chembox UNII Ref fdacite correct FDA UNII 2ZD004190S verifiedrevid 459442141 Name Threonine ImageFile L Threonin L Threonine.svg ImageSize 180px ImageName Skeletal formula ImageFile1 L Threonine 3D balls.png ImageSize1 160px ImageName1 Ball and stick model IUPACName Threonine OtherNames 2 Amino 3 hydroxybutanoic ..., g dl 10.6 30 ,14.1 52 ,19.0 61 Section3 Chembox Hazards EUIndex FlashPt Autoignition Threonine abbreviated ... amino acid is classified as Chemical polarity polar . Together with serine , threonine is one ... with isoleucine . The threonine residue is susceptible to numerous posttranslational modification s. The Hydroxyl hydroxy side chain can undergo O linked glycosylation . In addition, threonine residues undergo phosphorylation through the action of a threonine kinase . In its phosphorylated form, it can be referred to as phosphothreonine . History Threonine was discovered as the last of the 20 ... 120px br small L small Threonine 2 S ,3 R and small D small Threonine 2 R ,3 S br File L allo Threonine.svg 120px File D allo Threonine.svg 120px br small L small allo Threonine 2 S ,3 S and small D small allo Threonine 2 R ,3 R Threonine is one of two amino acids out of the twenty with two Chirality chemistry chiral centers. Threonine can exist in four possible stereoisomer s with the following ... threonine is used for one single diastereomer , 2 S ,3 R 2 amino 3 hydroxybutanoic acid. The second stereoisomer 2 S ,3 S , which is rarely present in nature, is called small L small allo threonine .... Biosynthesis As an essential amino acid, threonine is not synthesized in humans, hence we must ingest threonine in the form of threonine containing proteins. In plants and microorganisms, threonine ... group. ref Lehninger3rd . ref Enzymes involved in a typical biosynthesis of threonine include aspartokinase aspartate semialdehyde dehydrogenase homoserine dehydrogenase homoserine kinase threonine synthase . Image Thr biosynthesis.gif thumb center 600px Threonine biosynthesis Metabolism Threonine ... more details
enzyme Name threonine racemase EC number 5.1.1.6 CAS number 9024 11 7 IUBMB EC number 5 1 1 6 GO code 0018114 image width caption In enzymology , a threonine racemase EC number 5.1.1.6 is an enzyme that catalysis catalyzes the chemical reaction L threonine math rightleftharpoons math D threonine Hence, this enzyme has one substrate biochemistry substrate , L threonine , and one product chemistry product , D threonine . This enzyme belongs to the family of isomerase s, specifically those racemase s and epimerase s acting on amino acid s and derivatives. The systematic name of this enzyme class is threonine racemase . References reflist 1 cite journal author Amos H date 1954 title A racemase for threonine in Escherichia coli journal J. Am. Chem. Soc. volume 76 pages 3858 doi 10.1021 ja01643a083 issue 14 isomerase stub Category EC 5.1.1 Category Enzymes of unknown structure ... more details
enzyme Name threonine synthase EC number 4.2.3.1 CAS number 9023 97 6 IUBMB EC number 4 2 3 1 GO code 0004795 image width caption In enzymology , a threonine synthase EC number 4.2.3.1 is an enzyme that catalysis catalyzes the chemical reaction O phospho L homoserine H sub 2 sub O math rightleftharpoons math L threonine phosphate Thus, the two substrate biochemistry substrates of this enzyme are O phospho L homoserine and water H sub 2 sub O , whereas its two product chemistry products are L threonine and phosphate . This enzyme belongs to the family of lyase s, specifically those carbon oxygen lyases acting on phosphates. The systematic name of this enzyme class is O phospho L homoserine phosphate lyase adding water L threonine forming . Other names in common use include threonine synthetase , and O phospho L homoserine phospho lyase adding water . This enzyme participates in glycine, serine and threonine metabolism and vitamin B6 vitamin B sub 6 sub metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1UIM , PDB link 1UIN , PDB link 1V7C , PDB link 1VB3 , PDB link 2C2B , PDB link 2C2G , and PDB link 2D1F . References reflist 1 cite journal author FLAVIN M, SLAUGHTER C date 1960 title Purification and properties of threonine synthetase of Neurospora journal J. Biol. Chem. volume 235 pages 1103&ndash 8 pmid 13823379 4.2 enzyme stub Category EC 4.2.3 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name threonine aldolase EC number 4.1.2.5 CAS number 62213 23 4 IUBMB EC number 4 1 2 5 GO code 0004793 image width caption protein name threonine aldolase 1 pseudogene caption image width HGNCid 18004 Symbol THA1P AltSymbols EntrezGene 390816 OMIM RefSeq XM 372682 UniProt PDB ECnumber Chromosome 17 Arm q Band 25.3 LocusSupplementaryData In enzymology , a threonine aldolase EC number 4.1.2.5 is an enzyme that catalysis catalyzes the chemical reaction L threonine math rightleftharpoons math glycine acetaldehyde Hence, this enzyme has one substrate biochemistry substrate , L threonine , and two product chemistry products , glycine and acetaldehyde . This enzyme belongs to the family of lyase s, specifically the aldehyde lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is L threonine acetaldehyde lyase glycine forming . This enzyme is also called L threonine acetaldehyde lyase . This enzyme participates in glycine, serine and threonine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . 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 1JG8 , PDB link 1LW4 , PDB link 1LW5 , PDB link 1M6S , and PDB link 1SVV . References reflist 1 cite journal author Bell SC and Turner JM date 1973 title Bacterial threonine aldolase and serine hydroxymethyltransferase enzyme journal Biochem. Soc. Trans. volume 1 pages 678&ndash 681 cite journal author KARASEK MA, GREENBERG DM date 1957 title Studies on the properties of threonine aldolases journal J. Biol. Chem. volume 227 pages 191&ndash 205 pmid 13449064 issue 1 cite journal author Kumagai H, Nagate T, Yoshida H, Yamada H date 1972 title Threonine aldolase from Candida humicola. II. Purification, crystallization and properties journal Biochim. Biophys. Acta. volume 258 pages 779&ndash 90 pmid 5017702 issue 3 4.1 enzyme stub Amino acid metabolism enzymes ... more details
Infobox protein family Symbol Thr Name Threonine Protease image Protein PSMA1 PDB 1iru.png image source Protein Data Bank PDB rendering based on 1iru. PDB PDB2 1iru width caption Crystal structure of human proteasome alpha 1 Pfam Pfam clan InterPro SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein PDB Threnonine proteases are a family of proteolytic enzyme s harbouring a threonine Thr residue within the active site. The prototype members of this class of enzymes are the catalysis catalytic subunits of the proteasome . Category Enzymes biochem stub ... more details
enzyme Name L threonine 3 dehydrogenase EC number 1.1.1.103 CAS number 9067 99 6 IUBMB EC number 1 1 1 103 GO code 0008743 image width caption In enzymology , a L threonine 3 dehydrogenase EC number 1.1.1.103 is an enzyme that catalysis catalyzes the chemical reaction L threonine NAD sup sup math rightleftharpoons math L 2 amino 3 oxobutanoate NADH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are L threonine and nicotinamide adenine dinucleotide NAD sup sup , whereas its 3 product chemistry products are L 2 amino 3 oxobutanoate , 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 L threonine NAD oxidoreductase . Other names in common use include L threonine dehydrogenase , threonine 3 dehydrogenase , and threonine dehydrogenase . This enzyme participates in glycine, serine and threonine metabolism . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2D8A , PDB link 2DFV , and PDB link 2DQ4 . References reflist 1 cite journal author Green ML, Elliott WH date 1964 title The enzymic formation of aminoacetone from threonine and its further metabolism journal Biochem. J. volume 92 pages 537&ndash 49 pmid 4284408 issue 3 pmc 1206098 cite journal author HARTSHORNE D, GREENBERG DM date 1964 title STUDIES ON LIVER THREONINE DEHYDROGENASE journal Arch. Biochem. Biophys. volume 105 pages 173&ndash 8 pmid 14165492 doi 10.1016 0003 9861 64 90250 4 1.1.1 enzyme stub Category EC 1.1.1 Category NADH dependent enzymes Category Enzymes of known structure it L treonina 3 deidrogenasi ja L 3 ... more details
enzyme Name L threonine ammonia lyase EC number 4.3.1.19 CAS number IUBMB EC number 4 3 1 19 GO code 0004794 image width caption In enzymology , a threonine ammonia lyase EC number 4.3.1.19 is an enzyme that catalysis catalyzes the chemical reaction L threonine math rightleftharpoons math 2 oxobutanoate NH sub 3 sub Hence, this enzyme has one substrate biochemistry substrate , L threonine , and two product chemistry products , Alpha Ketobutyric acid and ammonia NH sub 3 sub . This enzyme belongs to the family of lyase s, specifically ammonia lyases, which cleave carbon nitrogen bonds. The systematic name of this enzyme class is L threonine ammonia lyase 2 oxobutanoate forming . Other names in common use include threonine deaminase , L serine dehydratase , serine deaminase , L threonine dehydratase , threonine dehydrase , L threonine deaminase , threonine dehydratase , L threonine hydro lyase deaminating , and L threonine ammonia lyase . This enzyme participates in glycine, serine and threonine metabolism and valine, leucine and isoleucine biosynthesis . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Enzyme Regulation This protein may use the morpheein model of allosteric regulation . ref name pmid22182754 cite journal author T. Selwood and E. K. Jaffe. title Dynamic dissociating homo oligomers and the control of protein function. journal Arch. Biochem. Biophys. volume 519 issue 2 pages 131 43 year 2011 pmid 22182754 url http www.ncbi.nlm.nih.gov entrez query.fcgi?cmd Retrieve&db PubMed&dopt Citation&list uids 22182754 doi 10.1016 j.abb.2011.11.020 ref ... Purification and characterization of a B6 independent threonine dehydratase from Pseudomonas putida ... journal author NISHIMURA JS, GREENBERG DM date 1961 title Purification and properties of L threonine ... threonine dehydrase journal J. Biol. Chem. volume 240 pages 4703&ndash 9 pmid 5321308 issue 12 ... 5 monophosphate dependent threonine deaminase from Escherichia coli journal J. Biol. Chem. volume ... more details
enzyme Name L Threonine dehydrogenase EC number 1.1.1.103 CAS number 9067 99 6 IUBMB EC number 1 1 1 103 GO code 0008743 image width caption protein name L Threonine dehydrogenase caption image width HGNCid 15547 Symbol TDH AltSymbols EntrezGene 157739 OMIM RefSeq NM 152566 UniProt Q8IZJ6 PDB ECnumber 1.1.1.103 Chromosome 8 Arm p Band 23.1 LocusSupplementaryData L Threonine dehydrogenase is an enzyme that facilitates the catabolism of threonine . It catalyses its conversion to glycine via 2 amino 3 ketobutyrate with concomitant reduction of NAD . References cite journal author Epperly BR, Dekker EE title L threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies journal J. Biol. Chem. volume 266 issue 10 pages 6086 92 year 1991 month April pmid 2007567 doi url http www.jbc.org cgi pmidlookup?view long&pmid 2007567 cite journal author Edgar AJ title The human L threonine 3 dehydrogenase gene is an expressed pseudogene journal BMC Genet. volume 3 pages 18 year 2002 month October pmid 12361482 doi 10.1186 1471 2156 3 18 url http www.biomedcentral.com 1471 2156 3 18 pmc 131051 biochem stub Amino acid metabolism enzymes Alcohol oxidoreductases ... more details
enzyme Name threonine phosphate decarboxylase EC number 4.1.1.81 CAS number IUBMB EC number 4 1 1 81 GO code 0048472 image width caption In enzymology , a threonine phosphate decarboxylase EC number 4.1.1.81 is an enzyme that catalysis catalyzes the chemical reaction phosphothreonine L threonine O 3 phosphate math rightleftharpoons math R 1 aminopropan 2 yl phosphate CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , L threonine O 3 phosphate , and two product chemistry products , R 1 aminopropan 2 yl phosphate and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is L threonine O 3 phosphate carboxy lyase R 1 aminopropan 2 yl phosphate forming . Other names in common use include L threonine O 3 phosphate decarboxylase , CobD , and L threonine O 3 phosphate carboxy lyase . This enzyme participates in porphyrin and chlorophyll metabolism. References reflist 1 cite journal author Cheong CG, Bauer CB, Brushaber KR, Escalante Semerena JC, Rayment I date 2002 title Three dimensional structure of the L threonine O 3 phosphate decarboxylase CobD enzyme from Salmonella enterica journal Biochemistry. volume 41 pages 4798&ndash 808 pmid 11939774 doi 10.1021 bi012111w issue 15 cite journal author O Toole GA, Escalante Semerena JC date 1995 title Purification and characterization of the bifunctional CobU enzyme of Salmonella typhimurium LT2. Evidence for a CobU GMP intermediate journal J. Biol. Chem. volume 270 pages 23560&ndash 9 pmid 7559521 doi 10.1074 jbc.270.40.23560 issue 40 cite journal author Warren MJ, Raux E, Schubert HL, Escalante Semerena JC date 2002 title The biosynthesis of adenosylcobalamin vitamin B12 journal Nat. Prod. Rep. volume 19 pages 390&ndash 412 pmid 12195810 doi 10.1039 b108967f issue 4 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of unknown structure ... more details
PBB geneid 140901 Serine threonine kinase 35 is a protein that in humans is encoded by the STK35 gene . ref name entrez cite web title Entrez Gene Serine threonine kinase 35 url http www.ncbi.nlm.nih.gov sites entrez?db gene&cmd retrieve&list uids 140901 accessdate 2012 02 18T18 49 54.823 08 00 ref The protein encoded by this gene is a kinase that is predominantly found in the nucleus. However, it can interact with PDLIM1 CLP 36 in the cytoplasm and localize to actin stress fibers. The encoded protein may be a regulator of actin stress fibers in nonmuscle cells. provided by RefSeq, Jul 2008 . ref name entrez cite web title Entrez Gene Serine threonine kinase 35 url http www.ncbi.nlm.nih.gov sites entrez?db gene&cmd retrieve&list uids 140901 accessdate 2012 02 18T18 49 54.823 08 00 ref References reflist Further reading refbegin 2 Cite pmid 11973348 Cite pmid 19756140 Cite pmid 21283756 refend gene 20 stub ... more details
enzyme Name threonine tRNA ligase EC number 6.1.1.3 CAS number 9023 46 5 IUBMB EC number 6 1 1 3 GO code 0004829 image width caption In enzymology , a threonine tRNA ligase EC number 6.1.1.3 is an enzyme that catalysis catalyzes the chemical reaction ATP L threonine tRNAThr math rightleftharpoons math AMP diphosphate L threonyl tRNAThr The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L threonine , and tRNA Thr , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L threonyl tRNA Thr . 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 threonine tRNAThr ligase AMP forming . Other names in common use include threonyl tRNA synthetase , threonyl transfer ribonucleate synthetase , threonyl transfer RNA synthetase , threonyl transfer ribonucleic acid synthetase , threonyl ribonucleic synthetase , threonine transfer ribonucleate synthetase , threonine translase , threonyl tRNA synthetase , and TRS . This enzyme participates in glycine, serine and threonine metabolism and aminoacyl trna biosynthesis . Structural studies As of late 2007, 17 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EVK , PDB link 1EVL , PDB link 1FYF , PDB link 1KOG , PDB link 1NYQ , PDB link 1NYR , PDB link 1QF6 , PDB link 1TJE , PDB link 1TKE , PDB link 1TKG , PDB link 1TKY , PDB link 1WWT , PDB link 1Y2Q , PDB link 2HKZ , PDB link 2HL0 , PDB link 2HL1 , and PDB link 2HL2 . 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 HOLLEY RW, BRUNNGRABER EF, SAAD F, WILLIAMS HH date 1961 title Partial purification of the threonine ... more details
Protein serine threonine phosphatase PSP ref name pmid19879837 cite journal author Shi Y title Serine threonine phosphatases mechanism through structure journal Cell volume 139 issue 3 pages 468 84 year 2009 month October pmid 19879837 doi 10.1016 j.cell.2009.10.006 url http linkinghub.elsevier.com retrieve pii S0092 8674 09 01254 9 ref is a form of phosphoprotein phosphatase that acts upon serine threonine residues. Serine and threonine phosphates are stable under physiological conditions, so a phosphatase has to remove the phosphate to reverse the regulation. Ser Thr specific protein phosphatases are regulated by their location within the cell biology cell and by specific Enzyme inhibitor inhibitor proteins. Examples There are several known groups with numerous members in each PPP1 , , 1, 2 Protein Phosphatase 2 PPP2 formerly 2A Calcineurin PPP3 formerly 2b, also known as calcineurin PPP2C PPP4C PPP4 PPP5C PPP5 PPP6C PPP6 links are to the catalytic subunit All but PPP2C have sequence homology in the enzyme catalytic domain protein domain , but differ in substrate specificity. Citation needed date November 2008 References reflist External links EC number 3.1.3.16 Esterases Intracellular signaling peptides and proteins Category Enzymes biochem stub ... more details
OrganicBox complete GENERAL wiki name Threonine image Image L threonine skeletal.png 110px Skeletal structure of small L small Threonine Image L threonine 3D sticks.png 130px 3D structure of small L small Threonine name 2S,3R 2 Amino 3 hydroxybutanoic acid C 4 H 9 N 1 O 3 mass 119.12 abbreviation T, Thr synonyms DATABASES SMILES CC O C N C O O InChI 1 C4H9NO3 c1 2 6 3 5 4 7 8 h2 3,6H,5H2,1H3, H,7,8 t2 ,3 m1 s1 f h7H CAS 72 19 5 DrugBank EINECS 200 774 1 ref 1 a PubChem 69435 D ref 2 a , 6288 L ref 3 a Structure and properties index of refraction abbe number dielectric constant magnetic susceptibility Spectral data lambda max extinction coefficient absorption bands proton NMR carbon NMR other NMR mass spectrometry Phase behaviour triple point K triple point C triple point Pa criticle point K criticle point C criticle point Pa delta fus H o delta fus S o delta vap H o delta vap S o Solid properties delta f H o S o solid heat capacity solid density solid melting point C 256 melting point F melting point K Liquid properties delta f H o liquid S o liquid heat capacity liquid density liquid viscosity liquid boiling point C boiling point F boiling point K Gas properties delta f H o gas 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 3.036 isoelectric point 5.60 disociation constant 2.20, 8.96 tautomers H bond donor 3 H bond acceptor 4 References note 1 a EINECSLink 200 774 1 Threonine note 2 a PubChemLink 69435 D Threonine note 3 a PubChemLink 6288 L Threonine AminoAcids Category Chemical data pages ar ... more details
Infobox rfam Name Threonine operon leader image RF00506.jpg width caption Predicted secondary structure and sequence conservation of Thr leader Symbol Thr leader AltSymbols Rfam RF00506 miRBase miRBase family RNA type Cis regulatory element Cis reg leader Tax domain Bacteria GO SO SO 0000233 CAS number EntrezGene HGNCid OMIM PDB RefSeq Chromosome Arm Band LocusSupplementaryData The threonine operon leader is an cis regulatory element RNA element . Threonine is one of at least 6 amino acid operon s are known to be regulated by Attenuator genetics attenuation . ref name kolter 1982 cite journal last Kolter first R coauthors Yanofsky C year 1982 title Attenuation in amino acid biosynthetic operons journal Annu Rev Genet volume 16 pages 113&ndash 134 pmid 6186194 doi 10.1146 annurev.ge.16.120182.000553 ref In each a leader sequence of 150 200 bp is found upstream of the first gene in the operon. This leader sequence can assume two different secondary structures known as the terminator and the anti terminator structure. In each case the leader also codes for very short peptide sequence that is rich in the end product amino acid of the operon. 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 the regulatory amino acid and ribosome movement over the leader transcript is not impeded. ref name kolter 1982 When there is a deficiency of the charged tRNA of the regulatory amino acid the ribosome translating the leader peptide stalls and the antiterminator structure can form. This allows RNA polymerase to transcribe the operon. ref name kolter 1982 References reflist 1 External links Rfam id RF00506 name Threonine operon leader Category Cis regulatory RNA elements molecular cell biology stub ... more details
enzyme Name Fas activated serine threonine kinase EC number 2.7.11.8 CAS number IUBMB EC number 2 7 11 8 GO code image width caption In enzymology , a Fas activated serine threonine kinase EC number 2.7.11.8 is an enzyme that catalysis catalyzes the chemical reaction ATP Fas activated serine threonine protein math rightleftharpoons math ADP Fas activated serine threonine phosphoprotein Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and Fas activated serine threonine protein , whereas its two product chemistry products are adenosine diphosphate ADP and Fas activated serine threonine phosphoprotein . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups protein serine threonine kinases. The systematic name of this enzyme class is ATP Fas activated serine threonine protein phosphotransferase . Other names in common use include FAST , FASTK , and STK10 . References reflist 1 cite journal author Tian Q, Taupin J, Elledge S, Robertson M, Anderson P date 1995 title Fas activated serine threonine kinase FAST phosphorylates TIA 1 during Fas mediated apoptosis journal J. Exp. Med. volume 182 pages 865&ndash 74 pmid 7544399 doi 10.1084 jem.182.3.865 issue 3 pmc 2192163 cite journal author Li W, Simarro M, Kedersha N, Anderson P date 2004 title FAST is a survival protein that senses mitochondrial stress and modulates TIA 1 regulated changes in protein expression journal Mol. Cell. Biol. volume 24 pages 10718&ndash 32 pmid 15572676 doi 10.1128 MCB.24.24.10718 10732.2004 issue 24 pmc 533970 enzyme stub Category EC 2.7.11 Category Enzymes of unknown structure ... more details
Cleanup date September 2007 infobox enzyme Name Non specific serine threonine protein kinase EC number 2.7.11.1 CAS number 9026 43 1 IUBMB EC number 2 7 11 1 GO code 0004682 image Protein AURKA PDB 1mq4.png width caption Human Aurora Kinase Protein Data Bank PDB PDBe 1mq4 ref cite pmid 12467573 ref Image L serine skeletal.png thumb serine Image L threonine skeletal.png thumb threonine Image Phosphate Group.PNG right thumb phosphate A serine threonine protein kinase EC number 2.7.11.1 is a kinase enzyme that phosphorylates the OH group of serine or threonine which have similar sidechains . At least 125 of the 500 human protein kinases are serine threonine kinases STK . ref name Capra Regulation Serine Threonine Kinase receptors plays a role in the regulation of cell proliferation, programmed cell death apoptosis , cell differentiation, and embryonic development. Selectivity While serine threonine kinases all phosphorylate serine or threonine residues in their substrates, they select specific residues to phosphorylate on the basis of residues that flank the phosphoacceptor site, which together ... is removed, the kinase can perform its normal function. EC numbers Many serine threonine .... Types Types include those acting directly as receptors Receptor protein serine threonine kinase ... synthase kinase 3 . EC number 2.7.1.37 IRAK1 Pelle is a serine threonine kinase that can phosphorylate ... threonine kinase STK expression is altered in many types of cancer . ref name Capra http cancerres.aacrjournals.org cgi content full 66 16 8147 Frequent Alterations in the Expression of Serine Threonine Kinases in Human Cancers Capra et al. Cancer Research. 2006 ref Serine threonine protein kinase ... cgi content abstract 65 8 3108 The Serine Threonine Protein Kinase, p90 Ribosomal ... threonine kinases Kinases Serine threonine specific protein kinases Intracellular signaling peptides and proteins DEFAULTSORT Serine Threonine Specific Protein Kinase Category EC 2.7.11 Category ... more details
enzyme Name Receptor protein serine threonine kinase EC number 2.7.11.30 CAS number 146702 86 5 IUBMB EC number 2 7 11 30 GO code image width caption In enzymology , a receptor protein serine threonine kinase EC number 2.7.11.30 is an enzyme that catalysis catalyzes the chemical reaction ATP receptor protein math rightleftharpoons math ADP receptor protein phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and receptor protein , whereas its two product chemistry products are adenosine diphosphate ADP and receptor protein phosphate . This enzyme belongs to the family of transferase s, to be specific those transferring phosphorus containing groups protein serine threonine kinases. The systematic name of this enzyme class is ATP receptor protein phosphotransferase . Other names in common use include activin receptor kinase , receptor type I serine threonine protein kinase , receptor type II serine threonine protein kinase , STK13 , TGF beta kinase , and receptor serine threonine protein kinase . This enzyme participates in 7 metabolism metabolic pathways mapk signaling pathway , cytokine cytokine receptor interaction , tgf beta signaling pathway , adherens junction , colorectal cancer , pancreatic cancer , and chronic myeloid leukemia . 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 2GOO , PDB link 2H62 , PDB link 2H64 , PDB link 2HLQ , and PDB link 2HLR . References reflist 1 refbegin cite journal author Wrana JL, Attisano L, Wieser R, Ventura F, Massague J date 1994 title Mechanism of activation of the TGF beta receptor journal Nature. volume 370 pages 341&ndash 7 pmid 8047140 doi 10.1038 370341a0 issue 6488 cite journal author Massague J, Chen YG date 2000 title Controlling TGF beta signaling journal Genes ... enzyme stub Serine threonine specific protein kinases Enzyme linked receptors Category EC 2.7.11 ... more details
enzyme Name Non specific serine threonine protein kinase EC number 2.7.11.1 CAS number IUBMB EC number 2 7 11 1 GO code image width caption In enzymology , the term non specific serine threonine protein kinase EC number 2.7.11.1 describes a class of enzyme s that belong to the family of transferase s, specifically protein serine threonine kinase s. These enzymes transfer phosphates to the oxygen atom of a serine or threonine sidechain in protein s. This process is called phosphorylation . Protein phosphorylation in particular plays a significant role in a wide range of cellular processes and is a very important posttranslational modification . The chemical reaction performed by these enzymes can be written as ATP a protein math rightleftharpoons math ADP a phosphoprotein Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and a protein , whereas its two product chemistry products are adenosine diphosphate ADP and phosphoprotein . The systematic name of this enzyme class is ATP protein phosphotransferase non specific . References reflist 1 DO WE NEED THIS? cite journal author Damuni Z, Reed LJ date 1988 title Purification and properties of a protamine kinase and a type II casein kinase from bovine kidney mitochondria journal Arch. Biochem. Biophys. volume 262 pages 574&ndash 84 pmid 2835010 doi 10.1016 0003 9861 88 90408 0 issue 2 cite journal author Baggio B, Pinna LA, Moret V, Siliprandi N date 1970 title A simple procedure for the purification of rat liver phosvitin kinase journal Biochim. Biophys. Acta. volume 212 pages 515&ndash 7 pmid 5456997 issue 3 cite journal author Jergil B, Dixon GH date 1970 title Protamine kinase from rainbow trout testis. Partial purification and characterization journal J. Biol. Chem. volume 245 pages 425&ndash 34 pmid 4312674 issue 2 cite journal author Langan TA date 1969 title Action of adenosine ... 00 00308 0 Serine threonine specific protein kinases Category EC 2.7.11 Category Enzymes of known ... more details
Orphan date April 2010 YCL064C is a gene in the genome of Saccharomyces cerevisiae , the most common species of Yeast. Its function is the catalyzation of the degradation of both L serine and L threonine. In order to survive using serine or threonine as the sole nitrogen source, YCL064C must be present and functional. It is transcriptionally induced by the presence of small L small serine and small L small threonine . Category Saccharomycetes ... more details
Dual specificity phosphatase is a form of phosphatase that can act upon tyrosine or serine threonine residues. ref MeshName Dual Specificity Phosphatases ref References reflist Intracellular signaling peptides and proteins Protein tyrosine phosphatases Category Enzymes biochem stub ... more details
enzyme Name Fluorothreonine transaldolase EC number 2.2.1.8 CAS number IUBMB EC number 2 2 1 8 GO code image width caption In enzymology , a fluorothreonine transaldolase EC number 2.2.1.8 is an enzyme that catalysis catalyzes the chemical reaction L threonine fluoroacetaldehyde math rightleftharpoons math acetaldehyde 4 fluoro L threonine Thus, the two substrate biochemistry substrates of this enzyme are L threonine and fluoroacetaldehyde , whereas its two product chemistry products are acetaldehyde and 4 fluoro L threonine . This enzyme belongs to the family of transferase s, specifically those transferring aldehyde or ketone ketonic groups transaldolases and transketolases, respectively . The systematic name of this enzyme class is fluoroacetaldehyde L threonine aldehydetransferase . References reflist 1 cite journal author Murphy CD, O Hagan D, Schaffrath C date 2001 title Identification of a PLP Dependent Threonine Transaldolase A Novel Enzyme Involved in 4 Fluorothreonine Biosynthesis in Streptomyces cattleya This work was supported by the Biotechnological and Biological Sciences Research Council and the University of St Andrews journal Angew. Chem. Int. Ed. Engl. volume 40 pages 4479&ndash 4481 pmid 12404452 doi 10.1002 1521 3773 20011203 40 23 4479 AID ANIE4479 3.0.CO 2 1 issue 23 cite journal author Murphy CD, Schaffrath C, O Hagan D date 2003 title Fluorinated natural products the biosynthesis of fluoroacetate and 4 fluorothreonine in Streptomyces cattleya journal Chemosphere. volume 52 pages 455&ndash 61 pmid 12738270 doi 10.1016 S0045 6535 03 00191 7 issue 2 transferase stub Category EC 2.2.1 Category Enzymes of unknown structure it Fluorotreonina transaldolasi ... more details
TDH can refer to Total dynamic head L threonine dehydrogenase The Dear Hunter , an American rock band. Turkey s Change Movement lang tr T rkiye De i im Hareketi , a Turkish political party. disambig Long comment to avoid being listed on short pages it TDH ... more details
DISPLAYTITLE C sub 4 sub H sub 9 sub NO sub 3 sub The molecular formula C sub 4 sub H sub 9 sub NO sub 3 sub may refer to Butyl nitrate Threonine MolFormDisambig fr C4H9NO3 sr C4H9NO3 ... more details
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