An enzyme that catalyzes the hydrolysis of allophanic acid to two molecules of ammonia plus two molecules of "active carbon dioxide". EC 3.5.1.54.
Used as feed supplement for sheep and cattle since it is a good non-protein nitrogen source. In strongly alkaline solution biuret gives a violet color with copper sulfate.
Amidohydrolases are enzymes that catalyze the hydrolysis of amides and related compounds, playing a crucial role in various biological processes including the breakdown and synthesis of bioactive molecules.
A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.
A urea hydantoin that is found in URINE and PLANTS and is used in dermatological preparations.
Amino-substituted glyoxylic acid derivative.

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)

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Structure and function of allophanate hydrolase. (5/14)

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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)

Allophanate hydrolase is an enzyme that catalyzes the hydrolysis of allophanates, which are cyclic urea derivatives, to form carboxylic acids and ammonia. This enzyme plays a role in the metabolism of urea-containing compounds in some organisms. The systematic name for this enzyme is allophanate hydrolase (decyclizing).

The biuret test is a medical/biochemical test used to detect the presence of peptide bonds, which are found in proteins. The test involves mixing a sample with a solution containing copper(II) sulfate and an alkaline substance, such as sodium hydroxide. If proteins are present in the sample, the copper ions will form a complex with the peptide bonds, resulting in a purple or violet color in the solution. The intensity of the color can be used to estimate the amount of protein present in the sample.

Biuret is actually a compound that is not related to proteins, but it was named after the same chemist as the biuret test. Biuret is a chemical compound with the formula CONHCONH2. It is formed by the reaction of two molecules of urea (CO(NH2)2) under heat. The biuret test does not detect biuret itself, but rather the peptide bonds found in proteins.

Amidohydrolases are a class of enzymes that catalyze the hydrolysis of amides and related compounds, resulting in the formation of an acid and an alcohol. This reaction is also known as amide hydrolysis or amide bond cleavage. Amidohydrolases play important roles in various biological processes, including the metabolism of xenobiotics (foreign substances) and endogenous compounds (those naturally produced within an organism).

The term "amidohydrolase" is a broad one that encompasses several specific types of enzymes, such as proteases, esterases, lipases, and nitrilases. These enzymes have different substrate specificities and catalytic mechanisms but share the common ability to hydrolyze amide bonds.

Proteases, for example, are a major group of amidohydrolases that specifically cleave peptide bonds in proteins. They are involved in various physiological processes, such as protein degradation, digestion, and regulation of biological pathways. Esterases and lipases hydrolyze ester bonds in various substrates, including lipids and other organic compounds. Nitrilases convert nitriles into carboxylic acids and ammonia by cleaving the nitrile bond (C≡N) through hydrolysis.

Amidohydrolases are found in various organisms, from bacteria to humans, and have diverse applications in industry, agriculture, and medicine. For instance, they can be used for the production of pharmaceuticals, biofuels, detergents, and other chemicals. Additionally, inhibitors of amidohydrolases can serve as therapeutic agents for treating various diseases, such as cancer, viral infections, and neurodegenerative disorders.

Urea is not a medical condition but it is a medically relevant substance. Here's the definition:

Urea is a colorless, odorless solid that is the primary nitrogen-containing compound in the urine of mammals. It is a normal metabolic end product that is excreted by the kidneys and is also used as a fertilizer and in various industrial applications. Chemically, urea is a carbamide, consisting of two amino groups (NH2) joined by a carbon atom and having a hydrogen atom and a hydroxyl group (OH) attached to the carbon atom. Urea is produced in the liver as an end product of protein metabolism and is then eliminated from the body by the kidneys through urination. Abnormal levels of urea in the blood, known as uremia, can indicate impaired kidney function or other medical conditions.

Allantoin is a naturally occurring substance that is found in some plants and animals, including humans. It is a white, crystalline powder that is only slightly soluble in water and more soluble in alcohol and ether. In the medical field, allantoin is often used as an ingredient in topical creams, ointments, and other products due to its ability to promote wound healing, skin soothing, and softening. It can also help to increase the water content of the extracellular matrix, which can be beneficial for dry or damaged skin. Allantoin has been shown to have anti-inflammatory properties, making it useful in the treatment of various skin conditions such as eczema, dermatitis, and sunburn. It is considered safe and non-irritating, making it a popular ingredient in many cosmetic and personal care products.

I'm sorry for any confusion, but "Oxamic Acid" is not a recognized term in medical terminology or pharmacology. It might be a chemical compound that you're interested in, and its scientific definition is as follows:

Oxamic acid, systematically named as ethanedioloic acid or oxalic acid diethyl ester, is an organic compound with the formula (CH3CH2)2C(COOH)2. It is a colorless liquid that is used as a solvent and in the manufacture of other chemicals.

If you're looking for medical information or definitions related to a different term, please let me know and I would be happy to help!

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 ...
Allophanate hydrolase Roon RJ; Levenberg B (1970). "[37a] ATP: Urea amidolyase (ADP) (Candida utilis)". Metabolism of Amino ... 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 ...
Urea carboxylase Allophanate hydrolase Urease test PDB: 2KAU​; Jabri E, Carr MB, Hausinger RP, Karplus PA (May 1995). "The ...
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 ...
... 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 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- ...
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 ...
83. ALLOPHANATE HYDROLASE [ԱԼՈՖԱՆԱՏ-ՀԻԴՐՈԼԱԶ] 34. ALCOHOLS, OCTYL [ՍՊԻՐՏՆԵՐ ՕԿՏԻԼԱՅԻՆ] 84. ALLOPURINOL [ԱԼՈՊՈՒՐԻՆՈԼ] ...
Putative allophanate hydrolase subunit 2 (NCBI). 61, 84. RSP_3450. RSP_3450. hypothetical protein (NCBI). 61, 84. ...
... "allophanate hydrolase subunit 1 [Ensembl]. Carboxyltransferase domain [Interproscan].","protein_coding" "AHY40722","CJ8421_ ... ","Sucrose-6-phosphate hydrolase [Ensembl]. Glycosyl hydrolases family 32 C terminal, Glycosyl hydrolases family 32 N-terminal ... ","Alpha/beta hydrolase family protein [Ensembl]. Alpha/beta hydrolase fold-5 [Interproscan].","protein_coding" "AKI49520"," ... haloacid dehalogenase-like hydrolase [Interproscan].","protein_coding" "CRO52307","No alias","Pseudomonas aeruginosa","putative ...
The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent. Lin Y, Boese CJ, St ...
Allophanate hydrolase (substance). Code System Preferred Concept Name. Allophanate hydrolase (substance). Concept Status. ...
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] ...
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] ...
Allophanate Hydrolase - Preferred Concept UI. M0000744. Scope note. An enzyme that catalyzes the hydrolysis of allophanic acid ...
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 ...
A hydrolase enzyme that converts L-asparagine and water to L-aspartate and NH3. EC 3.5.1.1. ... Allophanate Hydrolase. *Arylformamidase. *Asparaginase. *Aspartylglucosylaminase. *beta-Lactamases. *Biotinidase. *Ceramidases ...
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, ...

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