chembox verifiedrevid 408572342 ImageFileL1 L leucine skeletal.png ImageSizeL1 120px ImageFileR1 L leucine 3D balls.png ImageSizeR1 140px IUPACName Leucine OtherNames 2 Amino 4 methylpentanoic acid Section1 ... Leucine abbreviated as Leu or L ref cite web author IUPAC IUBMB Joint Commission on Biochemical Nomenclature ..., CUA, and CUG. With a hydrocarbon side chain, leucine is classified as a hydrophobic amino acid. It has an isobutyl R group. Leucine is a major component of the sub units in ferritin , astacin and other buffer protein s. Biosynthesis As an essential amino acid, leucine is not synthesized in animals ... undergoes reductive amination . Enzymes involved in a typical leucine biosynthesis include ref Nelson ... dehydratase , Isopropylmalate synthase , Isopropylmalate isomerase , Leucine aminotransferase . Biology Leucine is utilized in the liver , adipose tissue , and muscle tissue . In adipose and muscle tissue, leucine is used in the formation of sterol s, and the combined usage of leucine in these two ... al. Department of Medicine, University of Toronto, Toronto, Canada title Metabolic fate of leucine ... ref Leucine is the only dietary protein that has the capacity to stimulate muscle protein synthesis ... 134 4 996S.long pmid 15051860 ref As a dietary supplement, leucine has been found to slow the degradation ... L. Combaret, et al. Human Nutrition Research Centre of Clermont Ferrand title A leucine supplemented ... cgi reprint 569 2 489 accessdate 2008 03 25 ref Leucine potently activates the mammalian target of rapamycin kinase that regulates cell growth . Infusion of leucine into the rat brain has been shown ... PMID 16690869 ref Leucine toxicity, as seen in decompensated Maple Syrup Urine Disease MSUD , causes ... gene for leucine synthesis leu2 are transformed with a plasmid that contains a working leucine synthesis gene LEU2 and grown on minimal media. Leucine synthesis then becomes a useful selectable marker. Dietary aspects class wikitable sortable align right Food sources of Leucine ref Cite book ... more details
parallel alpha helices . ref name pmid3289117 A single leucine zipper consists of multiple leucine ... the motifs to zip together. Furthermore, the hydrophobic leucine region is absolutely required for DNA binding. Structure Image Leucine zipper.png thumb Leucine Zipper blue bound to DNA. The leucine residues that represent the teeth of the zipper are colored red The main feature of the leucine zipper domain is the predominance of the common amino acid leucine at the d position of the heptad repeat . Leucine zippers were first identified by sequence alignment of certain transcription factor ... shown to form the hydrophobic core of a coiled coil . Each half of a leucine zipper consists of a short alpha helix with a leucine residue at every seventh position. The standard 3.6 residues per turn ... repeat , one leucine comes in direct contact with another leucine on the other strand every ... leucine zipper region that is responsible for dimerization. Biology Leucine zipper regulatory proteins ... title Leucine scissors edition Revised year 1997 publisher Portland Press volume location London ... 06 24 title The leucine zipper a hypothetical structure common to a new class of DNA binding proteins ... Leucine zippers Transcription factors g1 Category Protein structural motifs Category DNA binding substances ... more details
enzyme Name leucine 2,3 aminomutase EC number 5.4.3.7 CAS number 59125 53 0 IUBMB EC number 5 4 3 7 GO code 0050047 image width caption In enzymology , a leucine 2,3 aminomutase EC number 5.4.3.7 is an enzyme that catalysis catalyzes the chemical reaction 2S alpha leucine math rightleftharpoons math 3R beta leucine Hence, this enzyme has one substrate biochemistry substrate , 2S alpha leucine , and one product chemistry product , 3R beta leucine . This enzyme belongs to the family of isomerase s, specifically those intramolecular transferase s transferring amino groups. The systematic name of this enzyme class is 2S alpha leucine 2,3 aminomutase . This enzyme participates in valine, leucine and isoleucine degradation . It employs one cofactor biochemistry cofactor , cobamide . References reflist 1 cite journal author Freer I, Pedrocchi Fantoni G, Picken DJ and Overton KH date 1981 title Stereochemistry of the leucine 2,3 aminomutase from tissue cultures of Andrographis paniculata journal J. Chem. Soc. Chem. volume Commun. pages 80&ndash 82 cite journal author Poston JM date 1976 title Leucine 2,3 aminomutase, an enzyme of leucine catabolism journal J. Biol. Chem. volume 251 pages 1859&ndash 63 pmid 1270414 issue 7 cite journal author Poston JM date 1976 title Coenzyme B12 dependent enzymes in potatoes leucine 2,3 aminomutase and methylmalonyl CoA mutase journal Phytochemistry journal Phytochemistry volume 17 pages 401&ndash 402 doi 10.1016 S0031 9422 00 89324 3 Category EC 5.4.3 Category Cobamide enzymes Category Enzymes of unknown structure isomerase stub ... 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
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 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 leucine N acetyltransferase EC number 2.3.1.66 CAS number 75496 56 9 IUBMB EC number 2 3 1 66 GO code 0050050 image width caption In enzymology , a leucine N acetyltransferase EC number 2.3.1.66 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA L leucine math rightleftharpoons math CoA N acetyl L leucine Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and L leucine , whereas its two product chemistry products are coenzyme A CoA and N acetyl L leucine . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl CoA L leucine N acetyltransferase . This enzyme is also called leucine acetyltransferase . References reflist 1 cite journal author Suzukake S, Hayashi H, Hori M and Umezawa H date 1982 title Biosnthesis of leupeptin III. Isolation and properties of an enzyme synthesizing acetyl L leucine journal J. Antibiot. volume 33 pages 857&ndash 862 transferase stub Category EC 2.3.1 Category Enzymes of unknown structure it Leucina N acetiltransferasi ... more details
refimprove date February 2008 Leucine responsive protein , or Lrp , ref name pmid17223133 cite journal author de los Rios S, Perona JJ title Structure of the Escherichia coli leucine responsive regulatory protein Lrp reveals a novel octameric assembly journal J. Mol. Biol. volume 366 issue 5 pages 1589 602 year 2007 month March pmid 17223133 pmc 1933502 doi 10.1016 j.jmb.2006.12.032 url http linkinghub.elsevier.com retrieve pii S0022 2836 06 01707 4 ref is a global regulator protein , meaning that it regulates the biosynthesis of leucine , as well as the other branched chain amino acids , valine and isoleucine . In bacteria , it is encoded by the lrp gene . Lrp alternatively activates and represses the expression of acetolactate synthase s ALS several isoenzymes . Lrp, in E. coli, along with DAM plays a role in the regulation of the pap operon , pylonephritis associated pili . I m too lazy busy to look up refs for this, but you can find most of them from the article Metabolic engineering of E coli for the production of valine based on transcriptome analysis and in silico gene knockout simulation by Park et al., 2007 References reflist External links MeshName Leucine Responsive Regulatory Protein Category Proteins biochemistry stub ... more details
enzyme Name leucine tRNA ligase EC number 6.1.1.4 CAS number 9031 15 6 IUBMB EC number 6 1 1 4 GO code 0004823 image width caption In enzymology , a leucine tRNA ligase EC number 6.1.1.4 is an enzyme that catalysis catalyzes the chemical reaction ATP L leucine tRNALeu math rightleftharpoons math AMP diphosphate L leucyl tRNALeu The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L leucine , and tRNA Leu , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L leucyl tRNA Leu . This enzyme belongs to the family of ligase s, specifically those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L leucine tRNALeu ligase AMP forming . Other names in common use include leucyl tRNA synthetase , leucyl transfer ribonucleate synthetase , leucyl transfer RNA synthetase , leucyl transfer ribonucleic acid synthetase , leucine tRNA synthetase , and leucine translase . This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl trna biosynthesis . Structural studies As of late 2007, 5 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1WKB , PDB link 1WZ2 , PDB link 2AJG , PDB link 2AJH , and PDB link 2AJI . See also Leucyl tRNA synthetase 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 journal author Bergmann FH, Berg P and Dieckmann M date 1961 title The enzymic ... more details
Rfam box acc RF00512 description Leucine operon leader abbreviation Leu leader avg length 145.00 avg identity 75.00 type Cis reg leader se Bateman A ss Published PMID 6186194 release 10.0 The Leucine operon leader is an cis regulatory element RNA element found upstream of the first gene in the Leucine biosynthetic operon . ref name pmid6186194 cite journal author Kolter R, Yanofsky C title Attenuation in amino acid biosynthetic operons journal Annu. Rev. Genet. volume 16 issue pages 113 34 year 1982 pmid 6186194 doi 10.1146 annurev.ge.16.120182.000553 issn ref The leader sequence can assume two different secondary structures known as the terminator and the anti terminator structure. The leader also codes for very short peptide sequence that is rich in leucine amino acid. The terminator structure is recognised as a termination signal for RNA polymerase and the operon is not transcribed. This structure forms when the cell has an excess of leucine and ribosome movement over the leader transcript is not impeded. ref name pmid6186194 When there is a deficiency of the charged leucyl tRNA the ribosome translation translating the leader peptide stalls and the antiterminator structure can form. This allows RNA polymerase to transcribe the operon. ref name pmid6186194 At least 6 amino acid operons are known to be regulated by attenuation. ref name pmid6186194 References reflist 1 External links Rfam id RF00512 name Leucine operon leader Category Cis regulatory RNA elements molecular cell biology stub ... more details
Pfam box Symbol LRR 1 Name image 2bnh topview.png width caption An example of a leucine rich repeat protein, a pig porcine ribonuclease inhibitor Pfam PF00560 Pfam clan CL0022 InterPro IPR001611 SMART Prosite SCOP 2bnh TCDB OPM family OPM protein 1xwd PDB PDB3 1ogq A 155 177 PDB3 1jl5 A 358 382 PDB3 1g9u A 358 382 PDB3 1k5d F 123 149 PDB3 2ca6 A 123 149 PDB3 1yrg A 123 149 PDB3 1k5g F 123 149 PDB3 1k15 A 165 187 PDB3 1m0z A 165 187 PDB3 1u0n D 165 187 PDB3 1qyy G 165 187 PDB3 1sq0 B 165 187 PDB3 1m10 B 165 187 PDB3 1ook G 165 187 PDB3 1k13 A 165 187 PDB3 1p9a G 165 187 PDB3 1p8v A 165 187 PDB3 1k14 A 165 187 PDB3 1ziw A 563 585 PDB3 2a0z A 563 585 PDB3 1wwl A 292 318 PDB3 1p8t A 131 153 PDB3 1ozn A 131 153 PDB3 1xum 54 75 PDB3 1xcd A 131 149 PDB3 1xec B 131 149 PDB3 1xku A 131 149 PDB3 1xwd C 194 217 PDB3 1xun 194 217 PDB3 1o6s A 274 294 PDB3 1koh B 292 315 PDB3 1fo1 B 292 315 PDB3 1ft8 D ... 618 PDB3 1a9n A 89 109 A leucine rich repeat LRR is a protein structural motif that forms an ... The leucine rich repeat a versatile binding motif journal Trends Biochem. Sci. volume 19 issue ... Structural principles of leucine rich repeat LRR proteins journal Proteins volume 54 issue 3 pages ... of repeating 20 30 amino acid stretches that are unusually rich in the hydrophobic amino acid leucine ... steric ally packed with leucine residues. Leucine rich repeats are frequently involved in the formation ... The leucine rich repeat as a protein recognition motif journal Curr. Opin. Struct. Biol. volume ... journal author Gay NJ, Packman LC, Weldon MA, Barna JC title A leucine rich repeat peptide derived ... T url http linkinghub.elsevier.com retrieve pii 0014 5793 91 81110 T issn ref Examples Leucine .... See also Leucine zipper References Reflist 2 Further reading cite book author Tooze, John Br nd n ... title LRRML a conformational database and an XML description of leucine rich repeats LRRs journal BMC ... http tollml.lrz.de LRRML a conformational database of leucine rich repeats Protein domains ... more details
OrganicBox complete wiki name Leucine name S 2 amino 4 methyl pentanoic acid GENERAL INFORMATION C 6 H 13 N 1 O 2 mass 131.18 abbreviation L, Leu image Image L leucine skeletal.png 130px Chemical structure of Leucine Image L leucine 3D sticks.png 230px Chemical structure of Leucine synonyms S L 2 amino 4 methylvaleric acid br 4 methyl norvaline br aminoisocaproic acid DATABASES SMILES CC C C C H C O O N ref 1 a InChI 1 C6H13NO2 c1 4 2 3 5 7 6 8 9 h4 5H,3,7H2,1 2H3, H,8,9 t5 m0 s1 f h8H ref 1 b ATC prefix ATC suffix ATC supplemental CAS 61 90 5 DrugBank EINECS 200 522 0 PubChem 6106 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 1.165 melting point C 293 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 c isoelectric point 5.98 ref 1 d disociation constant 2.32 9.58 ref 1 e tautomers H bond donor 2 H bond acceptor 3 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 PubChem 6106 refend AminoAcids Category Branched chain amino acids Category Essential amino acids Category Chemical data pages ar ... more details
Basic helix loop helix leucine zipper transcription factors are, as their name indicates, transcription factors containing both Basic helix loop helix and leucine zipper motifs. An example is Microphthalmia associated transcription factor . Another example is the Sterol regulatory element binding protein SREBP . External links MeshName Basic helix loop helix leucine zipper transcription factors Category Gene expression Category Transcription factors genetics stub Transcription factors g1 ... more details
PBB geneid 8125 Acidic leucine rich nuclear phosphoprotein 32 family member A is a protein that in humans is encoded by the ANP32A gene . ref name pmid8970164 cite journal author Chen TH, Brody JR, Romantsev FE, Yu JG, Kayler AE, Voneiff E, Kuhajda FP, Pasternack GR title Structure of pp32, an acidic nuclear protein which inhibits oncogene induced formation of transformed foci journal Mol Biol Cell volume 7 issue 12 pages 2045 56 year 1997 month Mar pmid 8970164 pmc 276049 doi ref ref name pmid9144194 cite journal author Ulitzur N, Humbert M, Pfeffer SR title Mapmodulin a possible modulator of the interaction of microtubule associated proteins with microtubules journal Proc Natl Acad Sci U S A volume 94 issue 10 pages 5084 9 year 1997 month Jun pmid 9144194 pmc 24635 doi 10.1073 pnas.94.10.5084 ref ref cite web title Entrez Gene ANP32A Acidic leucine rich nuclear phosphoprotein 32 family, member A url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 8125 accessdate ref It is one of the targets of an oncomiR, MIRN21 . The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text Interactions Acidic leucine rich nuclear phosphoprotein 32 family member A has been shown to Protein protein interaction interact with MAP1B , ref name pmid12807913 cite journal last Opal first Puneet authorlink coauthors Garcia Jesus J, Propst Friedrich, Matilla Antoni, Orr Harry T, Zoghbi Huda Y year 2003 month Sep. title Mapmodulin leucine rich acidic nuclear protein binds the light chain of microtubule associated protein 1B and modulates neuritogenesis journal J. Biol. Chem. volume 278 issue 36 pages 34691 9 publisher location United States issn 0021 9258 pmid 12807913 doi ... journal author Matilla A, Radrizzani M title The Anp32 family of proteins containing leucine rich ... Cite journal author Matilla A, Koshy BT, Cummings CJ, et al. title The cerebellar leucine rich acidic ... more details
Move to Commons By Richard Wheeler Zephyris 2006. For the Wikipedia Wikiproject Metabolic Pathways metabolic pathways wikiproject. Licensing GFDL self with disclaimers migration relicense ... more details
SLRP may be an abbreviation for Soluble low density lipoprotein receptor related protein Small leucine rich repeat protein Small leucine rich repeat proteoglycan disambig ... more details
UUG , according to the genetic code , is Leucine . UUG is an acronym for Uniface Users Group Universal Underwriters Group Unix User Group disambig de UUG fr UUG ... 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 ... g mol center category amino acids de Leucine ... more details
LRR may refer to Laminated root rot , a root disease in conifers Leucine rich repeat , a type of protein domain LoadingReadyRun , a Canadian comedy troupe Low rolling resistance tires , a type of tires designed for fuel efficiency See also LR disambiguation Lrrr disambiguation dab ... more details
E641 or E 641 may be the E number of the flavour enhancer L leucine European route E641 , a European route class B road connecting the Austrian cities of W rgland and Salzburg via Sankt Johann in Tirol and Bad Reichenhall in Germany Letter NumberCombDisambig ... 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
Unreferenced date December 2009 The heptad repeat is an example of a structural motif that consists of a repeating pattern of seven amino acid s a b c d e f g H P P H C P C where H represents hydrophobic residues, C represents, typically, charged residues, and P represents Chemical polarity polar and, therefore, hydrophilic residues. The positions of the heptad repeat are commonly denoted by the lowercase letters a through g . These motifs are the basis for most coiled coil s and, in particular, leucine zipper s, which have predominantly leucine in the d position of the heptad repeat. DEFAULTSORT Heptad Repeat Category Protein structural motifs ... more details
enzyme Name N alpha benzyloxycarbonylleucine hydrolase EC number 3.5.1.64 CAS number 100630 47 5 IUBMB EC number 3 5 1 64 GO code 0047413 image width caption In enzymology , a Nalpha benzyloxycarbonylleucine hydrolase EC number 3.5.1.64 is an enzyme that catalysis catalyzes the chemical reaction Nalpha benzyloxycarbonyl L leucine H sub 2 sub O math rightleftharpoons math benzyl alcohol CO sub 2 sub L leucine Thus, the two substrate biochemistry substrates of this enzyme are Nalpha benzyloxycarbonyl L leucine and water H sub 2 sub O , whereas its 3 product chemistry products are benzyl alcohol , carbon dioxide CO sub 2 sub , and L leucine . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is Nalpha benzyloxycarbonyl L leucine urethanehydrolase . Other names in common use include benzyloxycarbonylleucine hydrolase , Nalpha benzyloxycarbonyl amino acid urethane hydrolase IV , and alpha N benzyloxycarbonyl L leucine urethanehydrolase . References reflist 1 cite journal author Matsumura E, Shin T, Murao S, Sakaguchi M and Kawano T date 1985 title A novel enzyme, Nalpha benzyloxycarbonyl amino acid urethane hydrolase IV journal Agric. Biol. Chem. volume 49 pages 3643&ndash 3645 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
enzyme Name 2 aminohexanoate transaminase EC number 2.6.1.67 CAS number 111310 35 1 IUBMB EC number 2 6 1 67 GO code 0047537 image width caption In enzymology , a 2 aminohexanoate transaminase EC number 2.6.1.67 is an enzyme that catalysis catalyzes the chemical reaction L 2 aminohexanoate 2 oxoglutarate math rightleftharpoons math 2 oxohexanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L 2 aminohexanoate and 2 oxoglutarate , whereas its two product chemistry products are 2 oxohexanoate 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 2 aminohexanoate 2 oxoglutarate aminotransferase . Other names in common use include norleucine transaminase , norleucine leucine aminotransferase , and leucine L norleucine 2 oxoglutarate aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Der Garabedian PA, Vermeersch JJ date 1987 title Candida L norleucine,leucine 2 oxoglutarate aminotransferase Purification and properties journal Eur. J. Biochem. volume 167 pages 141&ndash 7 pmid 3622507 doi 10.1111 j.1432 1033.1987.tb13315.x issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
protein Name mitochondrially encoded tRNA leucine 2 CUN caption image width HGNCid 7491 Symbol MT TL2 AltSymbols MTTL2 EntrezGene 4568 OMIM RefSeq NC 001807 UniProt PDB ECnumber Chromosome MT Arm Band LocusSupplementaryData Mitochondrially encoded tRNA leucine 2 CUN also known as MT TL2 is a transfer RNA which in humans is encoded by the mitochondrion mitochondrial MT TL2 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 TL2 is a small 71 nucleotide RNA human mitochondrial map position 12266 12336 that transfers the amino acid leucine to a growing polypeptide chain at the ribosomal ribosome site of protein synthesis during translation genetics translation . References Reflist Mitochondrial enzymes genetics stub ... more details
KDEL is a sequence in the amino acid structure of a protein which keeps it from secreting from the endoplasmic reticulum ER . It also targets proteins from other locations such as the cytoplasm to the ER. Proteins can only leave the ER after this sequence has been cleaved off. The KDEL sequence is responsible for retrieval of ER luminal proteins from the Golgi apparatus . The word KDEL is formed by the corresponding letters to each amino acid being This letter system was defined by the IUPAC and IUBMB in 1983 K Lysine D Aspartic acid E Glutamic acid L Leucine Therefore being the sequence Lysine Lys Aspartic acid Asp Glutamic acid Glu Leucine Leu . References http www.ebi.ac.uk 2can biology molecules small aatable.html See also ER retention Endoplasmic reticulum protein retention receptors KDELR1 KDELR2 KDELR3 Category Amino acids Molecular biology stub ... more details
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