Allophanate Hydrolase
Biuret
Urea
Allantoin
Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. (1/14)
AtzF, allophanate hydrolase, is a recently discovered member of the amidase signature family that catalyzes the terminal reaction during metabolism of s-triazine ring compounds by bacteria. In the present study, the atzF gene from Pseudomonas sp. strain ADP was cloned and expressed as a His-tagged protein, and the protein was purified and characterized. AtzF had a deduced subunit molecular mass of 66,223, based on the gene sequence, and an estimated holoenzyme molecular mass of 260,000. The active protein did not contain detectable metals or organic cofactors. Purified AtzF hydrolyzed allophanate with a k(cat)/K(m) of 1.1 x 10(4) s(-1) M(-1), and 2 mol of ammonia was released per mol allophanate. The substrate range of AtzF was very narrow. Urea, biuret, hydroxyurea, methylcarbamate, and other structurally analogous compounds were not substrates for AtzF. Only malonamate, which strongly inhibited allophanate hydrolysis, was an alternative substrate, with a greatly reduced k(cat)/K(m) of 21 s(-1) M(-1). Data suggested that the AtzF catalytic cycle proceeds through a covalent substrate-enzyme intermediate. AtzF reacts with malonamate and hydroxylamine to generate malonohydroxamate, potentially derived from hydroxylamine capture of an enzyme-tethered acyl group. Three putative catalytically important residues, one lysine and two serines, were altered by site-directed mutagenesis, each with complete loss of enzyme activity. The identity of a putative serine nucleophile was probed using phenyl phosphorodiamidate that was shown to be a time-dependent inhibitor of AtzF. Inhibition was due to phosphoroamidation of Ser189 as shown by liquid chromatography/matrix-assisted laser desorption ionization mass spectrometry. The modified residue corresponds in sequence alignments to the nucleophilic serine previously identified in other members of the amidase signature family. Thus, AtzF affects the cleavage of three carbon-to-nitrogen bonds via a mechanism similar to that of enzymes catalyzing single-amide-bond cleavage reactions. AtzF orthologs appear to be widespread among bacteria. (+info)Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism. (2/14)
Growth substrates containing an s-triazine ring are typically metabolized by bacteria to liberate 3 mol of ammonia via the intermediate cyanuric acid. Over a 25-year period, a number of original research papers and reviews have stated that cyanuric acid is metabolized in two steps to the 2-nitrogen intermediate urea. In the present study, allophanate, not urea, was shown to be the 2-nitrogen intermediate in cyanuric acid metabolism in all the bacteria examined. Six different experimental results supported this conclusion: (i) synthetic allophanate was shown to readily decarboxylate to form urea under acidic extraction and chromatography conditions used in previous studies; (ii) alkaline extraction methods were used to stabilize and detect allophanate in bacteria actively metabolizing cyanuric acid; (iii) the kinetic course of allophanate formation and disappearance was consistent with its being an intermediate in cyanuric acid metabolism, and no urea was observed in those experiments; (iv) protein extracts from cells grown on cyanuric acid contained allophanate hydrolase activity; (v) genes encoding the enzymes AtzE and AtzF, which produce and hydrolyze allophanate, respectively, were found in several cyanuric acid-metabolizing bacteria; and (vi) TrzF, an AtzF homolog found in Enterobacter cloacae strain 99, was cloned, expressed in Escherichia coli, and shown to have allophanate hydrolase activity. In addition, we have observed that there are a large number of genes homologous to atzF and trzF distributed in phylogenetically distinct bacteria. In total, the data indicate that s-triazine metabolism in a broad class of bacteria proceeds through allophanate via allophanate hydrolase, rather than through urea using urease. (+info)Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. (3/14)
TrzF, the allophanate hydrolase from Enterobacter cloacae strain 99, was cloned, overexpressed in the presence of a chaperone protein, and purified to homogeneity. Native TrzF had a subunit molecular weight of 65,401 and a subunit stoichiometry of alpha(2) and did not contain significant levels of metals. TrzF showed time-dependent inhibition by phenyl phosphorodiamidate and is a member of the amidase signature protein family. TrzF was highly active in the hydrolysis of allophanate but was not active with urea, despite having been previously considered a urea amidolyase. TrzF showed lower activity with malonamate, malonamide, and biuret. The allophanate hydrolase from Pseudomonas sp. strain ADP, AtzF, was also shown to hydrolyze biuret slowly. Since biuret and allophanate are consecutive metabolites in cyanuric acid metabolism, the low level of biuret hydrolase activity can have physiological significance. A recombinant Escherichia coli strain containing atzD, encoding cyanuric acid hydrolase that produces biuret, and atzF grew slowly on cyanuric acid as a source of nitrogen. The amount of growth produced was consistent with the liberation of 3 mol of ammonia from cyanuric acid. In vitro, TrzF was shown to hydrolyze biuret to liberate 3 mol of ammonia. The biuret hydrolyzing activity of TrzF might also be physiologically relevant in native strains. E. cloacae strain 99 grows on cyanuric acid with a significant accumulation of biuret. (+info)The structure of allophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family. (4/14)
(+info)Structure and function of allophanate hydrolase. (5/14)
(+info)Control of vacuole permeability and protein degradation by the cell cycle arrest signal in Saccharomyces cerevisiae. (6/14)
Saccharomyces cerevisiae responds to deperivation of nutrients by arresting cell division at the unbudded G1 stage. Cells situated outside of G1 at the time of deperivation complete the cell cycle before arresting. This prompted an investigation of the source of nutrients used by these cells to complete division and the mechanisms controlling their availability. We found a close correlation between accumulation of unbudded cells and loss of previously formed allophanate hydrolase activity after nutrient starvation. These losses were not specific to the allantoin, system since they have been observed for a number of other enzymes and also when cellular protein levels were monitored with [3H]leucine. Loss of hydrolase activity was also observed when protein synthesis was inhibited either by addition of inhibitors or loss of the prtl gene product. We found that onset of nutrient starvation brought about release of large quantities of arginine and allantoin normally sequestered in the cell vacuole. Treatment of a cells with alpha-factor resulted in both the release of allantoin and arginine from the cell vacuole and the onset of intracellular protein degradation. These effects were not observed when either alpha cells or a/alpha diploid strains were treated with alpha-factor. These data suggest that release of vacuolar constitutents and protein turnover may be regulated by the G1 arrest signal. (+info)Structural analysis of the dur loci in S. cerevisiae: two domains of a single multifunctional gene. (7/14)
In Saccharomyces cerevisiae, the degradation of urea to carbon dioxide and ammonia is catalyzed by urea carboxylase and allophanate hydrolase. The loci coding for these enzymes (dur1 and dur2) are very tightly linked on the right arm of chromosome II between pet11 and met8. Pleiotropic mutations that fail to complement mutations in either of the dur loci were found to be predominantly located in or near the dur2 locus. We interpret these data as suggesting that the two dur loci might in reality be domains of a single gene that codes for a multifunctional polypeptide. In view of this conclusion, we have renamed the dur loci as the dur1,2 locus. (+info)Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast. (8/14)
Saccharomyces cerevisiae can use urea as sole nitrogen source by degrading it in two steps (urea carboxylase and allophanate hydrolase) to ammonia and carbon dioxide. We previously demonstrated that: 1) the enzymatic functions required for degradation are encoded in two tightly linked genetic loci and 2) pleiotropic mutations each resulting in the loss of both activities are found in both loci. These and other observations led to the hypothesis that urea degradation might be catalyzed by a multifunctional polypeptide. Waheed and Castric (1977) J. Biol. Chem. 252, 1628-1632), on the other hand, purified urea amidolyase from Candida utilis and reported it to be a tetramer composed of nonidentical 70- and 170-kilodalton subunits. To resolve the differing views of urea amidolyase structure, we purified the protein using rapid methods designed to avoid proteolytic cleavage. Application of these methods resulted in the isolation of a single, inducible and repressible, 204-kilodalton species. We observed no evidence for the existence of nonidentical subunits. A similar inducible, high molecular weight species was also detected in C. utilis. These biochemical results support our earlier hypothesis that urea degradation is carried out in yeast by an inducible and repressible protein composed of identical, multifunctional subunits. (+info)
DUR1,2 (YBR208C) Result Summary | BioGRID
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Allophanate hydrolase
In enzymology, an allophanate hydrolase (EC 3.5.1.54) is an enzyme that catalyzes the chemical reaction allophanate + 3 H2O + ... Kanamori T, Kanou N, Kusakabe S, Atomi H, Imanaka T (2005). "Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP ... Sumrada RA, Cooper TG (1982). "Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast ... Urea carboxylase Maitz GS, Haas EM, Castric PA (1982). "Purification and properties of the allophanate hydrolase from ...
Urea carboxylase
Allophanate hydrolase Roon RJ; Levenberg B (1970). ATP-Urea amidolyase (ADP) (Candida utilis). Methods Enzymol. Methods in ... Sumrada RA, Cooper TG (1982). "Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast ... allophanate). This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The ...
Urease
Urea carboxylase Allophanate hydrolase Urease test PDB: 2KAU; Jabri E, Carr MB, Hausinger RP, Karplus PA (May 1995). "The ...
Allophanic acid
The anion allophonate is the substrate for the enzyme allophanate hydrolase. Allophonate esters arise from the condensation of ... is called allophanate. Salt of this anion have been characterized by X-ray crystallography. ... "Novel Hydrogen-Bonded Host Lattices Built of Urea and the Elusive Allophanate Ion". Journal of the American Chemical Society. ... trimethylammonium Ions Included in a Channel Host Lattice Built of Urea Molecules and Allophanate Ions". Supramolecular ...
List of MeSH codes (D08)
... allophanate hydrolase MeSH D08.811.277.087.100 - arylformamidase MeSH D08.811.277.087.116 - asparaginase MeSH D08.811.277.087. ... thiolester hydrolases MeSH D08.811.277.352.897.075 - acetyl-CoA hydrolase MeSH D08.811.277.352.897.700 - palmitoyl-coa ... phosphoric diester hydrolases MeSH D08.811.277.352.640.050 - annexin A3 MeSH D08.811.277.352.640.125 - 3',5'-cyclic-GMP ... pyroglutamate hydrolase MeSH D08.811.277.087.831 - sirtuins MeSH D08.811.277.087.902 - urease MeSH D08.811.277.151.300 - gtp ...
List of EC numbers (EC 3)
... allophanate hydrolase EC 3.5.1.55: long-chain-fatty-acyl-glutamate deacylase EC 3.5.1.56: N,N-dimethylformamidase EC 3.5.1.57: ... phloretin hydrolase EC 3.7.1.5: acylpyruvate hydrolase EC 3.7.1.6: acetylpyruvate hydrolase EC 3.7.1.7: β-diketone hydrolase EC ... acetyl-CoA hydrolase EC 3.1.2.2: palmitoyl-CoA hydrolase EC 3.1.2.3: succinyl-CoA hydrolase EC 3.1.2.4: 3-hydroxyisobutyryl-CoA ... 3-dione hydrolase EC 3.7.1.11: cyclohexane-1,2-dione hydrolase EC 3.7.1.12: cobalt-precorrin 5A hydrolase EC 3.7.1.13: 2- ...
Frontiers | Metabolic Potential, Ecology and Presence of Associated Bacteria Is Reflected in Genomic Diversity of Mucoromycotina
... urea carboxylase and two copies of allophanate hydrolase (AtzF). The Paenibacillus genome encodes also one copy of ulilysin ... We also observed an expansion of GH16 hydrolases and hexosaminidase (GH20) in Umbelopsidales compared to Mucorales. On the ... GH, glycoside hydrolases; GT, glycosyltransferases; CMB, carbohydrate-binding modules; CE, carbohydrate esterase. ... and diverse hydrolases (Roukas et al., 2015; Voigt et al., 2016; Rivaldi et al., 2017). Certain Mucorales (e.g., M. indicus) ...
DeCS
Code System Concept
English-Armenian Medical - Terms starting with 'L' - MEDINDEX.AM
SACOL RS08485 - AureoWiki
YJR139C 267.488705 INESSENTIAL HOM6 "Homoserine dehydrogenase (L-homoserine:NADP oxidoreductase),5-amino-6-(5...
... contains urea carboxylase and allophanate hydrolase),allophanate hydrolase," YJR037W -0.194574 INESSENTIAL "biological_process ... "acetyl CoA hydrolase, acetate metabolism*, acetyl-CoA hydrolase, cytoplasm" YKL148C 1.29193 INESSENTIAL SDH1 "flavoprotein ... hydroxyacylglutathione hydrolase, mitochondrion*" YIL140W 2.126548 INESSENTIAL AXL2 "localizes to the plasma membrane, axial ... "ubiquitin hydrolase, deubiquitylation, ubiquitin-specific protease, cytoplasm" YPL189W 7.192523 INESSENTIAL GUP2 Putative ...
"sequence id","alias","species","description",...
"Putative allophanate hydrolase subunit 1 [Ensembl]. Carboxyltransferase domain [Interproscan].","protein_coding" "CCL17558","No ... ","Sucrose-6-phosphate hydrolase [Ensembl]. Glycosyl hydrolases family 32 C terminal, Glycosyl hydrolases family 32 N-terminal ... "allophanate hydrolase subunit 1 [Ensembl]. Carboxyltransferase domain [Interproscan].","protein_coding" "AHY40722","CJ8421_ ... "Putative allophanate hydrolase subunit 2 [Ensembl]. Carboxyltransferase domain [Interproscan].","protein_coding" "CCL17751"," ...
BiGG Metabolite h2o c in iMM904
Pre GI: Gene
Domain IPR003439:ABC transporter-like
Allophanate hydrolase 2 Family IPR010295:Protein of unknown function DUF898 2 Repeat IPR011690:Phosphate-starvation-induced ... Alpha/beta hydrolase fold-1 327 Domain IPR000792:Transcription regulator LuxR, C-terminal 326 Domain IPR000086:NUDIX hydrolase ... Glycoside hydrolase family 1 37 Domain IPR026888:Acetyl-CoA hydrolase/transferase C-terminal domain 37 Domain IPR001357:BRCT ... HAD-superfamily hydrolase, subfamily IIA 20 Family IPR019904:Peroxiredoxin OsmC 20 Domain IPR033452:Glycosyl hydrolase family ...
KEGG REACTION: R00005
Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis - PubMed
MeSH Browser
Allophanate Hydrolase Preferred Term Term UI T001450. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1975). ... Allophanate Hydrolase Preferred Concept UI. M0000744. Registry Number. EC 3.5.1.54. Scope Note. An enzyme that catalyzes the ... Allophanate Hydrolase. Tree Number(s). D08.811.277.087.060. Unique ID. D000492. RDF Unique Identifier. http://id.nlm.nih.gov/ ... Hydrolases [D08.811.277] * Amidohydrolases [D08.811.277.087] * N-Acetylmuramoyl-L-alanine Amidase [D08.811.277.087.030] ...
Experts and Doctors on protein binding in Sydney, New South Wales, Australia
MeSH Browser
Allophanate Hydrolase Preferred Term Term UI T001450. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1975). ... Allophanate Hydrolase Preferred Concept UI. M0000744. Registry Number. EC 3.5.1.54. Scope Note. An enzyme that catalyzes the ... Allophanate Hydrolase. Tree Number(s). D08.811.277.087.060. Unique ID. D000492. RDF Unique Identifier. http://id.nlm.nih.gov/ ... Hydrolases [D08.811.277] * Amidohydrolases [D08.811.277.087] * N-Acetylmuramoyl-L-alanine Amidase [D08.811.277.087.030] ...
Quantitative proteomic analysis reveals the ethanologenic metabolism regulation of Ethanoligenens harbinense by exogenous...
Open Research: Browsing Open Research
NDF-RT Code NDF-RT Name
Alkynes N0000005787 Allantoin N0000171131 Allergens N0000166347 Allethrin N0000179033 alloin N0000167672 Allophanate Hydrolase ... Phosphoric Diester Hydrolases N0000167640 Phosphoric Monoester Hydrolases N0000167660 Phosphoric Triester Hydrolases ... N0000168132 Acetyl-CoA C-Acyltransferase N0000167754 Acetyl-CoA Carboxylase N0000167609 Acetyl-CoA Hydrolase N0000166509 ... N0000010515 Palmitic Acid N0000008240 Palmitic Acids N0000170826 Palmitoyl Coenzyme A N0000167611 Palmitoyl-CoA Hydrolase ...
TransTermHP v2.07 (built on Jan 21 2009
... allophanate hydrolase subunit 1 TERM 582 648170 - 648181 + G 83 -3 -5.78622 , AAATTAATTTTGCAA TATC TGGA GATA TTTTTTTTAAAATCA ... allophanate hydrolase subunit 2 TERM 583 649528 - 649542 + G 72 -5 -4.84918 , TACAGCAGGTTTTTT CCAAGT AGG ATTTGG TTTTATATTTATAAC ... hydrolase and other HIT family hydrolase aprM 804704 - 805498 + , adenylylsulfate reductase membrane anchor TERM 726 805818 - ... alpha/beta hydrolase fold protein TERM 354 430548 - 430524 - H 76 -3.7 -5.49729 , opp_overlap 430527, overlap 430527 ...
Seed Viewer - Feature
ABORTIFACIENT AGENTS ABORTIFACIENT AGENTS
HYDROLASES ADP-RIBOSYLATION FACTORS HYDROLASES ALKALINE PHOSPHATASE HYDROLASES ALLOPHANATE HYDROLASE HYDROLASES ALPHA-AMYLASE ... HYDROLASES FACTOR IXA HYDROLASES FACTOR VIIA HYDROLASES FACTOR XA HYDROLASES FACTOR XIA HYDROLASES FACTOR XIIA HYDROLASES ... HYDROLASES CARDIAC MYOSINS HYDROLASES CASPASE 1 HYDROLASES CASPASES HYDROLASES CATHEPSIN B HYDROLASES CATHEPSIN D HYDROLASES ... HYDROLASES GAMMA-GLUTAMYL HYDROLASE HYDROLASES GELATINASE A HYDROLASES GELATINASE B HYDROLASES GELATINASES HYDROLASES GLUCAN 1, ...
DeCS
ExplorEnz: EC 3.5.1.84
Cameron, S.M., Durchschein, K., Richman, J.E., Sadowsky, M.J. and Wackett, L.P. A new family of biuret hydrolases involved in s ... allophanate = urea-1-carboxylate. Other name(s):. biuH (gene name). Systematic name: biuret amidohydrolase. ... Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of ...
c33c
... league matchless pedata pteronarcys trotter durable malarious ethiopia lycioides floridiensis recontact trachinotus hydrolases ... synchrotrons nitrosoureido mov18 enterochelin propeller mov10 schwalbe conspecifics emigration propelled allophanate tachyzoite ... glucopyranosiduronic sarcocystis michaelseni pelvetia adler peaceful angiopathic augsburg pyrimido benzylaniline hydrolase ...
µ
... hydrolase acyl-peptide hydrolase acylpeptide hydrolase acyl peptide hydrolases acyl-peptide hydrolases acylpeptide hydrolases ... allopatric allopatrically allopeptide allopeptides Allopetrolisthes spinifrons allophanamide allophanamides allophanate ... beta-hydroxyisobutyryl-CoA hydrolase beta-hydroxyisobutyryl-coenzyme A beta-hydroxyisobutyryl-coenzyme A hydrolase beta- ... choline acyl-choline acylcholineacylhydrolase acylcholine acylhydrolase acylcholine acyl hydrolase acylcholine acyl-hydrolase ...