Allophanate Hydrolase
Biuret
Urea
Allantoin
Environmental Microbiology
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Carbon-Nitrogen Ligases
GATA Transcription Factors
Search Engine
Information Storage and Retrieval
Barth Syndrome
Rare congenital X-linked disorder of lipid metabolism. Barth syndrome is transmitted in an X-linked recessive pattern. The syndrome is characterized by muscular weakness, growth retardation, DILATED CARDIOMYOPATHY, variable NEUTROPENIA, 3-methylglutaconic aciduria (type II) and decreases in mitochondrial CARDIOLIPIN level. Other biochemical and morphological mitochondrial abnormalities also exist.
Tripterygium
Medication Adherence
Internet
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Simbu virus
Silk
Spiders
Arthropods of the class ARACHNIDA, order Araneae. Except for mites and ticks, spiders constitute the largest order of arachnids, with approximately 37,000 species having been described. The majority of spiders are harmless, although some species can be regarded as moderately harmful since their bites can lead to quite severe local symptoms. (From Barnes, Invertebrate Zoology, 5th ed, p508; Smith, Insects and Other Arthropods of Medical Importance, 1973, pp424-430)
Atrazine
A selective triazine herbicide. Inhalation hazard is low and there are no apparent skin manifestations or other toxicity in humans. Acutely poisoned sheep and cattle may show muscular spasms, fasciculations, stiff gait, increased respiratory rates, adrenal degeneration, and congestion of the lungs, liver, and kidneys. (From The Merck Index, 11th ed)
Herbicides
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Pesticides
Methylmalonyl-CoA Decarboxylase
Carbon-Carbon Ligases
Pyruvate Carboxylase
Biotin
Acetyl-CoA Carboxylase
Biotinidase
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Oligonucleotide Array Sequence Analysis
Aortopulmonary Septal Defect
Gene Expression Regulation
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Transcription, Genetic
Desulfovibrio vulgaris
Desulfovibrio
Staphylococcaceae
Computational Biology
A field of biology concerned with the development of techniques for the collection and manipulation of biological data, and the use of such data to make biological discoveries or predictions. This field encompasses all computational methods and theories for solving biological problems including manipulation of models and datasets.
Amino Acid Motifs
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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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 ...
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 ...
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: beta-diketone hydrolase ... bile-acid-CoA hydrolase EC 3.1.2.27: choloyl-CoA hydrolase EC 3.1.2.28: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase EC 3.1.2.29: ... 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 ...
Allophanate hydrolase - Wikipedia
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 ...
FEZ53 01325 - Allophanate hydrolase subunit 2 - Staphylococcus xylosus - FEZ53 01325 gene & protein
Allophanate hydrolase subunit 2Imported. Automatic assertion inferred from database entriesi ... tr,A7KJH1,A7KJH1_STAXY Allophanate hydrolase subunit 2 OS=Staphylococcus xylosus OX=1288 GN=FEZ53_01325 PE=4 SV=1 ... HydrolaseImported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p>,a href="/ ...
Urea carboxylase - Wikipedia
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 ...
Complete Nucleotide Sequence and Organization of the Atrazine Catabolic Plasmid pADP-1 from Pseudomonassp. Strain ADP | Journal...
E. coli strains bearing atzEand atzF were shown to encode a biuret hydrolase and allophanate hydrolase, respectively. atzDEF ... had allophanate hydrolase activity. In contrast, only limited loss of allophanate was seen with extracts from E. coli(pUC18), ... Urea carboxylase and allophanate hydrolase are components of multifunctional protein in yeast.J. Biol. Chem.257198291199127. ... Urea carboxylase and allophanate hydrolase. Two components of adenosine triphosphate:urea amidolyase in Saccharomyces ...
KEGG BRITE: Enzymes - Equus caballus (horse)
EC 3.5.1.51 and EC 3.5.1.136
Accepted name: allophanate hydrolase. Reaction: urea-1-carboxylate + H2O = 2 CO2 + 2 NH3. For diagram of reaction click here.. ... 6-aminohexanoate oligomer hydrolase; Ahx-oligomer hydrolase; nylon hydrolase; nylon-oligomer hydrolase; NylC; nylon-6 hydrolase ... EC 3.5.1.54 allophanate hydrolase. EC 3.5.1.55 long-chain-fatty-acyl-glutamate deacylase. EC 3.5.1.56 N,N-dimethylformamidase. ... EC 3.5.1.99 fatty acid amide hydrolase EC 3.5.1.100 (R)-amidase EC 3.5.1.101 L-proline amide hydrolase EC 3.5.1.102 2-amino-5- ...
Overview: M062 02480, Pseudomonas aeruginosa RP73
Overview: PA2G 04413, Pseudomonas aeruginosa 2192
Complete Genome Sequence of Nitrobacter hamburgensis X14 and Comparative Genomic Analysis of Species within the Genus...
... and allophanate hydrolase (Nham_2040; COG2049). The latter two enzymes putatively contribute to ATP-dependent urea amidolyase ... All NOB genomes lack genes encoding a classical urease (ATP-independent urea hydrolase) or a urea transporter identified ... hydrolases, and sialic-acid based homopolysaccharide formation genes, some of which have little sequence similarity to any ...
urea | Applied and Environmental Microbiology
Frontiers | Reconstruction of the Metabolic Potential of Acidophilic Sideroxydans Strains from the Metagenome of an...
DUR1,2 (YBR208C) Result Summary | BioGRID
Expression Sensitive To Nitrogen Catabolite Repression And Induced By Allophanate, An Intermediate In Allantoin Degradation; ... Contains Both Urea Carboxylase And Allophanate Hydrolase Activities, Degrades Urea To CO2 And NH3; ... Urea amidolyase; contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression ... DUR80, bifunctional urea carboxylase/allophanate hydrolase, L000000532, L000000533, L000000536, YBR208C. ...
CDD Conserved Protein Domain Family: urea degr 1
A number of bacteria degrade urea as a nitrogen source by the urea carboxylase/allophanate hydrolase pathway, which uses biotin ... A number of bacteria degrade urea as a nitrogen source by the urea carboxylase/allophanate hydrolase pathway, which uses biotin ... tandem uncharacterized genes found together with the urea carboxylase and allophanate hydrolase genes. ...
KEGG SSDB Best Search Result: bdi:100835291
cyn:Cyan7425_3252 allophanate hydrolase K01457 607 100 ( -) 29 0.300 150 -, 1 fjg:BB050_03756 2-oxoisovalerate dehydrogenase ... ase:ACPL_5595 alpha/beta hydrolase fold protein 255 109 ( 7) 31 0.330 103 -, 2 asf:SFBM_0853 3-oxoacyl-[acyl-carrier-protein] ... taa:NMY3_01686 Alpha/beta hydrolase family protein K06889 346 104 ( -) 30 0.324 71 -, 1 tne:Tneu_1901 Radical SAM domain ...
KEGG SSDB Best Search Result: mhi:Mhar 2265
ror:RORB6_06485 allophanate hydrolase K01457 599 102 ( -) 29 0.301 73 -, 1 rro:104674625 early B-cell factor 4 K09103 645 102 ... sphk:SKP52_11960 glycosyl hydrolase family protein K05349 877 105 ( -) 30 0.307 189 ,-, 1 syc:syc0479_d oxidoreductase aldo/ ... scb:SCAB_25521 putative glycosyl hydrolase K01811 683 100 ( -) 29 0.316 79 -, 1 smt:Smal_3299 phosphoesterase PA-phosphatase ... rmu:RMDY18_03680 Zn-dependent hydrolase including glyox 322 112 ( -) 31 0.320 103 -, 1 rpe:RPE_0024 gamma-glutamyltransferase ...
Toxicity, degradation and analysis of the herbicide atrazine | Springer for Research & Development
SMART: Secondary literature for Biotin carb C domain
Urea amidolyase catalyzes the two reactions (urea carboxylase and a allophanate hydrolase) associated with urea degradation in ... These data are consistent with the suggestion that sequential induction of allophanate hydrolase and urea carboxylase ... we determined whether or not a detectable period of time elapsed between the appearance of allophanate hydrolase activity and ... approximately 2 to 6 min elapsed between the appearance of allophanate hydrolase and urea carboxylase activities. In search of ...
Structure and function of biotin-dependent carboxylases | SpringerLink
Multi-targeted priming for genome-wide gene expression assays | BMC Genomics | Full Text
Comparative and Functional Genomic Analysis of Prokaryotic Nickel and Cobalt Uptake Transporters: Evidence for a Novel Group of...
Complete genome sequence and metabolic potential of the quinaldine-degrading bacterium Arthrobacter sp. Rue61a | BMC Genomics |...
... allophanate) catalyzed by urea carboxylase, followed by hydrolysis to CO2 and ammonia by allophanate hydrolase (see Additional ... Two pathways seem to be present for the degradation of urea, namely, direct cleavage by urease (ureABC), and an allophanate ... The genome contains several genes coding for putative lipases/esterases of the α/β-hydrolase fold-superfamily or the SGNH- ... Urate degradation probably involves urate oxidase and 5-hydroxyisourate hydrolase. The next step, catalyzed by OHCU ...
Code System Concept
DeCS
4GYS | Genus
CN09 00845 protein (Agrobacterium rhizogenes) - STRING interaction network
Allophanate hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology (116 aa). ... Allophanate hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology ... Allophanate hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology ... Allophanate hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology ...
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Browse
Allophanate hydrolase subunit 2 YP_003110896 normal 0.368046 normal 0.0250714 Catenulispora acidiphila DSM 44928 Bacteria -. ... HAD-superfamily hydrolase, subfamily IA, variant 1 YP_003110860 normal 1 normal 1 Catenulispora acidiphila DSM 44928 Bacteria - ... HAD-superfamily subfamily IB hydrolase, TIGR01490 YP_003110850 normal 1 normal 1 Catenulispora acidiphila DSM 44928 Bacteria - ...
Subunit1
- In COG0327 its role is Allophanate hydrolase 2 subunit 2 (EC 3.5.1.54) . (theseed.org)
1.541
- In enzymology, an allophanate hydrolase (EC 3.5.1.54) is an enzyme that catalyzes the chemical reaction allophanate + 3 H2O + H+ ⇌ {\displaystyle \rightleftharpoons } 2 HCO3− + 2 NH4+ Thus, the two substrates of this enzyme are allophanate (urea-1-carboxylate or N-carbamoylcarbamate) and H2O, whereas its two products are HCO3− and NH4+. (wikipedia.org)
Biotin3
- A number of bacteria degrade urea as a nitrogen source by the urea carboxylase/allophanate hydrolase pathway, which uses biotin and consumes ATP, rather than my means of the nickel-dependent enzyme urease. (nih.gov)
- In Allophanate hydrolase 2 and Biotin carboxylase cluster its role is prokaryotic 5-oxoprolinase C, pxpC . (theseed.org)
- CO2 fixation and the involvement of allophanate in the biotin-enzyme-catalyzed cleavage of urea. (semanticscholar.org)
Biuret hydrolase3
- E. coli strains bearing atzE and atzF were shown to encode a biuret hydrolase and allophanate hydrolase, respectively. (asm.org)
- 25 Jan 2001 bearing atzE and atzF were shown to encode a biuret hydrolase and allophanate hydrolase, 51784 54699 d Transposase from IS1071. (fluoridefacts.org)
- The first enzyme, guanylurea hydrolase, is a member of the isochorismatase-like hydrolase protein family, which includes biuret hydrolase and triuret hydrolase. (bvsalud.org)
Urea-1-carboxylate1
- In enzymology, an urea carboxylase (EC 6.3.4.6) is an enzyme that catalyzes the chemical reaction ATP + urea + HCO3- ⇌ {\displaystyle \rightleftharpoons } ADP + phosphate + urea-1-carboxylate The 3 substrates of this enzyme are ATP, urea, and HCO3-, whereas its 3 products are ADP, phosphate, and urea-1-carboxylate (allophanate). (wikipedia.org)
Enzyme3
- This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. (wikipedia.org)
- This enzyme is also called allophanate lyase. (wikipedia.org)
- Guanylurea hydrolase, a newly described enzyme, was shown to transform guanylurea to one equivalent (each) of ammonia and guanidine. (bvsalud.org)
Genes2
- This model represents one of a pair of homologous, tandem uncharacterized genes found together with the urea carboxylase and allophanate hydrolase genes. (nih.gov)
- Genes encoding complete metabolic transformation were identified bioinformatically, defining the pathway as follows: guanylurea to guanidine to carboxyguanidine to allophanate to ammonia and carbon dioxide. (bvsalud.org)
Enzymes1
- Pairwise sequence comparisons and the use of sequence similarity networks allowed fine structure discrimination between the three homologous enzymes and provided insights into the evolutionary origins of guanylurea hydrolase.IMPORTANCE Metformin is a pharmaceutical most prescribed for type 2 diabetes and is now being examined for potential benefits to COVID-19 patients. (bvsalud.org)
Gene1
- Identification of the ureidoglycolate hydrolase gene in the DAL gene cluster of Saccharomyces cerevisiae. (semanticscholar.org)