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.

Reduced pyrazinamidase activity and the natural resistance of Mycobacterium kansasii to the antituberculosis drug pyrazinamide. (1/2620)

Pyrazinamide (PZA), an analog of nicotinamide, is a prodrug that requires conversion to the bactericidal compound pyrazinoic acid (POA) by the bacterial pyrazinamidase (PZase) activity of nicotinamidase to show activity against Mycobacterium tuberculosis. Mutations leading to a loss of PZase activity cause PZA resistance in M. tuberculosis. M. kansasii is naturally resistant to PZA and has reduced PZase activity along with an apparently detectable nicotinamidase activity. The role of the reduction in PZase activity in the natural PZA resistance of M. kansasii is unknown. The MICs of PZA and POA for M. kansasii were determined to be 500 and 125 micrograms/ml, respectively. Using [14C]PZA and [14C]nicotinamide, we found that M. kansasii had about 5-fold-less PZase activity and about 25-fold-less nicotinamidase activity than M. tuberculosis. The M. kansasii pncA gene was cloned on a 1.8-kb BamHI DNA fragment, using M. avium pncA probe. Sequence analysis showed that the M. kansasii pncA gene encoded a protein with homology to its counterparts from M. tuberculosis (69.9%), M. avium (65.6%), and Escherichia coli (28.5%). Transformation of naturally PZA-resistant M. bovis BCG with M. kansasii pncA conferred partial PZA susceptibility. Transformation of M. kansasii with M. avium pncA caused functional expression of PZase and high-level susceptibility to PZA, indicating that the natural PZA resistance in M. kansasii results from a reduced PZase activity. Like M. tuberculosis, M. kansasii accumulated POA in the cells at an acidic pH; however, due to its highly active POA efflux pump, the naturally PZA-resistant species M. smegmatis did not. These findings suggest the existence of a weak POA efflux mechanism in M. kansasii.  (+info)

Thermostability reinforcement through a combination of thermostability-related mutations of N-carbamyl-D-amino acid amidohydrolase. (2/2620)

For the improvement of N-carbamyl-D-amino acid amidohydrolase (DCase), which can be used for the industrial production of D-amino acids, the stability of DCase from Agrobacterium sp. KNK712 was improved through various combinations of thermostability-related mutations. The thermostable temperature (defined as the temperature on heat treatment for 10 min that caused a decrease in the DCase activity of 50%) of the enzyme which had three amino acids, H57Y, P203E, and V236A, replaced was increased by about 19 degrees C. The mutant DCase, designated as 455M, was purified and its enzymatic properties were studied. The enzyme had highly increased stability against not only temperature but also pH, the optimal temperature of the enzyme being about 75 degrees C. The substrate specificity of the enzyme for various N-carbamyl-D-amino acids was changed little in comparison with that of the native enzyme. Enzymochemical parameters were also measured.  (+info)

Insertion analysis of putative functional elements in the promoter region of the Aspergillus oryzae Taka-amylase A gene (amyB) using a heterologous Aspergillus nidulans amdS-lacZ fusion gene system. (3/2620)

Expression of the Taka-amylase A gene (amyB) of Aspergillus oryzae is induced by starch or maltose. The A. oryzae amyB gene promoter contains three highly conserved sequences, designated Regions I, II, and III, compared with promoter regions of the A. oryzae glaA encoding glucoamylase and the agdA encoding alpha-glucosidase. To identify the function of these sequences within the amyB promoter, various fragments containing conserved sequences in the amyB promoter were introduced into the upstream region of the heterologous A. nidulans amdS gene (encoding acetamidase) fused to the Escherichia coli lacZ gene as a reporter. Introduction of the sequence between -290 to -233 (the number indicates the distance in base pairs from the translation initiation point (+1)) containing Region III significantly increased the expression of the lacZ reporter gene in the presence of maltose. The sequence between -377 to -290 containing Region I also increased the lacZ activity, but its maltose inducibility was less than that of Region III. The sequence between -233 to -181 containing Region II had no effect on the expression. These results indicated that Region III is most likely involved in the maltose induction of the amyB gene expression.  (+info)

Human biotinidase isn't just for recycling biotin. (4/2620)

For years, the major role of biotin has been as the coenzyme for four carboxylases in humans. Although there has been evidence that biotin might have other functions, none has been firmly established. The discovery that human serum biotinidase has biotinyl-transferase activity, in addition to biotinidase hydrolase activity, presents new possibilities for the role of biotinidase in biotin metabolism. Specific transfer of biotin to histones by biotinidase provides a possible explanation for why biotin is found in the nucleus and the nature of its role in the regulation of protein transcription. Future studies will help to determine the functions of biotinidase in biotin metabolism and in disease states.  (+info)

IAR3 encodes an auxin conjugate hydrolase from Arabidopsis. (5/2620)

Amide-linked conjugates of indole-3-acetic acid (IAA) are putative storage or inactivation forms of the growth hormone auxin. Here, we describe the Arabidopsis iar3 mutant that displays reduced sensitivity to IAA-Ala. IAR3 is a member of a family of Arabidopsis genes related to the previously isolated ILR1 gene, which encodes an IAA-amino acid hydrolase selective for IAA-Leu and IAA-Phe. IAR3 and the very similar ILL5 gene are closely linked on chromosome 1 and comprise a subfamily of the six Arabidopsis IAA-conjugate hydrolases. The purified IAR3 enzyme hydrolyzes IAA-Ala in vitro. iar 3 ilr1 double mutants are more resistant than either single mutant to IAA-amino acid conjugates, and plants overexpressing IAR3 or ILR1 are more sensitive than is the wild type to certain IAA-amino acid conjugates, reflecting the overlapping substrate specificities of the corresponding enzymes. The IAR3 gene is expressed most strongly in roots, stems, and flowers, suggesting roles for IAA-conjugate hydrolysis in those tissues.  (+info)

Characterization of a novel rat brain glycosylphosphatidylinositol-anchored protein (Kilon), a member of the IgLON cell adhesion molecule family. (6/2620)

In the central nervous system, many cell adhesion molecules are known to participate in the establishment and remodeling of the neural circuit. Some of the cell adhesion molecules are known to be anchored to the membrane by the glycosylphosphatidylinositol (GPI) inserted to their C termini, and many GPI-anchored proteins are known to be localized in a Triton-insoluble membrane fraction of low density or so-called "raft." In this study, we surveyed the GPI-anchored proteins in the Triton-insoluble low density fraction from 2-week-old rat brain by solubilization with phosphatidylinositol-specific phospholipase C. By Western blotting and partial peptide sequencing after the deglycosylation with peptide N-glycosidase F, the presence of Thy-1, F3/contactin, and T-cadherin was shown. In addition, one of the major proteins, having an apparent molecular mass of 36 kDa after the peptide N-glycosidase F digestion, was found to be a novel protein. The result of cDNA cloning showed that the protein is an immunoglobulin superfamily member with three C2 domains and has six putative glycosylation sites. Since this protein shows high sequence similarity to IgLON family members including LAMP, OBCAM, neurotrimin, CEPU-1, AvGP50, and GP55, we termed this protein Kilon (a kindred of IgLON). Kilon-specific monoclonal antibodies were produced, and Western blotting analysis showed that expression of Kilon is restricted to brain, and Kilon has an apparent molecular mass of 46 kDa in SDS-polyacrylamide gel electrophoresis in its expressed form. In brain, the expression of Kilon is already detected in E16 stage, and its level gradually increases during development. Kilon immunostaining was observed in the cerebral cortex and hippocampus, in which the strongly stained puncta were observed on dendrites and soma of pyramidal neurons.  (+info)

Evidence for the existence of an unfolding intermediate state for aminoacylase during denaturation in guanidine solutions. (7/2620)

The equilibrium unfolding of pig kidney aminoacylase in guanidinium chloride (GdmCl) solutions was studied by following the fluorescence and circular dichroism (CD). At low concentrations of GdmCl, less than 1.0 M, the fluorescence intensity decreased with a slight red shift of the emission maximum (from 335 to 340 nm). An unfolding intermediate was observed in low concentrations of denaturant (between 1.2 and 1.6 M GdmCl). This intermediate was characterized by a decreased fluorescence emission intensity, a red-shifted emission maximum, and increased binding of the fluorescence probe 1-anilino-8-naphthalenesulfonate. No significant changes of the secondary structure were indicated by CD measurement. This conformation state is similar to a molten globule state which may exist in the pathway of protein folding. Further changes in the fluorescence properties occurred at higher concentrations of GdmCl, more than 1.6 M, with a decrease in emission intensity and a significant red shift of the emission maximum from 340 to 354 nm. In this stage, the secondary structure was completely broken. A study of apo-enzyme (Zn2+-free enzyme) produced similar results. However, comparison of the changes of the fluorescence emission spectra of native (Holo-) enzyme with Zn2+-free (Apo-) enzyme at low GdmCl concentrations showed that the structure of the Holo-enzyme was more stable than that of the Apo-enzyme.  (+info)

Processing of the fibrillin-1 carboxyl-terminal domain. (8/2620)

To investigate the processing and general properties of the fibrillin-1 carboxyl-terminal domain, three protein expression constructs have been developed as follows: one without the domain, one with the domain, and one with a mutation near the putative proteolytic processing site. The constructs have been expressed in two eukaryotic model systems, baculoviral and CHO-K1. Post-translational modifications that normally occur in fibrillin-1, including glycosylation, signal peptide cleavage, and carboxyl-terminal processing, occur in the three constructs in both cell systems. Amino-terminal sequencing of secreted protein revealed leader sequence processing at two sites, a primary site between Gly-24/Ala-25 and a secondary site of Ala-27/Asn-28. Processing of the carboxyl-terminal domain could be observed by migration differences in SDS-polyacrylamide gel electrophoresis and was evident in both mammalian and insect cells. Immunological identification by Western blotting confirmed the loss of the expected region. The failure of both cell systems to process the mutant construct shows that the multi-basic sequence is the site of proteolytic processing. Cleavage of the fibrillin-1 carboxyl-terminal domain occurred intracellularly in CHO-K1 cells in an early secretory pathway compartment as demonstrated by studies with secretion blocking agents. This finding, taken with the multi-basic nature of the cleavage site and observed calcium sensitivity of cleavage, suggests that the processing enzyme is a secretory pathway resident furin-like protease.  (+info)

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.

Amidohydrolases at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e (EC 3.5.1, EC 3.5.2, Hydrolases ... Amidohydrolases (or amidases) are a type of hydrolase that acts upon amide bonds. They are categorized under EC number EC 3.5.1 ... Due to its complexity and size, the amidohydrolase superfamily is being used by the Enzyme Function Initiative (EFI) for ... and 3.5.2. Examples include: Beta-lactamase Histone deacetylase Urease The amidohydrolase superfamily is a large protein family ...
... (EC 3.5.1.107, NicF) is an enzyme with systematic name maleamate amidohydrolase. This enzyme catalyses ... Maleamate+amidohydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.5.1). ...
In enzymology, a biuret amidohydrolase (EC 3.5.1.84) is an enzyme that catalyzes the chemical reaction biuret + H2O ⇌ {\ ... The systematic name of this enzyme class is biuret amidohydrolase. This enzyme participates in atrazine degradation. Cook AM, ...
In enzymology, a cyanuric acid amidohydrolase (EC 3.5.2.15) is an enzyme that catalyzes the chemical reaction cyanuric acid + ... The systematic name of this enzyme class is cyanuric acid amidohydrolase. This enzyme participates in atrazine degradation. ... "Cloning and comparison of the DNA encoding ammelide aminohydrolase and cyanuric acid amidohydrolase from three s-triazine- ...
Amidohydrolases are a type of hydrolase that acts upon amide bonds. All members of the amidohydrolase family employ a TIM ... Amidohydrolase enzymes can bind one, two, or three metal atoms in the active site. These metals can include Zn2+, Co2+, Fe2+, ... The systematic name of this enzyme class is N-acetyl-D-glucosamine-6-phosphate amidohydrolase. Other names in common use ... Liu A, Huo L (2014-08-15), John Wiley & Sons Ltd (ed.), "Amidohydrolase Superfamily", eLS, John Wiley & Sons, Ltd, doi:10.1002/ ...
Vogels GD (February 1966). "Reversible activation of allantoate amidohydrolase by acid-pretreatment and other properties of the ... This enzyme is also called allantoate amidohydrolase. This enzyme participates in purine metabolism. ...
The systematic name of this enzyme class is N-(long-chain-acyl)ethanolamine amidohydrolase. Other names in common use include N ... Schmid PC, Zuzarte-Augustin ML, Schmid HH (1985). "Properties of rat liver N-acylethanolamine amidohydrolase". J. Biol. Chem. ...
The domain is named after the acronym cysteine, histidine-dependent amidohydrolases/peptidases. Many of these proteins are ... L-glutamate-specific amidohydrolases". Trends Biochem. Sci. 28 (5): 230-4. doi:10.1016/s0968-0004(03)00062-8. PMID 12765833. ...
Ogawa J, Shimizu S, Yamada H (1993). "N-carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c purification and ...
... is a member of the urease-related amidohydrolases, the family of hydrolases, those acting on carbon-nitrogen bonds ... The systematic name of this enzyme class is creatinine amidohydrolase. This enzyme is also called creatinine hydrolase. This ... PDB: 3NO4​; Joint Center for Structural Genomics (2010). "Crystal structure of a creatinine amidohydrolase (Npun_F1913) from ... "Cloning of the creatinine amidohydrolase gene from Pseudomonas sp. PS-7". Biosci. Biotechnol. Biochem. 59 (7): 1331-1332. doi: ...
L-asparagine amidohydrolase) is an enzyme with systematic name N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase. ... Mahadevan S, Tappel AL (October 1967). "Beta-aspartylglucosylamine amido hydrolase of rat liver and kidney". The Journal of ... Tarentino AL, Maley F (March 1969). "The purification and properties of a beta-aspartyl N-acetylglucosylamine amidohydrolase ... "Purification and properties of 4-L-aspartylglycosylamine amidohydrolase from hog kidney". Biochimica et Biophysica Acta (BBA ...
This enzyme is also called glutathionylspermidine amidohydrolase (spermidine-forming). This enzyme participates in glutathione ...
The systematic name of this enzyme class is N-formyl-L-glutamate amidohydrolase. Other names in common use include beta-citryl- ... Hu L, Mulfinger LM, Phillips AT (1987). "Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida ... beta-citryl-L-glutamate amidohydrolase, beta-citryl-L-glutamate amidase, beta-citrylglutamate amidase, and beta-citryl-L- ...
"Entrez Gene: ASAH1 N-acylsphingosine amidohydrolase (acid ceramidase) 1". Zhou J, Tawk M, Tiziano FD, Veillet J, Bayes M, ...
... (EC 3.5.2.1) is a zinc-containing amidohydrolase. Its systemic name is barbiturate amidohydrolase (3-oxo-3- ... Although grouped into the naturally existing amidohydrolases, it demonstrates more homology with cyanuric acid amidohydrolase. ... Unlike other zinc containing amidohydrolases, the zinc binding motif of barbiturase is found on the carboxylic acid terminus, ... Soong CL, Ogawa J, Sakuradani E, Shimizu S (March 2002). "Barbiturase, a novel zinc-containing amidohydrolase involved in ...
"Entrez Gene: ASAHL N-acylsphingosine amidohydrolase (acid ceramidase)-like". Human NAAA genome location and NAAA gene details ...
Holm L, Sander C (1997). "An evolutionary treasure: unification of a broad set of amidohydrolases related to urease". Proteins ... Ureases (EC 3.5.1.5), functionally, belong to the superfamily of amidohydrolases and phosphotriesterases. Ureases are found in ...
The systematic name of this enzyme class is D-glutamine amidohydrolase. This enzyme participates in d-glutamine and d-glutamate ... Domnas A, Catimo EC (1965). "The behavior of amidohydrolases and L-glutamate in synchronized populations of Blastocladiella ...
"Entrez Gene: ASAH2 N-acylsphingosine amidohydrolase (non-lysosomal ceramidase) 2". Human ASAH2 genome location and ASAH2 gene ...
The systematic name of this enzyme class is pentanamide amidohydrolase. This enzyme is also called valeramidase. Friedrich CG, ...
The systematic name of this enzyme class is acylamide amidohydrolase. Other names in common use include acylamidase, acylase, ... In enzymology, an amidase (EC 3.5.1.4, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), ... amidohydrolase, deaminase, fatty acylamidase, and N-acetylaminohydrolase. This enzyme participates in 6 metabolic pathways: ...
The systematic name of this enzyme class is nicotinamide-D-ribonucleotide amidohydrolase. Other names in common use include NMN ... Imai T (January 1973). "Purification and properties of nicotinamide mononucleotide amidohydrolase from Azotobacter vinelandii ... deamidase, nicotinamide mononucleotide deamidase, and nicotinamide mononucleotide amidohydrolase. This enzyme participates in ...
The systematic name of this enzyme class is chenodeoxycholoyltaurine amidohydrolase. This enzyme participates in bile acid ...
The systematic name of this enzyme class is N-carbamoylputrescine amidohydrolase. Other names in common use include ... Yanagisawa H, Suzuki Y (1982). "Preparation and properties of N-carbamylputrescine amidohydrolase from maize shoots". ...
The systematic name of this enzyme class is penicillin amidohydrolase. Other names in common use include penicillin acylase, ...
The systematic name of this enzyme class is benzoylagmatine amidohydrolase. Other names in common use include acylagmatine ... hydrolysis of bleomycin B2 by a Fusarium acylagmatine amidohydrolase". The Journal of Antibiotics. 26 (2): 117-9. doi:10.7164/ ... amidohydrolase, and acylagmatine deacylase. Umezawa H, Takahashi Y, Fujii A, Saino T, Shirai T (February 1973). "Letter: ...
The systematic name of this enzyme class is mimosine amidohydrolase. Known to occur in all Leucaena and Mimosa. Negi & ...
The systematic name of this enzyme class is formamide amidohydrolase. This enzyme participates in glyoxylate and dicarboxylate ...
The systematic name of this enzyme class is peptidoglycan amidohydrolase. Other names in common use include acetylmuramyl-L- ...
The systematic name of this enzyme class is adenosylcobinamide amidohydrolase. Other names in common use include CbiZ, and ... Woodson JD, Escalante-Semerena JC (2004). "CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor ... AdoCbi amidohydrolase. This enzyme participates in porphyrin and chlorophyll metabolism. ...
Amidohydrolases at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e (EC 3.5.1, EC 3.5.2, Hydrolases ... Amidohydrolases (or amidases) are a type of hydrolase that acts upon amide bonds. They are categorized under EC number EC 3.5.1 ... Due to its complexity and size, the amidohydrolase superfamily is being used by the Enzyme Function Initiative (EFI) for ... and 3.5.2. Examples include: Beta-lactamase Histone deacetylase Urease The amidohydrolase superfamily is a large protein family ...
The amidohydrolases of this pathway are responsible for both the ring opening of dihydrouracil and dihydrothymine ( ... dihydropyrimidine amidohydrolase) and the hydrolysis of N-carba … ... with dihydropyrimidine amidohydrolase belonging to the amidohydrolase superfamily while the beta-alanine synthase from higher ... The amidohydrolases of this pathway are responsible for both the ring opening of dihydrouracil and dihydrothymine ( ...
This plant enzyme is involved in the degradation of ureidoglycolate, an intermediate of purine degradation ...
"Amidohydrolases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "Amidohydrolases" by people in this website by year, and ... Below are the most recent publications written about "Amidohydrolases" by people in Profiles. ... whether "Amidohydrolases" was a major or minor topic of these publications. To see the data from this visualization as text, ...
Amidohydrolases * Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase * GTP-Binding Proteins ...
Amidohydrolases [genetics] *Arginine [analogs & derivatives] [metabolism] *Biological Availability. *Cardiovascular Diseases [ ...
creatinine amidohydrolase: ABCDEF. SMTL:PDB. SMTL Chain Id:. PDB Chain Id:. A. A ...
MexAM1_META1p3487 6828386 N-formylglutamate amidohydrolase (Beta-citryl-L-glutamate hydrolase) (RefSeq). × Error message. * ...
Schnackerz KD, Dobritzsch D. Amidohydrolases of the reductive pyrimidine catabolic pathway purification, characterization, ...
Amidohydrolases / metabolism * Animals * Aquatic Organisms / microbiology * Bacteria / metabolism* * Bacterial Proteins / ...
Amidohydrolase. Hydrolase. 17. NA. group_6430. Putative restriction enzyme. Restriction enzyme. 17. NA. ...
Abbreviations: Akt, Protein kinase-B; ASAH1, N-acylsphingosine amidohydrolase; cAMP, cyclic adenosine monophosphate; EGFR, ... Abbreviations: Akt, Protein kinase-B; ASAH1, N-acylsphingosine amidohydrolase; cAMP, cyclic adenosine monophosphate; EGFR, ...
Categories: Amidohydrolases Image Types: Photo, Illustrations, Video, Color, Black&White, PublicDomain, CopyrightRestricted 28 ...
Pfam PF04909; Amidohydrolase; stand-alone domain. *. Protein 4-oxalomesaconate hydratase LigJ [141826] (1 species). ...
Pfam PF04909; Amidohydrolase; stand-alone domain. More info for Superfamily c.1.9: Metallo-dependent hydrolases. Timeline for ...
MeSH Terms: Acetylation/drug effects; Amidohydrolases/metabolism*; Animals; Cell Line, Tumor; Dexamethasone/pharmacology; ...
A novel amidohydrolase (DmhA) from Sphingomonas sp. that can hydrolyze the organophosphorus pesticide dimethoate to dimethoate ... For instance, a histone deacetylase-like amidohydrolase clustered together with the APAP-degrading amidase DmhA, suggesting its ... ", "amidohydrolase", and "amidotransferase" terms in the annotated metagenome. The highly-expressed and uncharacterized amidase ...
Homology searches reveled that the IAA-asp hydrolase was similar to a variety of amidohydrolases. In addition, IAA-asp ...
Dihydrouracil amidohydrolase deficiency, see Dihydropyrimidinase deficiency. *Dilated cardiomyopathy 3B, see X-linked dilated ...
Amidohydrolases / analysis Actions. * Search in PubMed * Search in MeSH * Add to Search ...
N-acylsphingosine amidohydrolase 2. Focal adhesion sites. VCL Vinculin. Focal adhesion sites. ...
Formation of 6-APA from IPN by Isopenicillin N Amidohydrolase (IAH). r. 3. =. k. 3. X. I. A. H. C. I. P. N. C. I. P. N. +. K. I ...
Pegaspargase is a conjugate of monomethoxypolyethylene glycol (mPEG) and L-asparaginase (L-asparagine amidohydrolase), an ...
Entwicklung und Charakterisierung einer photoschaltbaren Histondeacetylase-ähnlichen Amidohydrolase. Technische Universität. Ph ...
L-theanine amidohydrolase; 5-N-ethyl-L-glutamine amidohydrolase. Systematic name: N5-ethyl-L-glutamine amidohydrolase. ...
Amidohydrolases,N0000007690, Propoxyphene,N0000007689, Propoxycaine,N0000007688, Zinc Compounds,N0000007687, ...
... the anandamide transporter and fatty acid amidohydrolase.. Reggio PH; Traore H. Chem Phys Lipids; 2000 Nov; 108(1-2):15-35. ...
... followed the pattern of the known amidohydrolase [29]. Ice worm AMPD, which contains 26 predicted helices and strands, ...
... a novel cobalt-dependent amidohydrolase. Journal of Bacteriology, 193(20), 5810 - 5816.*Google Scholar ...
WH7805 requires urease (urea amidohydrolase, EC 3.5.1.5) to utilize urea as a nitrogen source: molecular genetic and ...
  • Amidohydrolases (or amidases) are a type of hydrolase that acts upon amide bonds. (wikipedia.org)
  • 2011). Gulosibacter molinativorax ON4 T molinate hydrolase, a novel cobalt-dependent amidohydrolase . (up.pt)
  • Fatty acid amide hydrolase , (FAAH, Oleamide hydrolase, Anandamide amidohydrolase), is an integral membrane protein that hydrolyzes bioactive amides, including anandamide , to free fatty acid and ethanolamine. (tocris.com)
  • Examples include: Beta-lactamase Histone deacetylase Urease The amidohydrolase superfamily is a large protein family of more than 20,000 members with diverse chemistry and physiologic roles. (wikipedia.org)
  • Due to its complexity and size, the amidohydrolase superfamily is being used by the Enzyme Function Initiative (EFI) for developing a large-scale strategy for functional assignment of unknown proteins. (wikipedia.org)
  • Structural and Functional Characterization of the Ureidoacrylate Amidohydrolase RutB from Escherichia coli . (bvsalud.org)
  • Salopek Sondi, Branka (2016) The role of conserved Cys residues in Brassica rapa auxin amidohydrolase: Cys139 is crucial for the enzyme activity and Cys320 regulates enzyme stability . (irb.hr)
  • Brassica rapa auxin amidohydrolase (BrILL2) participates in the homeostasis of the plant hormones auxins by hydrolyzing the amino acid conjugates of auxins, thereby releasing the free active form of hormones. (irb.hr)
  • The amidohydrolases of this pathway are responsible for both the ring opening of dihydrouracil and dihydrothymine (dihydropyrimidine amidohydrolase) and the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate (beta-alanine synthase). (nih.gov)
  • The two amidohydrolases of the reductive pyrimidine catabolic pathway have unrelated folds, with dihydropyrimidine amidohydrolase belonging to the amidohydrolase superfamily while the beta-alanine synthase from higher eukaryotes belongs to the nitrilase superfamily. (nih.gov)
  • Due to its complexity and size, the amidohydrolase superfamily is being used by the Enzyme Function Initiative (EFI) for developing a large-scale strategy for functional assignment of unknown proteins. (wikipedia.org)
  • WH7805 requires urease (urea amidohydrolase, EC 3.5.1.5) to utilize urea as a nitrogen source: molecular genetic and biochemical analysis of the enzyme. (springer.com)
  • Among them is the amidohydrolase domain containing 1 (AMDHD1) gene, which encodes an enzyme involved in the catabolism of histidine. (nih.gov)
  • Identification of the N-acylsphingosine amidohydrolase 1 gene (ASAH1) for susceptibility to schizophrenia in a Han Chinese population. (cdc.gov)
  • 11. Conformational requirements for endocannabinoid interaction with the cannabinoid receptors, the anandamide transporter and fatty acid amidohydrolase. (nih.gov)
  • Amidohydrolases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (jefferson.edu)
  • This rule also handles the 5-nitroanthranilate amidohydrolase reaction, which might include a transient benzoquinone intermediate, based on Qu and Spain (2010) . (ethz.ch)
  • This graph shows the total number of publications written about "Amidohydrolases" by people in this website by year, and whether "Amidohydrolases" was a major or minor topic of these publications. (jefferson.edu)