allophanate, and AH subsequently converts it to ammonium. The AH domain is composed of N- and C-domains, which catalyze sequential reactions in the allophanate to ammonium conversion
-
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. UC converts urea to allophanate, and AH subsequently converts it to ammonium. The AH domain is composed of N- and C-domains, which catalyze sequential reactions in the allophanate to ammonium conversion
-
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
-
additional information
-
binding process of allophanate to allophanate hydrolase, computational analysis using the three-dimensional structure of AH, PDB ID 4GYS, quantum chemistry calculations and molecular dynamics simulation, overview. The optimal enzyme-substrate complex conformation demonstrates that along with Arg307 and Tyr299, Gly124 is also one of the key anchor residues in the stable complex. The energetic calculation suggests the existence of an intermediate state in the enzyme-substrate binding process. The further atomic-level investigation illuminates that Tyr299, Arg307 and Ser172 can stabilize the substrate in the intermediate state. By this token, the residues Arg307 and Tyr299 function in both binding process and getting stable state. Active site structure with docked allophanate, overview
-
additional information
-
Tyr299 and Arg307 seem to serve to anchor and orient the substrate for attack by the catalytic nucleophile, Ser172, nucleophilic attack by serine results in a covalent tetrahedral intermediate that is stabilized by an oxyanion hole. After displacement of ammonia, the covalent intermediate is hydrolyzed to release the product. The unique C-terminal domain is conserved, but it does not contribute to catalysis or to the structural integrity of the core domain, suggesting that it may play a role in mediating transient and specific interactions with the urea carboxylase component of urea amidolyase. Active site architecture and structure-function analysis, overview
-
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
-
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
-
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. UC converts urea to allophanate, and AH subsequently converts it to ammonium. The AH domain is composed of N- and C-domains, which catalyze sequential reactions in the allophanate to ammonium conversion
-
additional information
-
binding process of allophanate to allophanate hydrolase, computational analysis using the three-dimensional structure of AH, PDB ID 4GYS, quantum chemistry calculations and molecular dynamics simulation, overview. The optimal enzyme-substrate complex conformation demonstrates that along with Arg307 and Tyr299, Gly124 is also one of the key anchor residues in the stable complex. The energetic calculation suggests the existence of an intermediate state in the enzyme-substrate binding process. The further atomic-level investigation illuminates that Tyr299, Arg307 and Ser172 can stabilize the substrate in the intermediate state. By this token, the residues Arg307 and Tyr299 function in both binding process and getting stable state. Active site structure with docked allophanate, overview
-
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. UC converts urea to allophanate, and AH subsequently converts it to ammonium. The AH domain is composed of N- and C-domains, which catalyze sequential reactions in the allophanate to ammonium conversion
-
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homohexamer
6 * 50000, recombinant enzyme, SDS-PAGE
homotetramer
the full-length wild-type enzyme is a homotetramer in solution, small-angle X-ray scattering
tetramer
4 * 66223, sequence calculation
?
x * 65000, about, recombinant His8-tagged enzyme, SDS-PAGE
?
-
x * 65000, about, recombinant His8-tagged enzyme, SDS-PAGE
-
dimer
2 * 68000, His-tagged recombinant enzyme, SDS-PAGE, 2 * 65401, sequence calculation
dimer
-
2 * 68000, His-tagged recombinant enzyme, SDS-PAGE, 2 * 65401, sequence calculation
-
dimer
enzyme domain architecture, overview. Both the N- and the C-domains require dimerization for their optimal activities
dimer
-
2 * 61999, sequence calculation
dimer
-
2 * 61999, sequence calculation
-
dimer
C-terminally truncated enzyme mutant, AtzF467, small-angle X-ray scattering
dimer
N-terminal enzyme amidase domain AtzF467
homodimer
2 * 190000, recombinant enzyme, SDS-PAGE
homodimer
-
2 * 190000, recombinant enzyme, SDS-PAGE
-
homodimer
-
2 * 190000, recombinant enzyme, SDS-PAGE
-
homodimer
-
2 * 190000, recombinant enzyme, SDS-PAGE
-
homodimer
-
2 * 190000, recombinant enzyme, SDS-PAGE
-
homodimer
-
2 * 190000, recombinant enzyme, SDS-PAGE
-
homodimer
-
2 * 190000, recombinant enzyme, SDS-PAGE
-
additional information
analysis of interactions between the KlUA monomers
additional information
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. KlUC and KlAH are monomeric and dimeric in solution, respectively. The relatively smaller UC-AH interface therefore does not play a major role in the UA holo-enzyme assembly. In the isolated KlAH, the active sites are located near the dimer interface. The extensive interactions at the dimer interface most likely stabilize the structure of the active sites. Consistent with this, the G559E/G572E mutation that renders the isolated KlAH monomeric severely inhibited its activity
additional information
-
analysis of interactions between the KlUA monomers
-
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. KlUC and KlAH are monomeric and dimeric in solution, respectively. The relatively smaller UC-AH interface therefore does not play a major role in the UA holo-enzyme assembly. In the isolated KlAH, the active sites are located near the dimer interface. The extensive interactions at the dimer interface most likely stabilize the structure of the active sites. Consistent with this, the G559E/G572E mutation that renders the isolated KlAH monomeric severely inhibited its activity
-
additional information
-
analysis of interactions between the KlUA monomers
-
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. KlUC and KlAH are monomeric and dimeric in solution, respectively. The relatively smaller UC-AH interface therefore does not play a major role in the UA holo-enzyme assembly. In the isolated KlAH, the active sites are located near the dimer interface. The extensive interactions at the dimer interface most likely stabilize the structure of the active sites. Consistent with this, the G559E/G572E mutation that renders the isolated KlAH monomeric severely inhibited its activity
-
additional information
-
analysis of interactions between the KlUA monomers
-
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. KlUC and KlAH are monomeric and dimeric in solution, respectively. The relatively smaller UC-AH interface therefore does not play a major role in the UA holo-enzyme assembly. In the isolated KlAH, the active sites are located near the dimer interface. The extensive interactions at the dimer interface most likely stabilize the structure of the active sites. Consistent with this, the G559E/G572E mutation that renders the isolated KlAH monomeric severely inhibited its activity
-
additional information
-
analysis of interactions between the KlUA monomers
-
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. KlUC and KlAH are monomeric and dimeric in solution, respectively. The relatively smaller UC-AH interface therefore does not play a major role in the UA holo-enzyme assembly. In the isolated KlAH, the active sites are located near the dimer interface. The extensive interactions at the dimer interface most likely stabilize the structure of the active sites. Consistent with this, the G559E/G572E mutation that renders the isolated KlAH monomeric severely inhibited its activity
-
additional information
-
analysis of interactions between the KlUA monomers
-
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. KlUC and KlAH are monomeric and dimeric in solution, respectively. The relatively smaller UC-AH interface therefore does not play a major role in the UA holo-enzyme assembly. In the isolated KlAH, the active sites are located near the dimer interface. The extensive interactions at the dimer interface most likely stabilize the structure of the active sites. Consistent with this, the G559E/G572E mutation that renders the isolated KlAH monomeric severely inhibited its activity
-
additional information
-
analysis of interactions between the KlUA monomers
-
additional information
-
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. KlUC and KlAH are monomeric and dimeric in solution, respectively. The relatively smaller UC-AH interface therefore does not play a major role in the UA holo-enzyme assembly. In the isolated KlAH, the active sites are located near the dimer interface. The extensive interactions at the dimer interface most likely stabilize the structure of the active sites. Consistent with this, the G559E/G572E mutation that renders the isolated KlAH monomeric severely inhibited its activity
-
additional information
AtzF has two main domains: the catalytic domain and a second all-alpha-helical domain that forms the dimer interface. The C-terminal domain has a function in coordinating the quaternary structure of the enzyme. AtzF forms a large, ca. 660-kDa, multienzyme complex with AtzD and AtzE that is capable of mineralizing cyanuric acid
additional information
structure analysis of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex, overview. AtzF forms a large, ca. 660-kDa, multienzyme complex with cyanuric acid amidohydrolase AtzD and biuret amidohydrolase AtzE. Analysis of the multimerization of AtzF and Atzf467 by small-angle x-ray scattering (SAXS)
additional information
-
structure analysis of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex, overview. AtzF forms a large, ca. 660-kDa, multienzyme complex with cyanuric acid amidohydrolase AtzD and biuret amidohydrolase AtzE. Analysis of the multimerization of AtzF and Atzf467 by small-angle x-ray scattering (SAXS)
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purified enzyme free or in complex with the substrate analog malonate, hanging-drop vapor diffusion method, mixing of 4 mg/ml protein in 10 mM HEPES, pH 8.0, 50 mM NaCl, and 1 mM DTT, with reservoir solution in a 1:1 ratio to a final volume of 0.005 ml, the latter containing 100 mM PIPES, pH 6.5, and 1.04 M sodium malonate, room temperature, 2 months, followed by microseeding, 5-15 days, X-ray diffraction structure determination and analysis at 2.2-2.8 A resolution, molecular replacement
three-dimensional structure analysis using PDB ID 4GYS
purified recombinant His-tagged enzyme, sitting drop vapor diffusion method, mixing of protein in 0.5 mM urea, 0.5 mM ADP, and 0.5 mM sodium malonate, pH 7.0, with reservoir solution containing 0.1 M Tris/HCl, pH 7.5, 0.2 M ammonium sulfate, 12% PEG 8000, and 2% PEG 3350, X-ray diffraction structure determination and analysis at 6.5 A resolution, modelling by molecular replacement method using the structures of KlUC (PDB 3VA7) and KlAH (PDB 4ISS) as search models
purified recombinant wild-type and mutant His-tagged SeMet-substituted enzymes, sitting drop vapour diffusion method, mixing of 10 mg/ml protein in 20 mM Tris/HCl, pH 7.5, 200 mM NaCl, 2-10 mM DTT, with reservoir containing 16% PEG 8000, 20% glycerol, and 0.04 M potassium phosphate, and 100 mM sodium/potassium tartrate, 20°C, X-ray diffraction structure determination and analysis at 2.5-2.6 A resolution, molecular replacement
purified full-length wild-type enzyme and truncated mutant enzyme, trypsin-treated AtzF (in situ proteolysis) from 1 M ammonium sulfate, 1 M lithium sulfate, 0.1 M Tris-HCl, pH 8.5, AtzF467 crystals grown from 20% w/v PEG 6000, 0.1 M Na MES pH 6.5, 0.2 M calcium chloride, are used in microseeding for truncated AtzF crystal growth from 11% w/v PEG 3350, 2% Tacsimate, pH 5.0, X-ray diffraction structure determination and analysis at 2.5 A resolution
purified recombinant wild-type and mutant enzymes, from a reservoir containing 11 to 14% w/v PEG 3350 and 2% Tacsimate reagent, pH 5.0, at 20°C, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement
purified recombinant amidase domain of allophanate hydrolase, AtzF467, X-ray diffraction structure determinations and analysis at 2.5 A resolution
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R307A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R307M
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y299A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y299A/R307A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y299A/R307M
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y299F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y299F/R307A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y299F/R307M
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R307A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
R307M
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
Y299A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
Y299A/R307M
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
Y299F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
G559E/G572E
-
site-directed mutagenesis, the mutant shows abolished activity
-
S177A
-
site-directed mutagenesis, the mutation inactivates the isolated KlAH
-
G559E/G572E
-
site-directed mutagenesis, the mutant shows abolished activity
-
S177A
-
site-directed mutagenesis, the mutation inactivates the isolated KlAH
-
G559E/G572E
-
site-directed mutagenesis, the mutant shows abolished activity
-
S177A
-
site-directed mutagenesis, the mutation inactivates the isolated KlAH
-
G559E/G572E
-
site-directed mutagenesis, the mutant shows abolished activity
-
S177A
-
site-directed mutagenesis, the mutation inactivates the isolated KlAH
-
G559E/G572E
-
site-directed mutagenesis, the mutant shows abolished activity
-
S177A
-
site-directed mutagenesis, the mutation inactivates the isolated KlAH
-
G559E/G572E
-
site-directed mutagenesis, the mutant shows abolished activity
-
S177A
-
site-directed mutagenesis, the mutation inactivates the isolated KlAH
-
H488A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme below pH 8.0, but slightly reduced activity above pH 8.0
K91A
site-directed mutagenesis, inactive mutant
S165A
site-directed mutagenesis, inactive mutant
S189A
site-directed mutagenesis, inactive mutant
H488A
site-directed mutagenesis
G559E/G572E
site-directed mutagenesis, crystal structure analysis, the mutant shows 14fold increaed Km for allophanate, and reduced substrate binding at the N-domain active site, but is catalytically active
G559E/G572E
site-directed mutagenesis, the mutant shows abolished activity
S177A
site-directed mutagenesis, crystal structure analysis
S177A
site-directed mutagenesis, the mutation inactivates the isolated KlAH
S179A
-
site-directed mutagenesis
S179A
-
site-directed mutagenesis
-
S179A
-
site-directed mutagenesis
-
S179A
-
site-directed mutagenesis
-
additional information
generation of isolated domains
additional information
-
generation of isolated domains
additional information
generation of the KlUADELTABCCP construct via insertion a stop codon after base pair 5223
additional information
-
generation of the KlUADELTABCCP construct via insertion a stop codon after base pair 5223
-
additional information
-
generation of the KlUADELTABCCP construct via insertion a stop codon after base pair 5223
-
additional information
-
generation of the KlUADELTABCCP construct via insertion a stop codon after base pair 5223
-
additional information
-
generation of the KlUADELTABCCP construct via insertion a stop codon after base pair 5223
-
additional information
-
generation of the KlUADELTABCCP construct via insertion a stop codon after base pair 5223
-
additional information
-
generation of the KlUADELTABCCP construct via insertion a stop codon after base pair 5223
-
additional information
construction of the gene encoding C-terminally truncated AtzF mutant, AtzF467
additional information
-
construction of the gene encoding C-terminally truncated AtzF mutant, AtzF467
additional information
construction of the gene encoding C-terminally truncated AtzF mutant, AtzF467, the mutant shows similar activity as the wild-type enzyme below pH 8.0, but slightly reduced activity above pH 8.0
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Whitney, P.A.; Cooper, T.G.
Urea carboxylase and allophanate hydrolase: two components of a multienzyme complex in Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
49
45-51
1972
Saccharomyces cerevisiae
brenda
Sumrada, R.A.; Cooper, T.G.
Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast
J. Biol. Chem.
257
9119-9127
1982
Saccharomyces cerevisiae
brenda
Nishiya,Y.; Toda, A.; Kawamura, Y.
Production of urea amidolase by recombinant yeast and application to the enzymic determination of urea
Seibutsu Shiro Bunseki
18
288-293
1995
Cyberlindnera jadinii, Cyberlindnera jadinii CA (u)-37
-
brenda
Maitz, G.S.; Haas, E.M.; Castric, P.A.
Purification and properties of the allophanate hydrolase from Chlamydomonas reinhardii
Biochim. Biophys. Acta
714
486-491
1982
Chlamydomonas reinhardtii
-
brenda
Cheng, G.; Shapir, N.; Sadowsky, M.J.; Wackett, L.P.
Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism
Appl. Environ. Microbiol.
71
4437-4445
2005
Agrobacterium tumefaciens, Ralstonia pickettii, Herbaspirillum huttiense, Pseudomonas sp. (Q936X2), Enterobacter cloacae (Q9ALV2), Enterobacter cloacae, Herbaspirillum huttiense NRRL B-12228, Agrobacterium tumefaciens J14a, Ralstonia pickettii D, Enterobacter cloacae 99 (Q9ALV2)
brenda
Shapir, N.; Cheng, G.; Sadowsky, M.J.; Wackett, L.P.
Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth
Appl. Environ. Microbiol.
72
2491-2495
2006
Enterobacter cloacae (Q9ALV2), Enterobacter cloacae, Enterobacter cloacae 99 (Q9ALV2)
brenda
Kanamori, T.; Kanou, N.; Kusakabe, S.; Atomi, H.; Imanaka, T.
Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea
FEMS Microbiol. Lett.
245
61-65
2005
Oleomonas sagaranensis, Oleomonas sagaranensis HD-1
brenda
Shapir, N.; Sadowsky, M.J.; Wackett, L.P.
Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP
J. Bacteriol.
187
3731-3738
2005
Pseudomonas sp. (Q936X2), Pseudomonas sp.
brenda
Jacques, D.A.; Langley, D.B.; Kuramitsu, S.; Yokoyama, S.; Trewhella, J.; Guss, J.M.
The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase
Acta Crystallogr. Sect. D
67
105-111
2011
no activity in Thermus thermophilus
brenda
Balotra, S.; Newman, J.; French, N.G.; Briggs, L.J.; Peat, T.S.; Scott, C.
Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP
Acta crystallogr. Sect. F
70
310-315
2014
Pseudomonas sp. (Q936X2), Pseudomonas sp.
brenda
Balotra, S.; Newman, J.; Cowieson, N.P.; French, N.G.; Campbell, P.M.; Briggs, L.J.; Warden, A.C.; Easton, C.J.; Peat, T.S.; Scott, C.
X-ray structure of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex
Appl. Environ. Microbiol.
81
470-480
2015
Pseudomonas sp. (Q936X2)
brenda
Lin, Y.; St Maurice, M.
The structure of allophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family
Biochemistry
52
690-700
2013
Granulibacter bethesdensis (Q0BRB0), Granulibacter bethesdensis, Granulibacter bethesdensis ATCC BAA-1260 (Q0BRB0)
brenda
Fan, C.; Li, Z.; Yin, H.; Xiang, S.
Structure and function of allophanate hydrolase
J. Biol. Chem.
288
21422-21432
2013
Kluyveromyces lactis (Q6CP22), Kluyveromyces lactis
brenda
Lin, Y.; Boese, C.; St. Maurice, M.
The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent
Protein Sci.
25
1812-1824
2016
Pseudomonas syringae pv. tomato, Candida albicans (A0A1D8PDC6), Saccharomyces cerevisiae (P32528), Granulibacter bethesdensis (Q0BRB0), Pseudomonas syringae pv. tomato DC3000, Pseudomonas syringae pv. tomato ATCC BAA-871D-5, Candida albicans ATCC MYA-2876 (A0A1D8PDC6), Granulibacter bethesdensis ATCC BAA-1260 (Q0BRB0), Saccharomyces cerevisiae ATCC 204508 (P32528), Granulibacter bethesdensis CGDN1H1 (Q0BRB0)
brenda
Balotra, S.; Newman, J.; Cowieson, N.; French, N.; Campbell, P.; Briggs, L.; Warden, A.; Easton, C.; Peat, T.; Scott, C.
X-Ray structure of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex
Appl. Environ. Microbiol.
81
470-480
2015
Pseudomonas sp. ADP (Q936X2), Pseudomonas sp. ADP
brenda
Zhao, J.; Zhu, L.; Fan, C.; Wu, Y.; Xiang, S.
Structure and function of urea amidolyase
Biosci. Rep.
38
BSR20171617
2018
Kluyveromyces lactis (Q6CP22), Kluyveromyces lactis CBS 2359 (Q6CP22), Kluyveromyces lactis NRRL Y-1140 (Q6CP22), Kluyveromyces lactis DSM 70799 (Q6CP22), Kluyveromyces lactis WM37 (Q6CP22), Kluyveromyces lactis ATCC 8585 (Q6CP22), Kluyveromyces lactis NBRC 1267 (Q6CP22)
brenda
Zhang, Z.; Zhang, J.; Zheng, Q.; Kong, C.; Li, Z.; Zhang, H.; Ma, J.
Theoretical investigation on binding process of allophanate to allophanate hydrolase
Chem. Res. Chin. Univ.
31
1023-1028
2015
Granulibacter bethesdensis (Q0BRB0), Granulibacter bethesdensis ATCC BAA-1260 (Q0BRB0), Granulibacter bethesdensis CGDNIH1 (Q0BRB0)
-
brenda