chembox verifiedrevid 455157745 Name small L small Isoleucine ImageFileL1 L Isoleucin L Isoleucine.svg ImageSizeL1 120px ImageNameL1 Chemical structure of Isoleucine ImageFileR1 L isoleucine 3D balls.png ImageSizeR1 120px ImageNameR1 Chemical structure of Isoleucine IUPACName Isoleucine OtherNames 2 ... C H C C H C O O N Section2 Chembox Properties C 6 H 13 N 1 O 2 Isoleucine abbreviated as Ile or I ref ... be ingested. Its codons are AUU, AUC and AUA. With a hydrocarbon side chain, isoleucine is classified as a hydrophobic amino acid. Together with threonine , isoleucine is one of two common amino acids that have a Chirality chemistry chiral side chain. Four stereoisomer s of isoleucine are possible, including two possible diastereomer s of small L small isoleucine. However, isoleucine present in nature ... amino acid, isoleucine is not synthesized in animals, hence it must be ingested, usually ... aminotransferase Catabolism Isoleucine is both a glucogenic and a ketogenic amino acid. After transamination ... to as Vitamin B7 or Vitamin H , is an absolute requirement for the full catabolism of isoleucine as well as leucine . Without adequate biotin, the human body will be unable to fully break down isoleucine ... of hydroxyisovalerate , a byproduct of incomplete isoleucine catabolism. Isovaleric acidemia is an example ... of isoleucine include eggs, soy protein, seaweed, turkey, chicken, lamb, cheese, and fish. ref name List of Foods high in Isoleucine http www.nutritiondata.com foods 000081000000000000000.html , List ... Isomers of isoleucine border 1 cellspacing 0 cellpadding 3 style font size x small margin 0 0 0 ... of Isoleucine style background color F3F3F3 Common name isoleucine D isoleucine L isoleucine DL isoleucine allo D isoleucine allo L isoleucine allo DL isoleucine style background color F3F3F3 Synonyms R Isoleucine L Isoleucine R , R isoleucine alloisoleucine style background color F3F3F3 PubChem PubChemCID ... File D isoleucine.svg 200px br small L small isoleucine 2 S ,3 S and small D small isoleucine 2 R ,3 ... more details
enzyme Name isoleucine tRNA ligase EC number 6.1.1.5 CAS number 9030 96 0 IUBMB EC number 6 1 1 5 GO code 0004822 image width caption In enzymology , an isoleucine tRNA ligase EC number 6.1.1.5 is an enzyme that catalysis catalyzes the chemical reaction ATP L isoleucine tRNAIle math rightleftharpoons math AMP diphosphate L isoleucyl tRNAIle The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L isoleucine , and tRNA Ile , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L isoleucyl tRNA Ile . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L isoleucine tRNAIle ligase AMP forming . Other names in common use include isoleucyl tRNA synthetase , isoleucyl transfer ribonucleate synthetase , isoleucyl transfer RNA synthetase , isoleucine transfer RNA ligase , isoleucine tRNA synthetase , and isoleucine translase . This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl trna biosynthesis . Structural studies As of late 2007, 10 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1FFY , PDB link 1JZQ , PDB link 1JZS , PDB link 1QU2 , PDB link 1QU3 , PDB link 1UDZ , PDB link 1UE0 , PDB link 1WK8 , PDB link 1WNY , and PDB link 1WNZ . References reflist 1 cite journal author ALLEN EH, GLASSMAN E, SCHWEET RS date 1960 title Incorporation of amino acids into ribonucleic acid. I. The role of activating enzymes journal J. Biol. Chem. volume 235 pages 1061&ndash 7 pmid 13792726 cite journal author Berg P, Bergmann FH, Ofengand EJ and Dieckmann M date 1961 title The enzymic synthesis of amino acyl derivatives of ribonucleic acid I. The mechanism of leucyl , valyl , isoleucyl and methionyl ribonucleic acid formation journal J. Biol. Chem. volume 236 pages 1726&ndash 1734 cite ... more details
OrganicBox complete wiki name Isoleucine name 2 S ,3 S 2 amino 3 methylpentanoic acid GENERAL INFORMATION C 6 H 13 N 1 O 2 mass 131.18 ref 1 a abbreviation I, Ile image Image L isoleucine skeletal.png 110px Chemical structure of Isoleucine Image L isoleucine 3D sticks.png 100px Chemical structure of Isoleucine synonyms 2 amino 3 methylvaleric acid br 3 methyl erythro norvaline br Amino sec butyl acetic acid br Amino 1 methylpropyl acetic acid DATABASES SMILES CC C H C C H C O O N ref 1 b InChI 1 C6H13NO2 c1 3 4 2 5 7 6 8 9 h4 5H,3,7H2,1 2H3, H,8,9 t4 ,5 m0 s1 f h8H ref 1 c ATC prefix ATC suffix ATC supplemental CAS 73 32 5 DrugBank EINECS 200 798 2 ref 1 d PubChem 6306 PHYSICAL PROPERTIES Structure index of refraction abbe number dielectric constant magnetic susceptibility dipole moment U V data lambda max extinction coefficient Infrared data absorption bands NMR data proton NMR carbon NMR other NMR Spectrometry data mass spectrometry Phase behaviour delta f H o delta fus H o delta fus S o triple point K triple point C triple point Pa criticle point K criticle point C criticle point Pa Solid properties S o solid heat capacity solid density solid melting point C 284 melting point F melting point K Liquid properties delta vap H o delta vap S o S o liquid heat capacity liquid density liquid viscosity liquid boiling point C boiling point F boiling point K Gas properties S o gas heat capacity gas viscosity gas HAZARD PROPERTIES MSDS main hazards nfpa health nfpa flammability nfpa reactivity nfpa special flash point r phrases s phrases RTECS number CHEMICAL PROPERTIES XLogP 1.743 ref 1 e isoelectric point 6.02 disociation constant 2.26 9.60 tautomers H bond donor 2 ref 1 f H bond acceptor 3 ref 1 g PHARMACOLOGICAL PROPERTIES bioavailability metabolism elimination half life excretion pregnancy category legal status routes of administration References refbegin note 1 a note 1 b note 1 c note 1 d note 1 e note 1 f note 1 g PubChem 6306 refend AminoAcids Category Chemical ... more details
enzyme Name valine 3 methyl 2 oxovalerate transaminase EC number 2.6.1.32 CAS number 9023 14 7 IUBMB EC number 2 6 1 32 GO code 0047301 image width caption In enzymology , a valine 3 methyl 2 oxovalerate transaminase EC number 2.6.1.32 is an enzyme that catalysis catalyzes the chemical reaction L valine S 3 methyl 2 oxopentanoate math rightleftharpoons math 3 methyl 2 oxobutanoate L isoleucine Thus, the two substrate biochemistry substrates of this enzyme are L valine and S 3 methyl 2 oxopentanoate , whereas its two product chemistry products are 3 methyl 2 oxobutanoate and L isoleucine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L valine S 3 methyl 2 oxopentanoate aminotransferase . Other names in common use include valine isoleucine transaminase , valine 3 methyl 2 oxovalerate aminotransferase , alanine valine transaminase , valine 2 keto methylvalerate aminotransferase , and valine isoleucine aminotransferase . References reflist 1 cite journal last Kagan first Z. S. coauthors A. S. Dronov and V. L. Kretovich year 1968 trans title Some properties of valine isoleucine and valine glutamate aminotransferases of pea sprouts language Russian journal Doklady Akademii Nauk SSSR volume 179 pages 1236&ndash 1239 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
DISPLAYTITLE C sub 6 sub H sub 13 sub NO sub 2 sub The molecular formula C sub 6 sub H sub 13 sub NO sub 2 sub may refer to Aminocaproic acid Isoleucine Leucine Norleucine MolFormDisambig el C6H13NO2 fr C6H13NO2 it C6H13NO2 lv C6h13no2 ... more details
Peptide PHI or peptide histidine isoleucine is a peptide which functions as a hormone . It plays a role in the regulation of prolactin in humans. ref cite journal author Kulick R, Chaiseha Y, Kang S, Rozenboim I, El Halawani M title The relative importance of vasoactive intestinal peptide and peptide histidine isoleucine as physiological regulators of prolactin in the domestic turkey journal Gen Comp Endocrinol volume 142 issue 3 pages 267 273 year 2005 pmid 15935152 doi 10.1016 j.ygcen.2004.12.024 ref References references External links MeshName Peptide PHI Category Hormones biochemistry stub sr Peptid PHI ... more details
protein Name mitochondrially encoded tRNA isoleucine caption image width HGNCid 7488 Symbol MT TI AltSymbols MTTI EntrezGene 4565 OMIM RefSeq NC 001807 UniProt PDB ECnumber Chromosome MT Arm Band LocusSupplementaryData Mitochondrially encoded tRNA isoleucine also known as MT TI is a transfer RNA which in humans is encoded by the mitochondrion mitochondrial MT TI gene . ref name pmid7219534 cite journal author Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG title Sequence and organization of the human mitochondrial genome journal Nature volume 290 issue 5806 pages 457 65 year 1981 month April pmid 7219534 doi 10.1038 290457a0 url ref MT TI is a small 69 nucleotide RNA human mitochondrial map position 4263 4331 that transfers the amino acid isoleucine to a growing polypeptide chain at the ribosomal ribosome site of protein synthesis during translation genetics translation . References Reflist Mitochondrial enzymes gene stub ... more details
wiktionary ile Ile ile Ile can be different things Ile military unit , a Greek military term for a cavalry company An abbreviation of isoleucine , an amino acid Ile, a district of Mozambique Another name for Ilargi , the moon in Basque mythology ile is the ISO 639 2 and ISO 639 3 code for the Interlingue constructed language disambig de Ile nl le pt le sv Ile uk ... more details
br clear all Infobox Disease Name Beta ketothiolase deficiency Image l isoleucine.png Caption Isoleucine DiseasesDB 29824 ICD10 ICD9 ICDO OMIM 203750 MedlinePlus eMedicineSubj eMedicineTopic MeshID Beta ketothiolase deficiency is a rare, autosomal recessive metabolic disorder in which the body cannot properly process the amino acid isoleucine or the products of lipid breakdown. The typical age of onset for this disorder is between 6 months and 24 months. Symptoms The signs and symptoms of beta ketothiolase deficiency include vomiting , dehydration , trouble breathing, extreme tiredness, and occasionally convulsion s. These episodes are called ketoacidotic attacks and can sometimes lead to coma . Attacks occur when compounds called organic acids which are formed as products of amino acid and fat breakdown build up to toxic levels in the blood. These attacks are often triggered by an infection, fasting not eating , or in some cases, other types of stress. Genetic prevalence This condition is inherited in an autosomal recessive pattern and is extremely rare having only been reported in 50 to 60 individuals throughout the world. Image autorecessive.svg thumb right Beta ketothiolase deficiency has an autosomal recessive pattern of inheritance. Mutation s in the ACAT1 gene cause beta ketothiolase deficiency. The enzyme made by the ACAT1 gene plays an essential role in breaking down proteins and fats in the diet. Specifically, the enzyme is responsible for processing isoleucine, an amino acid that is part of many proteins. This enzyme also processes ketone s, which are produced during the breakdown of fats. If a mutation in the ACAT1 gene reduces or eliminates the activity of this enzyme, the body is unable to process isoleucine and ketones properly. As a result, harmful compounds can build up and cause the blood to become too acidic ketoacidosis , which impairs tissue function, especially in the central nervous system . References This article incorporates public domain text ... more details
ILE can refer to ILE plastics industry , Intermittent Layer Extrusion, a process which allows the extrusion of a variable layer thickness tube Isolagen Inc AMEX stock symbol ILE Institution of Lighting Engineers , ILE UK and Ireland s largest professional lighting association Isoleucine Ile Instituci n Libre de Ense anza , a Spanish education organization Intuitive Logical Extrovert , a Socionics term Integrated Language Environment disambig eo ILE it ILE ... more details
The leucines are primarily the four isomer ic amino acid s leucine , isoleucine , tert Leucine tert leucine and norleucine . Being compared with the four butanol s, they could be classified as butyl substituted glycine s they represent all four possible variations. Leucine and isoleucine belong to the proteinogenic amino acid s the others are non natural. Including the stereoisomers, six further isomers could be added small D small leucine, small D small isoleucine, small L small allo isoleucine, small D small allo isoleucine, small D small tert leucine and small D small norleucine., Cycloleucine could be classified as a cyclic derivate of norleucine . With a cyclopentane ring, it has two hydrogen atoms less and thus is not an isomer. The carbon atom is not a stereocenter. center class wikitable centered style text align center font size 90 class hintergrundfarbe6 align center colspan 6 Leucines class hintergrundfarbe5 align left Name small L small Leucine small L small Isoleucine small L small tert Leucine tert Leucine Terleucine small L small Norleucine Cycloleucine class hintergrundfarbe5 align left Other names 2 Amino 4 methylpentanoic acid, br Isobutylglycine 2 Amino 3 methylpentanoic acid, br sec Butylglycine 2 Amino 3,3 dimethylbutanoic acid, br tert Butylglycine 2 Amino hexanoic acid, br n Butylglycine 1 Amino cyclopentane 1 carboxylic acid br class hintergrundfarbe5 align left Structure Image L Leucin L Leucine.svg 150px Image L Isoleucin L Isoleucine.svg 150px Image L tert Leucine.svg 110px Image L Norleucin.svg 175px Image Cycloleucin.svg 105px class hintergrundfarbe5 align left CAS number 61 90 5 73 32 5 20859 02 3 327 57 1 52 52 8 class hintergrundfarbe5 align left PubChem PubChem 6106 PubChem 791 PubChem 164608 PubChem 21236 PubChem 2901 class hintergrundfarbe5 align left Molecular formula colspan 4 C sub 6 sub H sub 13 sub NO sub 2 sub C sub 6 sub H sub 11 sub NO sub 2 sub class hintergrundfarbe5 align left Molar mass colspan 4 131.18 g mol 129.16 ... more details
Unreferenced date October 2009 Notability date October 2009 Image Diesel can 16 photo angled.jpg frame right A 16 ounce can of Diesel Diesel is an energy drink produced by Diesel Beverage Company in La Mesa, California . Diesel advertises that it provides high octane power with 6000 or 9000 horsepower and can be purchased in 16 cylinder or 24 cylinder sizes. The horsepower tagline refers to the amount in milligrams of energy components found in each can. The cylinder aspect refers to the number of ounces in each can. Diesel has typical energy components of caffeine , ginseng , taurine , and guarana guarana extract , but also include a number of amino acids which are thought to promote energy and cellular health. The amino acids in Diesel are as follows Carnitine L carnitine , Valine L valine , Leucine L leucine , Isoleucine L isoleucine , and Tyrosine L tyrosine . A serving of Diesel provides 100 RDA of Vitamin C and 190 of Vitamin B6 vitamin B sub 6 sub . The flavor is mixed fruit. See also List of energy drinks External links http www.dieseldrink.com Diesel Energy Drink Category Energy drinks nonalcoholic drink stub ... more details
enzyme Name 2 acetolactate mutase EC number 5.4.99.3 CAS number 37318 52 8 IUBMB EC number 5 4 99 3 GO code 0047534 image width caption In enzymology , a 2 acetolactate mutase EC number 5.4.99.3 is an enzyme that catalysis catalyzes the chemical reaction 2 acetolactate math rightleftharpoons math 3 hydroxy 3 methyl 2 oxobutanoate Hence, this enzyme has one substrate biochemistry substrate , 2 acetolactate , and one product chemistry product , 3 hydroxy 3 methyl 2 oxobutanoate . This enzyme belongs to the family of isomerase s, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 2 acetolactate methylmutase . Other names in common use include acetolactate mutase , and acetohydroxy acid isomerase . This enzyme participates in valine, leucine and isoleucine biosynthesis . It employs one cofactor biochemistry cofactor , ascorbate . References reflist 1 cite journal author Allaudeen HS, Ramakrishnan T date 1968 title Biosynthesis of isoleucine and valine in Mycobacterium tuberculosis H37 Rv journal Arch. Biochem. Biophys. volume 125 pages 199&ndash 209 pmid 4384955 doi 10.1016 0003 9861 68 90655 3 issue 1 isomerase stub Category EC 5.4.99 Category Ascorbate enzymes Category Enzymes of unknown structure ... more details
PHI is a three letter acronym or abbreviation that can refer to Packard Humanities Institute Pepco Holdings Pepco Holdings Inc. Post Polio Health International Protected Health Information as part of the HIPAA regulations The Golden ratio The Philippines IOC country code Philadelphia, Pennsylvania Philadelphia Phillies , a Major League Baseball team Philadelphia Flyers , a National Hockey League team Philadelphia Eagles , a National Football League team Philadelphia 76ers , a National Basketball Association team Peptide PHI Peptide Histidine Isoleucine See also Phi disambiguation disambig eo PHI fr PHI it PHI ja PHI sr PHI vi ezna na odrednica ... more details
chembox verifiedrevid 383787414 ImageFile Furanomycin.svg ImageSize IUPACName 2 S 2 amino 2 2 R ,5 S 5 methyl 2,5 dihydrofuran 2 yl acetic acid OtherNames Section1 Chembox Identifiers CASNo 18455 25 9 PubChem 73423 SMILES CC1C CC O1 C C O O N Section2 Chembox Properties Formula C sub 7 sub H sub 11 sub NO sub 3 sub MolarMass 157.16714 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Furanomycin is an isoleucine analog. heterocyclic stub Category Amino acids Category 2,5 Dihydrofurans ... more details
enzyme Name 3 hydroxy 2 methylbutyryl CoA dehydrogenase EC number 1.1.1.178 CAS number 52227 66 4 IUBMB EC number 1 1 1 178 GO code 0047015 image width caption In enzymology , a 3 hydroxy 2 methylbutyryl CoA dehydrogenase EC number 1.1.1.178 is an enzyme that catalysis catalyzes the chemical reaction 2S,3S 3 hydroxy 2 methylbutanoyl CoA NAD sup sup math rightleftharpoons math 2 methylacetoacetyl CoA NADH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are 2S,3S 3 hydroxy 2 methylbutanoyl CoA and nicotinamide adenine dinucleotide NAD sup sup , whereas its 3 product chemistry products are 2 methylacetoacetyl CoA , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is 2S,3S 3 hydroxy 2 methylbutanoyl CoA NAD oxidoreductase . Other names in common use include 2 methyl 3 hydroxybutyryl coenzyme A dehydrogenase , 2 methyl 3 hydroxybutyryl coenzyme A dehydrogenase , and 2 methyl 3 hydroxy butyryl CoA dehydrogenase . This enzyme participates in valine, leucine and isoleucine degradation . Structural studies As of 20 January 2010, 6 tertiary structure structure have been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1E3S , PDB link 1E3W , PDB link 1E6W , PDB link 1SO8 , PDB link 1U7T , PDB link 2O23 . References reflist 1 cite journal author Conrad RS, Massey LK, Sokatch JR date 1974 title D and L isoleucine metabolism and regulation of their pathways in Pseudomonas putida journal J. Bacteriol. volume 118 pages 103&ndash 11 pmid 4150713 issue 1 pmc 246645 1.1.1 enzyme stub Category EC 1.1.1 Category NADH dependent enzymes Category Enzymes of known structure it 3 idrossi 2 metilbutirril CoA deidrogenasi ja 3 2 CoA ... more details
enzyme Name leucine dehydrogenase EC number 1.4.1.9 CAS number 9082 71 7 IUBMB EC number 1 4 1 9 GO code 0050049 image width caption In enzymology , a leucine dehydrogenase EC number 1.4.1.9 is an enzyme that catalysis catalyzes the chemical reaction L leucine H sub 2 sub O NAD sup sup math rightleftharpoons math 4 methyl 2 oxopentanoate NH sub 3 sub NADH H sup sup The 3 substrate biochemistry substrates of this enzyme are L leucine , water H sub 2 sub O , and nicotinamide adenine dinucleotide NAD sup sup , whereas its 4 product chemistry products are 4 methyl 2 oxopentanoate , ammonia NH sub 3 sub , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH2 group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is L leucine NAD oxidoreductase deaminating . Other names in common use include L leucine dehydrogenase , L leucine NAD oxidoreductase, deaminating , and LeuDH . This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1LEH . References reflist 1 cite journal author Sanwal BD and Zink MW date 1961 title L Leucine dehydrogenase of Bacillus cereus journal Arch. Biochem. Biophys. volume 94 pages 430&ndash 435 doi 10.1016 0003 9861 61 90070 4 cite journal author Zink MW and Sanwal BD date 1962 title The distribution and substrate specificity of L leucine dehydrogenase journal Arch. Biochem. Biophys. volume 99 pages 72&ndash 77 doi 10.1016 0003 9861 62 90245 X 1.4 enzyme stub Category EC 1.4.1 Category NADH dependent enzymes Category Enzymes of known structure es Leucina deshidrogenasa it Leucina deidrogenasi ja ... more details
enzyme Name dihydroxy acid dehydratase EC number 4.2.1.9 CAS number 9024 32 2 IUBMB EC number 4 2 1 9 GO code 0004160 image width caption In enzymology , a dihydroxy acid dehydratase EC number 4.2.1.9 is an enzyme that catalysis catalyzes the chemical reaction 2,3 dihydroxy 3 methylbutanoate math rightleftharpoons math 3 methyl 2 oxobutanoate H sub 2 sub O Hence, this enzyme has one substrate biochemistry substrate , 2,3 dihydroxy 3 methylbutanoate , and two product chemistry products , 3 methyl 2 oxobutanoate and water H sub 2 sub O . This enzyme belongs to the family of lyase s, specifically the hydro lyases, which cleave carbon oxygen bonds. The systematic name of this enzyme class is 2,3 dihydroxy 3 methylbutanoate hydro lyase 3 methyl 2 oxobutanoate forming . Other names in common use include acetohydroxyacid dehydratase , alpha,beta dihydroxyacid dehydratase , 2,3 dihydroxyisovalerate dehydratase , alpha,beta dihydroxyisovalerate dehydratase , dihydroxy acid dehydrase , DHAD , and 2,3 dihydroxy acid hydro lyase . This enzyme participates in valine, leucine and isoleucine biosynthesis and pantothenate and coa biosynthesis . References reflist 1 cite journal author KANAMORI M, WIXOM RL date 1963 title Studies in valine biosynthesis. V. Characteristics of the purified dihydroxyacid dehydratase from spinach leaves journal J. Biol. Chem. volume 238 pages 998&ndash 1005 pmid 14030545 cite journal author MYERS JW date 1961 title Dihydroxy acid dehydrase an enzyme involved in the biosynthesis of isoleucine and valine journal J. Biol. Chem. volume 236 pages 1414&ndash 8 pmid 13727223 4.2 enzyme stub Category EC 4.2.1 Category Enzymes of unknown structure ... more details
enzyme Name leucine transaminase EC number 2.6.1.6 CAS number 9030 37 9 IUBMB EC number 2 6 1 6 GO code 0050048 image width caption In enzymology , a leucine transaminase EC number 2.6.1.6 is an enzyme that catalysis catalyzes the chemical reaction L leucine 2 oxoglutarate math rightleftharpoons math 4 methyl 2 oxopentanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L leucine and 2 oxoglutarate , whereas its two product chemistry products are 4 methyl 2 oxopentanoate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L leucine 2 oxoglutarate aminotransferase . Other names in common use include L leucine aminotransferase , leucine 2 oxoglutarate transaminase , leucine aminotransferase , and leucine alpha ketoglutarate transaminase . This enzyme participates in 3 metabolism metabolic pathways valine, leucine and isoleucine degradation , valine, leucine and isoleucine biosynthesis , and pantothenate and coa biosynthesis . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Aki K, Ogawa K, Ichihara A date 1968 title Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes from rat liver journal Biochim. Biophys. Acta. volume 159 pages 276&ndash 84 pmid 4968655 issue 2 cite journal author Ikeda T, Konishi Y, Ichihara A date 1976 title Transaminase of branched chain amino acids. XI. Leucine methionine transaminase of rat liver mitochondria journal Biochim. Biophys. Acta. volume 445 pages 622&ndash 31 pmid 974100 issue 3 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
SM date 1979 title Stereochemistry of valine and isoleucine biosynthesis. IV Synthesis, configuration ... AN date 1965 title Biosynthesis of valine and isoleucine in plants. 3. Reductoisomerase of Phaseolus ... more details
. A diet with minimal levels of the amino acids leucine, isoleucine, and valine must be maintained in order ... acids leucine , isoleucine , and valine , which are present in many kinds of food in particular ... the function of the enzyme complex, preventing the normal breakdown of isoleucine , leucine , and valine ... more details
A ketogenic amino acid is an amino acid that can be converted into ketone bodies through ketogenesis . This is in contrast to the glucogenic amino acid s, which are converted into glucose . Ketogenic amino acids are unable to be converted to glucose as both carbon atoms in the ketone body are ultimately degraded to carbon dioxide in the citric acid cycle . In humans, two amino acids are exclusively ketogenic leucine lysine In humans, five amino acids are both ketogenic and glucogenic isoleucine phenylalanine tryptophan tyrosine threonine See also List of standard amino acids Glucogenic amino acid Ketogenesis Metabolism External links http web.indstate.edu thcme mwking amino acid metabolism.html Amino acid metabolism http www.ncbi.nlm.nih.gov books bv.fcgi?rid stryer.chapter.3193 Chapter on Amino acid catabolism in Biochemistry by Jeremy Berg, John Tymoczko, Lubert Stryer. Fourth ed. by Lubert Stryer. ISBN 0 7167 4955 6 Accessed 2007 03 17 http www.dentistry.leeds.ac.uk biochem thcme aminoacidmetabolism.pdf Amino acid metabolism AminoAcids Category Ketogenic amino acids Category Nitrogen metabolism biochem stub fr Acide amin c toformateur gl Amino cido cetox nico it Amminoacidi chetogenici ja sr Ketogena aminokiselina fi Ketogeeninen aminohappo zh ... more details
Infobox rfam Name Potassium channel RNA editing signal image RF00485.jpg width caption Predicted secondary structure and sequence conservation of K chan RES Symbol K chan RES AltSymbols Rfam RF00485 miRBase miRBase family RNA type Cis regulatory element Cis reg Tax domain Eukaryota GO SO SO 0000233 CAS number EntrezGene HGNCid OMIM PDB RefSeq Chromosome Arm Band LocusSupplementaryData The potassium channel RNA editing signal is an cis regulatory element RNA element found in human Kv1.1 and its homologues which directs the efficient modification of an adenosine to inosine by an adenosine deaminase acting on RNA ADAR . The ADAR modification causes an isoleucine valine recoding event which lies in the ion conducting pore of the potassium channel . It is thought that this editing event targets the process of fast inactivation and allows a more rapid recovery from inactivation at negative potentials. ref cite journal last Bhalla first T coauthors Rosenthal JJ, Holmgren M, Reenan R year 2004 title Control of human potassium channel inactivation by editing of a small mRNA hairpin journal Nat Struct Mol Biol volume 11 pages 950&ndash 956 pmid 15361858 doi 10.1038 nsmb825 issue 10 ref References reflist 1 External links Rfam id RF00485 name Potassium channel RNA editing signal Category Cis regulatory RNA elements molecular cell biology stub ... more details
enzyme Name R 2 methylmalate dehydratase EC number 4.2.1.35 CAS number 9027 92 3 IUBMB EC number 4 2 1 35 GO code 0047508 image width caption In enzymology , a R 2 methylmalate dehydratase EC number 4.2.1.35 is an enzyme that catalysis catalyzes the chemical reaction R 2 methylmalate math rightleftharpoons math 2 methylmaleate H sub 2 sub O Hence, this enzyme has one substrate biochemistry substrate , R 2 methylmalate , and two product chemistry products , 2 methylmaleate and water H sub 2 sub O . This enzyme belongs to the family of lyase s, specifically the hydro lyases, which cleave carbon oxygen bonds. The systematic name of this enzyme class is R 2 methylmalate hydro lyase 2 methylmaleate forming . Other names in common use include citraconate hydratase , citraconase , citramalate hydro lyase , citramalate hydro lyase , and R 2 methylmalate hydro lyase . This enzyme participates in valine, leucine and isoleucine biosynthesis and c5 branched dibasic acid metabolism . It employs one cofactor biochemistry cofactor , iron . References reflist 1 cite journal author Subramanian SS, Rao MR date 1968 title Purification and properties of citraconase journal J. Biol. Chem. volume 243 pages 2367&ndash 72 pmid 4296839 issue 9 4.2 enzyme stub Category EC 4.2.1 Category Iron enzymes Category Enzymes of unknown structure ... more details
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