3.5.1.54: allophanate hydrolase
This is an abbreviated version!
For detailed information about allophanate hydrolase, go to the full flat file.
Word Map on EC 3.5.1.54
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3.5.1.54
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carboxylase
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ammonia
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amidolyase
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amidase
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s-triazine
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dioxide
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ah
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cyanuric
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biuret
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ribonucleic
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kluyveromyces
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chlamydomonas
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enterobacter
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atrazine
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lactis
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allantoin
- 3.5.1.54
- carboxylase
- ammonia
-
amidolyase
- amidase
- s-triazine
- dioxide
- ah
-
cyanuric
- biuret
-
ribonucleic
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kluyveromyces
- chlamydomonas
- enterobacter
- atrazine
- lactis
- allantoin
Reaction
Synonyms
allophanate lyase, AtzF, DUR1,2, GbCGDNIH1_1744, KlAH, KLLA0_E08119g, PsAH, TrzF, UAL, urea amidolyase
ECTree
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General Information
General Information on EC 3.5.1.54 - allophanate hydrolase
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evolution
malfunction
metabolism
physiological function
additional information
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
Pseudomonas syringae pv. tomato ATCC BAA-871D-5
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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
Granulibacter bethesdensis CGDN1H1
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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
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allophanate hydrolase (AH) is a member of the AS family
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the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC
malfunction
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the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC
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malfunction
Pseudomonas syringae pv. tomato ATCC BAA-871D-5
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the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC
-
malfunction
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the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC
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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
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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
-
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
Pseudomonas syringae pv. tomato ATCC BAA-871D-5
-
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
Granulibacter bethesdensis CGDN1H1
-
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
-
the enzyme's N and C domains catalyze sequential reactions, overview
additional information
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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
Pseudomonas syringae pv. tomato ATCC BAA-871D-5
-
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
Granulibacter bethesdensis CGDN1H1
-
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
-