infobox enzyme Name Arginase EC number 3.5.3.1 CAS number 9000 96 8 IUBMB EC number 3 5 3 1 GO code 0004053 image Ribbon Diagram.png width caption Ribbon diagram of cobalt reconstituted human arginase ... A, Rodriguez PC, Ochoa AC, Centeno F, Christianson DW title Crystal structure of human arginase ... doi 10.1073 pnas.0504027102 url ref Protein Name Liver arginase image caption Symbol ARG1 AltSymbols ... 383 RefSeq NM 000045 UniProt P05089 PDB Protein Name Arginase, type II image caption Symbol ARG2 ... EntrezGene 384 RefSeq NM 001172 UniProt P78540 PDB Arginase is a manganese containing enzyme . The reaction ... enzyme of the urea cycle . Structure and function Arginase belong to the ureohydrolase family of enzymes. Arginase catalyzes the fifth and final step in the urea cycle , a series of biochemical reactions in mammals during which the body disposes of harmful ammonia . Specifically, arginase converts ... 336 0001 bj3360001.htm issn ref In most mammals, two isozymes of this enzyme exist the first, Arginase ... isozyme, Arginase II, has been implicated in the regulation of the arginine ornithine concentrations ..., and crystal structure of perdeuterated human arginase I journal Archives of biochemistry and biophysics ... j.abb.2007.04.036 url issn ref Arginase consists of three tetramers. The enzyme requires a two molecule ... cite journal author Reczkowski RS, Ash DE title Rat liver arginase kinetic mechanism, alternate ..., 28 Spetember 2011 Arginase s active site is extraordinarily specific. Modifying the substrate structure ..., is a moderate inhibitor of arginase. Crystal structure of its complex with the enzyme ... substrate, and is a potent inhibitor of human arginase I. ref name pmid10542097 cite journal author Cox JD, Kim NN, Traish AM, Christianson DW title Arginase boronic acid complex highlights a physiological ... year 1999 month November pmid 10542097 doi 10.1038 14929 url issn ref Role in sexual response Arginase ... engorgement of tissue necessary for normal sexual response. However, since NO synthase and arginase ... more details
an enzyme called arginase. This enzyme controls the final step of the urea cycle, which produces urea by removing nitrogen from arginine. In people with arginase deficiency, arginase is damaged ... are believed to cause the neurological problems and other signs and symptoms of arginase ... Cycle Disorders Overview http www.ncbi.nlm.nih.gov books NBK1159 GeneReviews NCBI NIH UW entry on Arginase ... entries on Arginase Deficiency NLM arginasedeficiency Amino acid metabolic pathology Category Amino ... more details
, Xu Q title Developmental and hormonal regulation of the Xenopus liver type arginase gene journal Eur. J. Biochem. volume 211 issue 3 pages 891 898 year 1993 pmid 7916684 ref . There are several arginase ... more details
Chembox Name L Canaline ImageFile L Canaline.svg ImageSize IUPACName 2 S 2 amino 4 aminooxy butanoic acid OtherNames Section1 Chembox Identifiers InChIKey FQPGMQABJNQLLF VKHMYHEABX CASNo 496 93 5 PubChem 441443 ChEMBL 1231652 ChemSpiderID 390176 KEGG C08270 SMILES O C O C H N CCON InChI 1 C4H10N2O3 c5 3 4 7 8 1 2 9 6 h3H,1 2,5 6H2, H,7,8 t3 m0 s1 Section2 Chembox Properties C 4 H 10 N 2 O 3 MolarMass 134.13 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition L Canaline IUPAC name 2 amino 4 aminooxy butyric acid is a non protein amino acid . The compound is found in legumes that contain canavanine , from which it is produced by the action of arginase . The most common used source for this amino acid is the jack bean, Canavalia ensiformis . It is grown commercially as a source of the enzyme urease. L Canaline is the only naturally occurring amino acid known that has an O alkyl hydroxylamine functionality in the side chain. This amino acid is structurally related to ornithine it is the 5 oxa derivative and is a potent insecticide. Tobacco hornworm larvae fed a diet containing 2.5 mM canaline showed massive developmental aberrations, and most larvae so treated died at the pupal stage. It also exhibits potent neurotoxic effects in the moth. Its toxicity stems primarily from the fact that it readily forms oximes with keto acids and aldehydes, especially the pyridoxal phosphate cofactor of many Vitamin B sub 6 sub dependent enzymes. It inhibits ornithine aminotransferase at concentrations as low as 10 nM. L Canaline is a substrate for ornithine aminotransferase resulting in the synthesis of L ureidohomoserine the corresponding analog of L citrulline . In turn, the latter forms L canavaninosuccinic acid in a reaction mediated by argininosuccinic acid synthetase. L Canavaninosuccinic acid is cleaved to form L canavanine by argininosuccinic acid synthetase. By these sequential reactions, the canaline urea cycle analogous ... more details
Argininosuccinate lyase ASL cytosol 5 Arginine Arg H sub 2 sub O ornithine urea Arginase 1 ARG1 cytosol ... br ASL argininosuccinate lyase br ARG1 Arginasearginase 1 blockquote clear In the first reaction ... more details
chembox Verifiedfields changed verifiedrevid 408781245 Name small L small Ornithine ImageFile L Ornithin2.svg IUPACName small L small Ornithine OtherNames S 2,5 Diaminovaleric acid, S 2,5 Diaminopentanoic acid Section1 Chembox Identifiers UNII Ref fdacite correct FDA UNII E524N2IXA3 InChI 1 C5H12N2O2 c6 3 1 2 4 7 5 8 9 h4H,1 3,6 7H2, H,8,9 t4 m0 s1 InChI1 1 C5H12N2O2 c6 3 1 2 4 7 5 8 9 h4H,1 3,6 7H2, H,8,9 t4 m0 s1 InChIKey1 AHLPHDHHMVZTML BYPYZUCNBZ ChEMBL Ref ebicite correct EBI ChEMBL 446143 StdInChI Ref stdinchicite correct chemspider StdInChI 1S C5H12N2O2 c6 3 1 2 4 7 5 8 9 h4H,1 3,6 7H2, H,8,9 t4 m0 s1 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey AHLPHDHHMVZTML BYPYZUCNSA N CASNo 70 26 8 CASNo Ref cascite correct CAS EC number 200 731 7 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 6026 PubChem 6262 KEGG Ref keggcite correct kegg KEGG D08302 DrugBank Ref drugbankcite changed drugbank DrugBank DB00129 ChEBI Ref ebicite changed EBI ChEBI 15729 SMILES O C O C H N CCCN MeSHName Ornithine Section2 Chembox Properties Reference ref RubberBible62nd page C 408 . ref Formula C sub 5 sub H sub 12 sub N sub 2 sub O sub 2 sub MolarMass 132.16 g mol Appearance Density MeltingPt 140 C Solubility soluble SpecRotation 11.5 H sub 2 sub O, c 6.5 Section7 Chembox Hazards EUIndex FlashPt Ornithine is an amino acid that plays a role in the urea cycle . Role in urea cycle small L small Ornithine is one of the products of the action of the enzyme arginase on small L small arginine , creating urea . Therefore, ornithine is a central part of the urea cycle, which allows for the disposal of excess nitrogen . Ornithine is recycled and, in a manner, is a catalyst. First, ammonia is converted into carbamoyl phosphate phosphate CONH sub 2 sub , which creates one half of urea. Ornithine is converted into a urea derivative at the terminal nitrogen by carbamoyl phosphate. Another nitrogen is added from aspartate , producing the denitrogenated fumarate , and ... more details
Infobox scientist name Henry Drysdale Dakin image image size caption birth date 12 March 1880 birth place London , England residence Image Flag of England.svg 20px England nationality Image Flag of England.svg 20px England English death date death date and age 1952 2 10 1880 3 12 df y death place Scarsdale, New York , USA field work institution University of Leeds , br University of Heidelberg , br Columbia University alma mater University of Leeds doctoral advisor Julius B. Cohen , br Albrecht Kossel doctoral students known for Carrel Dakin method, br Dakin reaction , br Dakin West reaction prizes religion footnotes Henry Drysdale Dakin Fellow of the Royal Society FRS 1880 1952 was an England English chemist . He was born in London as the youngest of 8 children to a family of steel merchants from Leeds . As a school boy he did water analysis with the Leeds City Analyst. He studied chemistry at the University of Leeds with Julius B. Cohen and after he worked with Albrecht Kossel on arginase at the University of Heidelberg he joined Columbia University in 1905, working in the lab of Christian Archibald Herter physician Christian Herter . During his work on amino acids he obtained his PhD from Leeds. In 1914 he went back to England to offer his service with the war effort. Due to a request for a chemist by Alexis Carrel to the Rockefeller Institute, Dakin joined Carrel in 1916 at a temporary hospital in Compi gne . There they developed the Carrel Dakin method of wound treatments. This consisted of intermittently irrigating the wound with Dakin s solution. This solution is a highly diluted antiseptic, consisting of sodium hypochlorite 0.4 to 0.5 and boric acid 4 . It is unstable and deteriorates within a few days, and must be made as needed. Since 1982 a modified, more stable Dakin s Solution has been commercially available from Century Pharmaceuticals, Inc. After he married the widow of Christian Archibald Herter physician Christian Herter in 1916, he worked in his pr ... more details
colored glass. Biological role File Arginase.jpeg thumb right 400px Reactive center of arginase with boronic ... containing polypeptides may be arginase , the diphtheria toxin , and Mn containing superoxide dismutase ... more details
This list contains a list of Enzyme Commission number EC numbers for the third group, EC 3 , hydrolases , placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology . EC 3.1 Acting on Ester Bonds EC 3.1.1 Carboxylic Ester Hydrolases EC number 3.1.1.1 carboxylesterase EC number 3.1.1.2 arylesterase EC number 3.1.1.3 triacylglycerol lipase EC number 3.1.1.4 phospholipase A2 EC number 3.1.1.5 lysophospholipase EC number 3.1.1.6 acetylesterase EC number 3.1.1.7 acetylcholinesterase EC number 3.1.1.8 cholinesterase EC number 3.1.1.9 deleted EC number 3.1.1.10 tropinesterase EC number 3.1.1.11 pectinesterase EC number 3.1.1.12 deleted EC number 3.1.1.13 sterol esterase EC number 3.1.1.14 chlorophyllase EC number 3.1.1.15 L arabinonolactonase EC number 3.1.1.16 deleted, mixture of EC 5.3.3.4 and EC 3.1.1.24 EC number 3.1.1.17 gluconolactonase EC number 3.1.1.18 deleted, included in EC 3.1.1.17 EC number 3.1.1.19 uronolactonase EC number 3.1.1.20 tannase EC number 3.1.1.21 retinyl palmitate esterase EC number 3.1.1.22 hydroxybutyrate dimer hydrolase EC number 3.1.1.23 acylglycerol lipase EC number 3.1.1.24 3 oxoadipate enol lactonase EC number 3.1.1.25 1,4 lactonase EC number 3.1.1.26 galactolipase EC number 3.1.1.27 4 pyridoxolactonase EC number 3.1.1.28 acylcarnitine hydrolase EC number 3.1.1.29 aminoacyl tRNA hydrolase EC number 3.1.1.30 D arabinonolactonase EC number 3.1.1.31 6 phosphogluconolactonase EC number 3.1.1.32 phospholipase A1 EC number 3.1.1.33 6 acetylglucose deacetylase EC number 3.1.1.34 lipoprotein lipase EC number 3.1.1.35 dihydrocoumarin hydrolase EC number 3.1.1.36 limonin D ring lactonase EC number 3.1.1.37 steroid lactonase EC number 3.1.1.38 triacetate lactonase EC number 3.1.1.39 actinomycin lactonase EC number 3.1.1.40 orsellinate depside hydrolase EC number 3.1.1.41 cephalosporin C deacetylase EC number 3.1.1.42 chlorogenate hydrolase EC number 3.1.1.43 a amino acid ester ... more details
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