Allantoin
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Internet
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Proteins
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
Polyunsaturated Alkamides
Amides composed of unsaturated aliphatic FATTY ACIDS linked with AMINES by an amide bond. They are most prominent in ASTERACEAE; PIPERACEAE; and RUTACEAE; and also found in ARISTOLOCHIACEAE; BRASSICACEAE; CONVOLVULACEAE; EUPHORBIACEAE; MENISPERMACEAE; POACEAE; and SOLANACEAE. They are recognized by their pungent taste and for causing numbing and salivation.
Endocannabinoids
Receptors, Cannabinoid
A class of G-protein-coupled receptors that are specific for CANNABINOIDS such as those derived from CANNABIS. They also bind a structurally distinct class of endogenous factors referred to as ENDOCANNABINOIDS. The receptor class may play a role in modulating the release of signaling molecules such as NEUROTRANSMITTERS and CYTOKINES.
Phenylmethylsulfonyl Fluoride
Cannabinoids
Herbicides
Comamonadaceae
Glutamine
Methionyl Aminopeptidases
Amino Acid Sequence
Proline
Aminoacyltransferases
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.
Glutamate-Ammonia Ligase
GTP Cyclohydrolase
(GTP cyclohydrolase I) or GTP 7,8-8,9-dihydrolase (pyrophosphate-forming) (GTP cyclohydrolase II). An enzyme group that hydrolyzes the imidazole ring of GTP, releasing carbon-8 as formate. Two C-N bonds are hydrolyzed and the pentase unit is isomerized. This is the first step in the synthesis of folic acid from GTP. EC 3.5.4.16 (GTP cyclohydrolase I) and EC 3.5.4.25 (GTP cyclohydrolase II).
Riboflavin
Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. The richest natural source is yeast. It occurs in the free form only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as FLAVIN MONONUCLEOTIDE and FLAVIN-ADENINE DINUCLEOTIDE.
Encyclopedias as Topic
Pimelic Acids
MedlinePlus
Carbon
Sarcina
Penicillins
A group of antibiotics that contain 6-aminopenicillanic acid with a side chain attached to the 6-amino group. The penicillin nucleus is the chief structural requirement for biological activity. The side-chain structure determines many of the antibacterial and pharmacological characteristics. (Goodman and Gilman's The Pharmacological Basis of Therapeutics, 8th ed, p1065)
Pseudomonas aeruginosa
Penicillin G
A penicillin derivative commonly used in the form of its sodium or potassium salts in the treatment of a variety of infections. It is effective against most gram-positive bacteria and against gram-negative cocci. It has also been used as an experimental convulsant because of its actions on GAMMA-AMINOBUTYRIC ACID mediated synaptic transmission.
Bacillus megaterium
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)
6DY2 | GUINEA PIG N-ACYLETHANOLAMINE-HYDROLYZING ACID AMIDASE (NAAA) COVALENTLY BOUND TO BETA-LACTAM INHIBITOR ARN726 | 6DY2 B ...
ASAHL/N-acylethanolamine-hydrolyzing Acid Amidase Antibody (AF4886): Novus Biologicals
Vascular endothelial-specific dimethylarginine dimethylaminohydrolase-1- deficient mice reveal that vascular endothelium plays...
N-acylethanolamine-hydrolyzing acid amidase
Sphingolipid Ceramide N-Deacylase | SCDase | Sphingolipid Hydrolysis
Sphingolipid Ceramide N-Deacylase | SCDase | Sphingolipid Hydrolysis
Localization of the endocannabinoid-degrading enzyme fatty acid amide hydrolase in rat dorsal root ganglion cells and its...
Dimethylarginine dimethylaminohydrolase and endothelial dysfunction in failing hearts<...
Fatty Acid Amide Hydrolase Inhibitors - Progress and Potential by Ish K. Khanna and Christopher W. Alexander
The fatty acid amide hydrolase inhibitor URB597 exerts anti-inflammatory effects in hippocampus of aged rats and restores an...
Activation of TRPA1 Channels by the Fatty Acid Amide Hydrolase Inhibitor 3 -Carbamoylbiphenyl-3-yl - Semantic Scholar
Fatty Acid Amide Hydrolase in Prostate Cancer: Association with Disease Severity and Outcome, CB1 Receptor Expression and...
Lanopepden camsylate | CAS#1441390-28-8 | peptide deformylase inhibitor| MedKoo
Fatty Acid Amide Hydrolase | Metabolic Enzyme|Neuronal Signaling| CSNpharm
N(G),N(G)-dimethylarginine dimethylaminohydrolase 1
Fatty acid amide hydrolase ablation promotes ectopic lipid storage and insulin resistance due to centrally mediated...
科研成果 by Type: 期刊论文 | 胡新立
PDF peptide deformylase, mitochondrial [Homo sapiens (human)] - Gene - NCBI
OPUS 4 | Search
OPUS 4 | Search
The endocannabinoid system : drug targets, lead compounds, and potential therapeutic applications.
Specific Lowering of Asymmetric Dimethylarginine by Pharmacological Dimethylarginine Dimethylaminohydrolase Improves...
Recent Process in the Inhibitors of UDP-3-O-(R-3-hydroxyacyl)-Nacetylglucosamine Deacetylase (LpxC) Against Gram-Negative...
DDAH2 - N(G),N(G)-dimethylarginine dimethylaminohydrolase 2 - Homo sapiens (Human) - DDAH2 gene & protein
Dimethylarginine dimethylaminohydrolase activity modulates ADMA levels, VEGF expression, and cell phenotype - UCL Discovery
Bile Salt Hydrolase, Chinaîn Hilberên Hîdrolase ya Siltanê Bile, Hilberîner, Bazirgan - Hunan Nanbeiwang Teknolojiya Biyolojîk...
Urease from Bacteria, Recombinant(EC 3.5.1.5) - Creative Enzymes
Author: VAN DER KAMP, MARC W. - PubAg Search Results
Synthesis and antibacterial activity of peptide deformylase inhibitors. - PubMed - NCBI
Dylan Kim | In Vitro Activities of Peptide Deformylase Inhibitors
In Vitro Activities of Peptide Deformylase Inhibitors
Functional Characterization of Plant Fatty Acid Amide Hydrolases - Digital Library
Dimethylarginine Dimethylaminohydrolase Regulates Nitric Oxide Synthesis | Circulation
Infection Is Associated with Impaired Hepatic Dimethylarginine Dimethylaminohydrolase Activity and Disruption of Nitric Oxide...
The Role of Dimethylarginine Dimethylaminohydrolase in Idiopathic Pulmonary Fibrosis | Science Translational Medicine
B. smithii RAPc8 amidase - SBRU
Discovery of potent, non-carbonyl inhibitors of fatty acid amide hydrolase (FAAH)
Inactivation of fatty acid amide hydrolase exacerbates experimental fibrosis by enhanced endocannabinoid-mediated activation of...
Fatty Acid Amide Hydrolase
Orexin1 Receptors | PARP inhibitor BMN-673 targeting of the mutant p53-PARP-MCM chromatin axis
Discovery of PF-04457845: A Highly Potent, Orally Bioavailable, and Selective Urea FAAH Inhibitor - PubMed
Assessment of the direct effects of DDAH I on tumour angiogenesis in vivo.
Crystallization and Structure of a Plant Peptide Deformylase by Robert L. Houtz, David W. Rodgers et al.
Metabolism of asymmetric dimethylarginines is regulated in the lung developmentally and with pulmonary hypertension induced by...
The association of dimethylarginine dimethylaminohydrolase 1 gene polymorphism with type 2 diabetes: a cohort study |...
Germination-specific N-acetylmuramoyl-L-alanine amidase elisa and antibody
Zinc in the structure of Crystal Structure Of Mutant R322A of Beta-Alanine Synthase From Saccharomyces Kluyveri (pdb 2v8v)
Aspartoacylase deficiency legal definition of Aspartoacylase deficiency
Domain combinations for Peptide deformylase superfamily in Mycoplasma penetrans HF-2
Role of arginine residues of D-aminoacylase from Alcaligenes x...
Fegley, D., Gaetani, S., Duranti, A., Tontini, A., Mor, M. and Tarzia, G. (2005) Characterization of the fatty acid amide...
Biomolecules | Free Full-Text | Tackling Critical Catalytic Residues in Helicobacter pylori L-Asparaginase
Novel amidases of two Aminobacter sp. strains: Biotransformation experiments and elucidation of gene sequences | AMB Express |...
Novel amidases of two Aminobacter sp. strains: Biotransformation experiments and elucidation of gene sequences | AMB Express |...
FAAH inhibitor 1 (Benzothiazole analog 3) | FAAH Inhibitor | MedChemExpress
Expression studies of Bacillus licheniformis chitin deacetylase in E. coli Rosetta cells<...
Inserting a Mutation into the Putative Clostridium difficile Bile Salt Hydrolase-Encoding Gene
Chloramphenicol and Ampicillin-Induced Changes in Rat Hepatic Esterase and Amidase Activities | Bioscience Reports | Portland...
Amide Utilization in Aspergillus nidulans: Evidence for a Third Amidase Enzyme | Microbiology Society
Publications - Professor Anthony Gordon
Unscramble acetanilid | Words unscrambled from letters acetanilid | Scrabble Word acetanilid | Words Made with the Letters...
RCSB PDB
- 1N5N: Crystal Structure of Peptide Deformylase from Pseudomonas aeruginosa Literature Report Page
RCSB PDB
- 1LME: Crystal Structure of Peptide Deformylase from Thermotoga maritima Literature Report Page
Pesquisa | Portal Regional da BVS
Analgesic trial ends in death | Australian Doctor Group
Rabbit polyclonal to PNLIPRP3 | Syntheses, Structures and Antibiotic Activities of LpxC Inhibitors
EC 3.5.1.88
NDST2 overexpression lysate - LY418535 | acris-antibodies.com
Rabbit Polyclonal to GABRA6. | Syntheses, Structures and Antibiotic Activities of LpxC Inhibitors
Amidase - Wikipedia
ADMA(Asymmetrical Dimethylarginine) ELISA Kit - ADMA(Asymmetrical Dimethylarginine) ELISA Kit Exporter, Importer, Manufacturer,...
RCSB PDB - 7D6Z: Molecular model of the cryo-EM structure of 70S ribosome in complex with peptide deformylase and trigger factor
Asymmetric Dimethylarginine, L-Arginine, and Endothelial Dysfunction in Essential Hypertension | JACC: Journal of the American...
Glycoproteomic Analysis of Prostate Cancer Tissues by SWATH Mass Spectrometry Discovers N-acylethanolamine Acid Amidase and...
Plus it
Amidases(AMD): synthesis of chiral carboxylic acids and amides,Enzyme,Syncozymes (Shanghai) Co
Plasma concentrations of asymmetric dimethylarginine are increased in patients with type 2 diabetes mellitus
Acetic Acid Amide
EMBOSS: featcopy
EMBOSS: sixpack
Computational Complexity: Amir Pnueli (1941-2009)
PATCH v2 0/5] Nested overlay tests
1228362-74-0 | 5-Methyl-4-nitro-2H-pyrazole-3-carboxylic acid amide | MolCore
Sotrastaurin | FAAH inhibitors in the limelight
Dictamnine IC50 | FAAH inhibitors in the limelight
NWMN RS14730 - AureoWiki
Dr Amir Shirzadi | OU people profiles
Protocols and Video Articles Authored by Amir Segev
Dr. Amir Gerges, DO - Prescott, AZ - Nephrology | Healthgrades.com
GTP cyclohydrolase II
Thus, the two substrates of this enzyme are GTP and H2O, whereas its 3 products are formate, 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine, and diphosphate.. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is GTP 7,8-8,9-dihydrolase (diphosphate-forming). Other names in common use include guanosine triphosphate cyclohydrolase II, and GTP-8-formylhydrolase. This enzyme participates in riboflavin metabolism.. ...
Succinyl-diaminopimelate desuccinylase
The systematic name of this enzyme class is N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase. This enzyme is also called N ...
HDAC4
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to class II of the histone deacetylase/acuc/apha family. It possesses histone deacetylase activity and represses transcription when tethered to a promoter. This protein does not bind DNA directly but through transcription factors MEF2C and MEF2D. It seems to interact in a multiprotein complex with RbAp48 and HDAC3.[7] Furthermore, HDAC4 is required for TGFbeta1-induced myofibroblastic differentiation.[8] ...
Adenozilkobinamidna hidrolaza
Woodson, J.D. and Escalante-Semerena, J.C. (2004). "CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 ...
Multiregionalno podrijetlo modernih ljudi - Wikipedija
"Population Genetic Analysis of the N-Acylsphingosine Amidohydrolase Gene Associated With Mental Activity in Humans". Genetics ...
Multiregional origin of modern humans
"Population Genetic Analysis of the N-Acylsphingosine Amidohydrolase Gene Associated With Mental Activity in Humans" (Free full ...
N-acetylglucosamine-6-phosphate deacetylase
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/ ...
Allantoate deiminase
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. ...
N-(long-chain-acyl)ethanolamine deacylase
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. ...
CHAP domain
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. ...
N-carbamoyl-D-amino acid hydrolase
Ogawa J, Shimizu S, Yamada H (1993). "N-carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c purification and ...
Creatininase
... is a member of the urease-related amidohydrolases, the family of hydrolases, those acting on carbon-nitrogen bonds ... Cite journal requires ,journal= (help) Yamamoto K, Oka M, Kikuchi T, Emi S (1995). "Cloning of the creatinine amidohydrolase ... 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 ...
N4-(beta-N-acetylglucosaminyl)-L-asparaginase
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 ...
Glutathionylspermidine amidase
This enzyme is also called glutathionylspermidine amidohydrolase (spermidine-forming). This enzyme participates in glutathione ...
N-formylglutamate deformylase
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- ...
ASAH1
"Entrez Gene: ASAH1 N-acylsphingosine amidohydrolase (acid ceramidase) 1". Zhou J, Tawk M, Tiziano FD, Veillet J, Bayes M, ...
Barbiturase
... (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 ...
ASAHL
"Entrez Gene: ASAHL N-acylsphingosine amidohydrolase (acid ceramidase)-like". Human NAAA genome location and NAAA gene details ...
Urease
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 ...
D-glutaminase
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 ...
ASAH2
"Entrez Gene: ASAH2 N-acylsphingosine amidohydrolase (non-lysosomal ceramidase) 2". Human ASAH2 genome location and ASAH2 gene ...
Pentanamidase
The systematic name of this enzyme class is pentanamide amidohydrolase. This enzyme is also called valeramidase. Friedrich CG, ...
Amidase
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: ...
Nicotinamide-nucleotide amidase
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 ...
Chenodeoxycholoyltaurine hydrolase
The systematic name of this enzyme class is chenodeoxycholoyltaurine amidohydrolase. This enzyme participates in bile acid ...
Penicillin amidase
The systematic name of this enzyme class is penicillin amidohydrolase. Other names in common use include penicillin acylase, ...
Acylagmatine amidase
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: ...
Mimosinase
The systematic name of this enzyme class is mimosine amidohydrolase. Tangendjaja B, Lowry JB, Wills RH (1986). "Isolation of a ...
Formamidase
The systematic name of this enzyme class is formamide amidohydrolase. This enzyme participates in glyoxylate and dicarboxylate ...
N-acetylmuramoyl-L-alanine amidase
The systematic name of this enzyme class is peptidoglycan amidohydrolase. Other names in common use include acetylmuramyl-L- ...
Amidohydrolase - Wikipedia
Amidohydrolases (or amidases) are a type of hydrolase that acts upon amide bonds. They are categorized under EC number EC 3.5.1 ... Biology portal Aminohydrolases Amidohydrolases at the US National Library of Medicine Medical Subject Headings (MeSH) ... Amidohydrolase Overview from the EFI[permanent dead link] v t e. ... Beta-lactamase Histone deacetylase Urease The amidohydrolase ...
Maleamate amidohydrolase - Wikipedia
Amidohydrolase dictionary definition | amidohydrolase defined
... plural amidohydrolases) 1. Any of a class of hydrolases that act upon amide bonds. ... ... amidohydrolase. Noun (countable and uncountable, plural amidohydrolases). *Any of a class of hydrolases that act upon amide ... How would you define amidohydrolase? Add your definition here.. Please enable JavaScript to view the comments powered by Disqus ...
creatinine amidohydrolase (creatininase) protein [Rhizobium etli CFN 4 - Protein - NCBI
AMDHD1 amidohydrolase domain containing 1 [Homo sapiens (human)] - Gene - NCBI
AMDHD1 amidohydrolase domain containing 1 [Homo sapiens] AMDHD1 amidohydrolase domain containing 1 [Homo sapiens]. Gene ID: ... amidohydrolase domain containing 1provided by HGNC. Primary source. HGNC:HGNC:28577 See related. Ensembl:ENSG00000139344 Gene ... AMDHD1 amidohydrolase domain containing 1 [ Homo sapiens (human) ] Gene ID: 144193, updated on 24-Nov-2020 ... HutI; Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism]. cd01296. ...
RCSB PDB - Protein Feature View
- Allantoate amidohydrolase - P77425 (ALLC ECOLI)
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
RCSB PDB - 3NUR: Crystal structure of a putative amidohydrolase from Staphylococcus aureus
Amidohydrolase. A. 357. Staphylococcus aureus. Mutation(s): 0 Gene Names: SAOG_01574, SAV2580. EC: 3.5.1. ... Crystal structure of a putative amidohydrolase from Staphylococcus aureus. Qiu, W., Lam, R., Romanov, V., Lam, K., Soloveychik ... Crystal structure of a putative amidohydrolase from Staphylococcus aureus. *DOI: 10.2210/pdb3NUR/pdb ...
Distribution of anandamide amidohydrolase in rat tissues with special reference to small intestine
... is hydrolyzed by an amidohydrolase and its biological activity is lost. Previously, we partially purified the enzyme from ... Distribution of anandamide amidohydrolase in rat tissues with special reference to small intestine Biochim Biophys Acta. 1997 ... Anandamide (arachidonylethanolamide), an endogenous ligand for cannabinoid receptors, is hydrolyzed by an amidohydrolase and ...
WDYHV1 - Protein N-terminal glutamine amidohydrolase - Homo sapiens (Human) - WDYHV1 gene & protein
Protein N-terminal glutamine amidohydrolase (EC:3.5.1.122By similarity. Manual assertion inferred from sequence similarity toi ... "Crystal structure of human protein N-terminal glutamine amidohydrolase, an initial component of the N-end rule pathway.". Park ... sp,Q96HA8,NTAQ1_HUMAN Protein N-terminal glutamine amidohydrolase OS=Homo sapiens OX=9606 GN=WDYHV1 PE=1 SV=2 ...
Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida. | Journal of Bacteriology
Plants | Free Full-Text | Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to...
Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis by Beatriz ... "Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis." Plants 3, ... Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis. Plants 2014 ... Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis. Plants. 2014 ...
cbiZ - Adenosylcobinamide amidohydrolase - Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) - cbiZ gene &...
Adenosylcobinamide amidohydrolaseAdd BLAST. 231. Proteomic databases. PaxDb, a database of protein abundance averages across ... "CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor cobinamide in archaea.". Woodson J.D., ... Adenosylcobinamide amidohydrolase (EC:3.5.1.90*Search proteins in UniProtKB for this EC number. ... sp,Q9HPK9,CBIZ_HALSA Adenosylcobinamide amidohydrolase OS=Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) OX= ...
Target Selection and Annotation for the Structural Genomics of the Amidohydrolase and Enolase Superfamilies
... we use the amidohydrolase and enolase superfamilies as model systems; members of these superfamilies share a common TIM barrel ... Target Selection and Annotation for the Structural Genomics of the Amidohydrolase and Enolase Superfamilies J Struct Funct ... To study the substrate specificity of enzymes, we use the amidohydrolase and enolase superfamilies as model systems; members of ... To date, 20 unique amidohydrolase and 41 unique enolase structures have been determined, increasing the fraction of sequences ...
AMDHD1 (amidohydrolase domain containing 1) - KOMP (Knockout Mouse Project)
Frontiers | Structural Investigations of N-carbamoylputrescine Amidohydrolase from Medicago truncatula: Insights into the...
In the final reaction, N-carbamoylputrescine is hydrolyzed to putrescine by N-carbamoylputrescine amidohydrolase (CPA, EC 3.5. ... In the final reaction, N-carbamoylputrescine is hydrolyzed to putrescine by N-carbamoylputrescine amidohydrolase (CPA, EC 3.5. ... 2000). Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases. ... N-carbamoylputrescine amidohydrolase enzymes belong to nitrilases, and more precisely, to C-N hydrolases breaking non-peptide ...
Characterization of the phenylurea hydrolases A and B: founding members of a novel amidohydrolase subgroup | Biochemical Journal
Characterization of the phenylurea hydrolases A and B: founding members of a novel amidohydrolase subgroup. Jeevan L. Khurana, ... Sequence analysis showed that these enzymes belong to the metal-dependent amidohydrolase superfamily, although they contain a ... Characterization of the phenylurea hydrolases A and B: founding members of a novel amidohydrolase subgroup ... Characterization of the phenylurea hydrolases A and B: founding members of a novel amidohydrolase subgroup ...
ClyJ Is a Novel Pneumococcal Chimeric Lysin with a Cysteine- and Histidine-Dependent Amidohydrolase/Peptidase Catalytic Domain ...
By fusing GPB to the CHAP (cysteine, histidine-dependent amidohydrolase/peptidase) catalytic domain of the PlyC lysin, we ... ClyJ Is a Novel Pneumococcal Chimeric Lysin with a Cysteine- and Histidine-Dependent Amidohydrolase/Peptidase Catalytic Domain ... ClyJ Is a Novel Pneumococcal Chimeric Lysin with a Cysteine- and Histidine-Dependent Amidohydrolase/Peptidase Catalytic Domain ... CHAP, cysteine, histidine-dependent amidohydrolases/peptidases; PlyCA CHAP, the CHAP domain from PlyCA (amino acids 314 to 465 ...
Allantoate amidohydrolase elisa and antibody
Recombinant Protein and Allantoate amidohydrolase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody ... Allantoate amidohydrolase. Allantoate amidohydrolase ELISA Kit. Allantoate amidohydrolase Recombinant. Allantoate ... Below are the list of possible Allantoate amidohydrolase products. If you cannot find the target and/or product is not ... Also known as Allantoate amidohydrolase (Allantoate deiminase).. Escherichia coli is able to utilize allantoin as a sole ...
Protein N-terminal glutamine amidohydrolase
Substrate specificity and function of acetylpolyamine amidohydrolases from Pseudomonas aeruginosa
N-acylsphingosine amidohydrolase 1 - Target Profiles - BCIQ
For the biopharma industry investment, business development and competitive intelligence professionals who require information to support financing, partnering and licensing activities, BCIQ provides accurate information and context to support profitable and strategic decision making. Unlike other intelligence solutions, BCIQ exclusively supports the unique needs of the biopharma industry and provides in-depth, integrated analysis and context on clinical, strategic, financial, regulatory and policy issues.
Q2RGM7 | Moth 2120 | Cyanuric acid amidohydrolase | Druggability | Cancer
Creatinine amidohydrolase, 150 units/mg solid, 250 U - JuniperLifeSciences
GTP cyclohydrolase II - Wikipedia
Thus, the two substrates of this enzyme are GTP and H2O, whereas its 3 products are formate, 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine, and diphosphate.. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is GTP 7,8-8,9-dihydrolase (diphosphate-forming). Other names in common use include guanosine triphosphate cyclohydrolase II, and GTP-8-formylhydrolase. This enzyme participates in riboflavin metabolism.. ...
Succinyl-diaminopimelate desuccinylase - Wikipedia
NAVER Academic | Penicillin amidohydrolase productivity of locally isolated bacterial species
Penicillin amidohydrolase productivity of four locally isolated bacterial species is described. Organisms were identified ... Penicillin amidohydrolase productivity of locally isolated bacterial species. Author. Z. A. Mahmood, D. Shaikh, S. M. S. Zoha. ... Penicillin amidohydrolase productivity of four locally isolated bacterial species is described. Organisms were identified ...
Substrate specificity and function of acetylpolyamine amidohydrolases from Pseudomonas aeruginosa | BMC Biochemistry | Full Text
... all three putative acetylpolyamine amidohydrolases (APAHs) from P. aeruginosa have been expressed in enzymatic active form. The ... A new amidohydrolase from Bordetella or Alcaligenes strain FB188 with similarities to histone deacetylases. J Bacteriol. 2004; ... a Multiple Sequence Alignment of PA0321, PA1409 and PA3774 from P. aeruginosa, acetylpolyamine amidohydrolase APAH from M. ... 1a). Based on their sequence, PA0321 and PA1409 form a cluster with the verified functional acetylpolyamine amidohydrolase APAH ...
Gentaur Molecular :EIAab \ ELISA kit ACY1,ACY-1,Aminoacylase-1,N-acyl-L-amino-acid amidohydrolase,Pig,Sus scrofa \ E2259p
N-acyl-L-amino-acid amidohydrolase,Pig,Sus scrofa \ E2259p for more molecular products just contact us ... Product name : ELISA kit ACY1,ACY-1,Aminoacylase-1,N-acyl-L-amino-acid amidohydrolase,Pig,Sus scrofa ... E2259p ELISA kit ACY1,ACY-1,Aminoacylase-1,N-acyl-L-amino-acid amidohydrolase,Pig,Sus scrofa Ask technical file . ... We have also other products like : ELISA kit ACY1,ACY-1,Aminoacylase-1,N-acyl-L-amino-acid amidohydrolase,Pig,Sus scrofa. ...
Structure and catalytic mechanism of LigI: Insight into the amidohydrolase enzymes of cog3618 and lignin degradation<...
This protein is a member of the amidohydrolase superfamily of enzymes. The protein was expressed in Escherichia coli and then ... This protein is a member of the amidohydrolase superfamily of enzymes. The protein was expressed in Escherichia coli and then ... This protein is a member of the amidohydrolase superfamily of enzymes. The protein was expressed in Escherichia coli and then ... This protein is a member of the amidohydrolase superfamily of enzymes. The protein was expressed in Escherichia coli and then ...
ASAH2 Gene - GeneCards | ASAH2 Protein | ASAH2 Antibody
N-Acylsphingosine Amidohydrolase 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - ... ASAH2 (N-Acylsphingosine Amidohydrolase 2) is a Protein Coding gene. Diseases associated with ASAH2 include Sphingolipidosis ... View all R&D Systems ASAH2 (ASAH2/N-acylsphingosine Amidohydrolase-2) Proteins and Enzymes*Recombinant Human ASAH2 Protein, CF ... View all 3 R&D Systems ASAH2 (ASAH2/N-acylsphingosine Amidohydrolase-2) Primary Antibodies*Human ASAH2/N-acylsphingosine ...
Superfamily9
- We present case studies of proteins related to uronate isomerase (an amidohydrolase superfamily member) and mandelate racemase (an enolase superfamily member), to illustrate how this structure-focused approach can be used to generate hypotheses about sequence-structure-function relationships. (nih.gov)
- Sequence analysis showed that these enzymes belong to the metal-dependent amidohydrolase superfamily, although they contain a hitherto unreported Asn-X-His metal-binding motif and appear to form a novel sub-group within this superfamily. (biochemj.org)
- 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)
- This protein is a member of the amidohydrolase superfamily of enzymes. (elsevier.com)
- This is the first enzyme from the amidohydrolase superfamily that does not require a divalent metal ion for catalytic activity. (elsevier.com)
- Structural Determinants for Substrate Selectivity in Guanine Deaminase Enzymes of the Amidohydrolase Superfamily. (anl.gov)
- Here, we report the crystal structures of and guanine deaminase enzymes (EcGuaD and Gud1, respectively), both members of the amidohydrolase superfamily. (anl.gov)
- These proteins are members of the amidohydrolase superfamily and are currently misannotated in NCBI as catalyzing the hydrolysis of L-Xaa-L-Pro dipeptides. (elsevier.com)
- GLI, a member of the functionally diverse amidohydrolase superfamily, is a homologue of LigI that catalyzes the hydrolysis of 2-pyrone-4,6-dicarboxylate in lignin degradation. (illinois.edu)
Glutamine amidohydrolase1
- Crystal structure of human protein N-terminal glutamine amidohydrolase, an initial component of the N-end rule pathway. (nih.gov)
Hydrolase1
- Amidohydrolases (or amidases) are a type of hydrolase that acts upon amide bonds. (wikipedia.org)
Histidine-dependent3
- By fusing GPB to the CHAP (cysteine, histidine-dependent amidohydrolase/peptidase) catalytic domain of the PlyC lysin, we constructed a novel chimeric lysin, ClyJ, with improved activity to the pneumococcal Cpl-1 lysin. (asm.org)
- Inhibitor studies predicted the presence of an active-site cysteine, and bioinformatic analysis revealed a cysteine, histidine-dependent amidohydrolase/peptidase domain within PlyCA. (pnas.org)
- Cysteine/histidine-dependent amidohydrolase/peptidase (CHAP) and amidase are shown lytic activity against methicillin-resistant Staphylococcus aureus (MRSA). (indybedbugpros.com)
Gene3
- ASAH2 (N-Acylsphingosine Amidohydrolase 2) is a Protein Coding gene. (genecards.org)
- Gene Ontology (GO) annotations related to this gene include N-acylsphingosine amidohydrolase activity . (genecards.org)
- Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterization of the metal-substituted enzyme. (pseudomonas.com)
Putative1
- Results: To elucidate the role of acetylpolyamines and their enzymatic deacetylation in more detail, all three putative acetylpolyamine amidohydrolases (APAHs) from P. aeruginosa have been expressed in enzymatic active form. (kit.edu)
Enzyme5
- Here, we describe a collaboration between the Enzyme Specificity Consortium (ENSPEC) and the New York SGX Research Center for Structural Genomics (NYSGXRC) that aims to maximize the structural coverage of the amidohydrolase and enolase superfamilies. (nih.gov)
- Maleamate amidohydrolase (EC 3.5.1.107, NicF) is an enzyme with systematic name maleamate amidohydrolase. (wikipedia.org)
- The systematic name of this enzyme class is N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase . (wikipedia.org)
- Schnackerz KD, Dobritzsch D. Amidohydrolases of the reductive pyrimidine catabolic pathway purification, characterization, structure, reaction mechanisms and enzyme deficiency. (medlineplus.gov)
- 2 . The electrode strip of claim 1 wherein said enzyme is selected from the group consisting of glucose oxidase, lactate oxidase, cholesterol oxidase, and creatinine amidohydrolase. (google.com)
Amidase1
- 1) Amidase, EC 3.5.1.4 (Acylamide amidohydrolase). (thefreedictionary.com)
Allantoate3
- Below are the list of possible Allantoate amidohydrolase products. (mybiosource.com)
- Also known as Allantoate amidohydrolase (Allantoate deiminase). (mybiosource.com)
- Similar nitrate-dependent senescence phenotypes were evident in the older leaves of allantoinase ( Ataln ) and allantoate amidohydrolase ( Ataah ) mutants, which also are impaired in purine catabolism. (plantphysiol.org)
Maleamate amidohydrolase1
- The fifth step of this catabolic pathway involves hydrolytic deamidation of maleamate into maleate by maleamate amidohydrolase, NicF. (wooster.edu)
Pseudomonas1
- Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida. (asm.org)
Creatinine1
- It is a cyclic amidohydrolase catalysing the reversible conversion of creatinine to creatine. (juniperlifesciences.com)
Functionally3
- The functionally related amidohydrolases, including D-hydantoinases, dihydropyrimidinases, allantoinases and dihydro-orotases, share a similar catalytic function of acting on the cyclic amide ring. (kaist.ac.kr)
- As a particular sequence, one aspartic acid and four histidine residues are found to be rigidly conserved in the functionally related amidohydrolases. (kaist.ac.kr)
- On the basis of the similar catalytic function and existence of the rigidly conserved sequence, we propose a close evolutionary relationship among the functionally related amidohydrolases, including D-hydantoinase, dihydropyrimidinase, allantoinase and dihydroorotase. (kaist.ac.kr)
Substrate2
- Despite the availability of several crystal structures, the molecular determinants of substrate orientation and mechanism remain to be elucidated for the amidohydrolase family of guanine deaminase enzymes. (anl.gov)
- Overall, this work details key structural features of substrate recognition and catalysis of the amidohydrolase family of guanine deaminase enzymes in support of our long-term goal to engineer these enzymes with altered activity and substrate specificity. (anl.gov)
Characterization1
- Sánchez-Parra B, Frerigmann H, Alonso M-MP, Loba VC, Jost R, Hentrich M, Pollmann S. Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis. (mdpi.com)
Biological1
- Anandamide (arachidonylethanolamide), an endogenous ligand for cannabinoid receptors, is hydrolyzed by an amidohydrolase and its biological activity is lost. (nih.gov)
MEDLINE1
- Search Medline for phenylurea AND amidohydrolase . (ethz.ch)
Enzymes2
- As one of the primary enzymes in the system, fatty acid amidohydrolase (FAAH) works to break down anandamide. (royalqueenseeds.ru)
- A key gap in this docking approach has been the reliance on modeling noncovalent fit between a substrate and an enzyme using modifications of methods first developed for inhibitor discovery.22?26 Whereas this has proven effective for metalloenzymes such as those in the amidohydrolase and enolase superfamilies many enzymes proceed through a covalent intermediate that does not lend itself readily to noncovalent modeling. (livingseas.org)
Primary1
- A hydrolytic mechanism for a Mn2+ dependent amidohydrolases that disfavour Zn2+ as the primary catalytically active site metal proposed here is supported by these likely cases of convergent evolution. (uio.no)