enzyme Name thymidylate kinase EC number 2.7.4.9 CAS number 9014 43 1 IUBMB EC number 2 7 4 9 GO code 0004798 image width caption lowercase In enzymology , a dTMP kinase EC number 2.7.4.9 is an enzyme that catalysis catalyzes the chemical reaction ATP dTMP math rightleftharpoons math ADP dTDP Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and dTMP , whereas its two product chemistry products are adenosine diphosphate ADP and Deoxythymidine monophosphate dTDP . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with a phosphate group as acceptor. The systematic name of this enzyme class is ATP dTMP phosphotransferase . Other names in common use include thymidine monophosphate kinase , thymidylate kinase , thymidylate monophosphate kinase , thymidylic acid kinase , thymidylic kinase , deoxythymidine 5 monophosphate kinase , TMPK , and thymidine 5 monophosphate kinase . This enzyme participates in pyrimidine metabolism . Structural studies As of late 2007, 40 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1E2D , PDB link 1E2E , PDB link 1E2F , PDB link 1E2G , PDB link 1E2Q , PDB link 1E98 , PDB link 1E99 , PDB link 1E9A , PDB link 1E9B , PDB link 1E9C , PDB link 1E9D , PDB link 1E9E , PDB link 1E9F , PDB link 1G3U , PDB link 1GSI , PDB link 1GTV , PDB link 1MRN , PDB link 1MRS , PDB link 1N5I , PDB link 1N5J , PDB link 1N5K , PDB link 1N5L , PDB link 1NMX , PDB link 1NMY , PDB link 1NMZ , PDB link 1NN0 , PDB link 1NN1 , PDB link 1NN3 , PDB link 1NN5 , PDB link 1TMK , PDB link 1W2G , PDB link 1W2H , PDB link 2CCG , PDB link 2CCJ , PDB link 2CCK , PDB link 2PBR , PDB link ... 1970 title Purification and properties of thymidine monophosphate kinase from mouse hepatoma journal ..., Carter CE date 1969 title Purification and characterization of Thymidine 5 monophosphate kinase from ... more details
p70S6 kinase or p70S6K is a serine threonine kinase that acts downstream of Phosphatidylinositol 3,4,5 trisphosphate PIP3 and phosphoinositide dependent kinase 1 in the Phosphoinositide 3 kinase PI3 kinase pathway. ref Cite journal journal Nature title PDGF and insulin dependent pp70S6k activation mediated by phosphatidylinositol 3 OH kinase volume 370 issue 6484 year 1994 authors Chung J, Grammer TC, Lemon KP, Kazlauskas A, Blenis J. page 71 75 doi 10.1038 370071a0 PMID 8015612 ref As the name suggests, its target Substrate biochemistry substrate is the Ribosomal protein s6 S6 ribosomal protein . ref Cite journal journal Cell title Rapamycin FKBP specifically blocks growth dependent activation of and signaling by the 70 kd S6 protein kinases. authors Chung J, Kuo CJ, Crabtree GR, Blenis J. volume 69 issue 7 year 1992 page 1227 1236 doi 10.1016 0092 8674 92 90643 Q PMID 1377606 ref Phosphorylation of S6 induces protein synthesis at the ribosome. mTOR P70S6 kinase is in a signaling pathway that includes mTOR the mammalian target of rapamycin . mTOR can be activated in distinct ways, thereby activating p70S6K. For example, branched chain amino acid s such as leucine are sufficient to activate mTOR, resulting in an increase in p70S6K phosphorylation and thereby activating it . mTOR is also in a pathway downstream of the kinase Akt . Akt is typically activated upon stimulation of a cell with a growth factor such as IGF 1 . Akt then activates mTOR by inhibiting the Tsc complex , leading to p70S6K activation. Physical exercise activates protein synthesis via phosphorylation activation of p70S6K in a pathway that is dependent on mTOR. This has been demonstrated by using an inhibitor of mTOR, rapamycin, to block an increase in muscle mass, despite increases in load e.g., exercise . Exercise has been shown to increase levels of IGF 1 in muscle, thus inducing the IGF 1 PI3K Akt ... Reflist Serine threonine specific protein kinases DEFAULTSORT P70s6 Kinase Category Protein ... more details
enzyme Name deoxyguanosine kinase EC number 2.7.1.113 CAS number 39471 28 8 IUBMB EC number 2 7 1 113 GO code 0004138 image width caption In enzymology , a deoxyguanosine kinase EC number 2.7.1.113 is an enzyme that catalysis catalyzes the chemical reaction ATP deoxyguanosine math rightleftharpoons math ADP dGMP Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and deoxyguanosine , whereas its two product chemistry products are adenosine diphosphate ADP and deoxyguanosine monophosphate dGMP . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ATP deoxyguanosine 5 phosphotransferase . Other names in common use include deoxyguanosine kinase phosphorylating , dihydroxypropoxymethyl guanine kinase , 2 deoxyguanosine kinase , and NTP deoxyguanosine 5 phosphotransferase . This enzyme participates in purine metabolism . Structural studies As of late 2007, 4 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2JAQ , PDB link 2JAS , PDB link 2JAT , and PDB link 2OCP . Clinical Mutations in this gene have been linked to inherited mitochondrial DNA depletion syndromes, neonatal liver failure, nystagmus and hypotonia . References reflist 1 cite journal author Barker J, Lewis RA date 1981 title Deoxyguanosine kinase of neonatal mouse skin tissue journal Biochim. Biophys. Acta. volume 658 pages 111&ndash 23 pmid 6260206 issue 1 cite journal author Gower WR Jr, Carr MC, Ives DH date 1979 title Deoxyguanosine kinase. Distinct molecular forms in mitochondria and cytosol journal J. Biol. Chem. volume 254 pages 2180&ndash 3 pmid 218928 issue 7 enzyme stub Category EC 2.7.1 Category Enzymes of known structure ... more details
enzyme Name S methyl 5 thioribose kinase EC number 2.7.1.100 CAS number 68247 56 3 IUBMB EC number 2 7 1 100 GO code 0046522 image width caption In enzymology , a S methyl 5 thioribose kinase EC number 2.7.1.100 is an enzyme that catalysis catalyzes the chemical reaction ATP S methyl 5 thio D ribose math rightleftharpoons math ADP S methyl 5 thio alpha D ribose 1 phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and S methyl 5 thio D ribose , whereas its two product chemistry products are adenosine diphosphate ADP and S methyl 5 thio alpha D ribose 1 phosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ATP S methylmethyl 5 thio D ribose 1 phosphotransferase . Other names in common use include 5 methylthioribose kinase phosphorylating , methylthioribose kinase , 5 methylthioribose kinase , and ATP S5 methyl 5 thio D ribose 1 phosphotransferase . This enzyme participates in methionine metabolism . Structural studies As of late 2007, 6 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2OLC , PDB link 2PU8 , PDB link 2PUI , PDB link 2PUL , PDB link 2PUN , and PDB link 2PUP . References reflist 1 cite journal author Ferro AJ, Barrett A, Shapiro SK date 1978 title 5 Methylthioribose kinase. A new enzyme involved in the formation of methionine from 5 methylthioribose journal J. Biol. Chem. volume 253 pages 6021&ndash 5 pmid 210167 issue 17 cite journal author Guranowski A date 1983 title Plant 5 methylthioribose kinase journal Plant Physiol. volume 71 pages 932&ndash 935 pmid 16662931 doi 10.1104 pp.71.4.932 pmc 1066146 enzyme stub Category EC 2.7.1 Category Enzymes of known structure ... more details
enzyme Name UMP kinase EC number 2.7.4.22 CAS number 9036 23 1 IUBMB EC number 2 7 4 22 GO code 0033862 image width caption In enzymology , an UMP kinase EC number 2.7.4.22 is an enzyme that catalysis catalyzes the chemical reaction ATP UMP math rightleftharpoons math ADP UDP Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and uridine monophosphate UMP , whereas its two product chemistry products are adenosine diphosphate ADP and uridine diphosphate UDP . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with a phosphate group as acceptor. The systematic name of this enzyme class is ATP UMP phosphotransferase . Other names in common use include uridylate kinase , UMPK , uridine monophosphate kinase , PyrH , UMP kinase , and SmbA . This enzyme participates in pyrimidine metabolism . Structural studies As of March 2010, 19 tertiary structure structures have been solved for this class of enzymes, and are deposited in the Protein Data Bank PDB . All have a 3 layer aba sandwich architecture CATH code 3.40.1160.10 . These include accession codes PDB link 2J4J , PDB link 2J4K , PDB link 2J4L , and PDB link 2VA1 . Search for all UMP Kinases in the PDB using the http www.ebi.ac.uk pdbe srv PDBeXplore enzyme enzyme Browser at http www.pdbe.org PDBe . input the EC number References reflist 1 cite journal author Gilles AM, Barzu O date 1995 title Escherichia coli UMP kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP journal Biochemistry. volume 34 pages 5066 5074 pmid 7711027 doi 10.1021 bi00015a018 issue 15 cite journal author Marco Marin C, Gil Ortiz F, Rubio V date 2005 title The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis journal J. Mol. Biol. volume 352 pages 438 454 pmid 16095620 doi 10.1016 j.jmb.2005.07.045 ... more details
enzyme Name uridine kinase EC number 2.7.1.48 CAS number 9026 39 5 IUBMB EC number 2 7 1 48 GO code 0004849 image width caption In enzymology , an uridine kinase EC number 2.7.1.48 is an enzyme that catalysis catalyzes the chemical reaction ATP uridine math rightleftharpoons math ADP UMP Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and uridine , whereas its two product chemistry products are adenosine diphosphate ADP and uridine monophosphate UMP . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ATP uridine 5 phosphotransferase . Other names in common use include pyrimidine ribonucleoside kinase , uridine cytidine kinase , uridine kinase phosphorylating , and uridine phosphokinase . This enzyme participates in pyrimidine metabolism . Structural studies As of late 2007, 8 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1UDW , PDB link 1UEI , PDB link 1UEJ , PDB link 1UFQ , PDB link 1UJ2 , PDB link 1XRJ , PDB link 2JEO , and PDB link 2UVQ . References reflist 1 cite journal author Orengo A date 1969 title Regulation of enzymic activity by metabolites. I. Uridine cytidine kinase of Novikoff ascites rat tumor journal J. Biol. Chem. volume 244 pages 2204&ndash 9 pmid 5782006 issue 8 cite journal author Skold O date 1960 title Uridine kinase from Erlich ascites tumor purification and properties journal J. Biol. Chem. volume 235 pages 3273&ndash 3279 enzyme stub Category EC 2.7.1 Category Enzymes of known structure ... more details
Infobox protein family Symbol Acetate kinase Name Acetate kinase image PDB 1x9j EBI.jpg width caption structure of butyrate kinase 2 reveals both open and citrate induced closed conformations implications for substrate induced fit conformational changes Pfam PF00871 Pfam clan CL0108 InterPro IPR000890 SMART PROSITE PDOC00826 MEROPS SCOP 1g99 TCDB OPM family OPM protein CAZy CDD In molecular biology, acetate kinase EC number 2.7.2.1 , which is predominantly found in micro organisms, facilitates the production of acetyl CoA by Phosphorylation phosphorylating acetate in the presence of ATP and a divalent cation . ref name pmid8226682 cite journal author Grundy FJ, Waters DA, Allen SH, Henkin TM title Regulation of the Bacillus subtilis acetate kinase gene by CcpA journal J. Bacteriol. volume 175 issue 22 pages 7348 55 year 1993 month November pmid 8226682 pmc 206879 doi url ref ref name pmid8396545 cite journal author Oultram JD, Burr ID, Elmore MJ, Minton NP title Cloning and sequence analysis of the genes encoding phosphotransbutyrylase and butyrate kinase from Clostridium acetobutylicum NCIMB 8052 journal Gene volume 131 issue 1 pages 107 12 year 1993 month September pmid 8396545 doi 10.1016 0378 1119 93 90677 U url ref The enzyme is important in the process of glycolysis , enzyme levels being increased in the presence of excess glucose . The cell growth growth of a bacteria bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydrate . ref name pmid8226682 cite journal author Grundy FJ, Waters DA, Allen SH, Henkin TM title Regulation of the Bacillus subtilis acetate kinase gene by CcpA journal J. Bacteriol. volume 175 issue 22 pages 7348 55 year 1993 month November pmid 8226682 pmc 206879 doi url ref A related enzyme, butyrate kinase , facilitates the formation of butyryl ... of the genes encoding phosphotransbutyrylase and butyrate kinase from Clostridium acetobutylicum NCIMB ... more details
enzyme Name shikimate kinase EC number 2.7.1.71 CAS number 9031 51 0 IUBMB EC number 2 7 1 71 GO code 0004765 image width caption Pfam box Symbol SKI Name Shikimate kinase image 1e6c opm.gif width caption Shikimate kinase of Erwinia chrysanthemi Pfam PF01202 Pfam clan CL0023 InterPro IPR000623 SMART PROSITE PDOC00868 SCOP 2shk TCDB OPM family OPM protein 1e6c PDB PDB3 1l4y A 11 167 PDB3 1we2 A 11 167 PDB3 1l4u A 11 167 PDB3 1u8a A 11 167 PDB3 2shk B 11 169 PDB3 1shk A 11 169 PDB3 1e6c B 11 169 PDB3 1kag A 13 171 PDB3 2IYQ PDB3 2IYR PDB3 2IYS PDB3 2IYT PDB3 2IYU PDB3 2IYV PDB3 2IYW PDB3 2IYX PDB3 2IYY PDB3 2IYZ Shikimate kinase EC number 2.7.1.71 is an enzyme that catalyzes the Adenosine triphosphate ATP dependent phosphorylation of shikimate to form shikimate 3 phosphate. This reaction is the fifth step of the shikimate pathway ref Cite pmid 15012217 ref , which is used by plants and bacteria to synthesize the common precursor of aromatic amino acids and secondary metabolites. The systematic ... shikimate kinase phosphorylating , and shikimate kinase II . Background The shikimate pathway ... kinase in the pathway are DAHP synthase , 3 dehydroquinate synthase , 3 dehydroquinate dehydratase ... and herbicides. Activity The reaction catalyzed by shikimate kinase is shown below Image shikimate kinase reaction.png left 600px reaction catalyzed by shikimate kinase This reaction involves the transfer of a phosphate group from ATP to the 3 hydroxyl group of shikimate. Shikimate kinase thus has ... products , shikimate 3 phosphate and Adenosine diphosphate ADP . Structure Image shikimate kinase cartoon.png thumb right A cartoon representation of shikimate kinase from Mycobacterium tuberculosis ... kinase with products.png thumb right A space filling model of shikimate kinase with ADP and shikimate ... title Shikimate kinase isoenzymes in Salmonella typhimurium journal J. Biol. Chem. volume 243 pages ... N, Bartunik HD year 2006 title Mechanism of phosphoryl transfer catalyzed by shikimate kinase ... more details
LIM kinase 1 LIMK1 and LIM kinase 2 LIMK2 are actin binding kinase s that phosphorylate members of the ADF cofilin family of actin binding and filament severing protein s. ADF cofilin are the only Substrate biochemistry substrate s yet identified for the LIM kinases. Upstream, LIMK1 is regulated by Pak1, ref Edwards, D.C., Sanders, L.C., Bokoch, G.M. & Gill, G.N. 1999 Nature Cell Biol. 1, 253 259. ref and LIMK2 by the Rho dependent kinase ROCK. ref Sumi, T., Matsumoto, K. & Nakamura, T. 2001 . Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, ref Lim Kinases are activated by PAK p21 activated kinase . There are approximately 40 known eukaryotic LIM protein s, so named for the LIM domains they contain. LIM domains are highly conserved cysteine rich structures containing 2 zinc fingers. Although zinc fingers usually function by binding to DNA or RNA , the LIM Structural motif motif probably mediates protein protein interactions. LIM kinase 1 and LIM kinase 2 belong to a small subfamily with a unique combination of 2 N terminal LIM motifs and a C terminal protein kinase domain. LIMK1 is likely to be a component of an intracellular signaling pathway and may be involved in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome . ref http www.ncbi.nlm.nih.gov entrez query.fcgi?db gene&cmd Retrieve&dopt Graphics&list uids 3984 NIH ref References reflist External links MeshName Lim Kinases Category EC 2.7.1 ... more details
enzyme Name acylglycerol kinase EC number 2.7.1.94 CAS number 62213 37 0 IUBMB EC number 2 7 1 94 GO code 0047620 image width caption In enzymology , an acylglycerol kinase EC number 2.7.1.94 is an enzyme that catalysis catalyzes the chemical reaction ATP acylglycerol math rightleftharpoons math ADP acyl sn glycerol 3 phosphate The two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and acylglycerol , whereas its two product chemistry products are adenosine diphosphate ADP and acyl sn glycerol 3 phosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ATP acylglycerol 3 phosphotransferase . Other names in common use include monoacylglycerol kinase , monoacylglycerol kinase phosphorylating , sn 2 monoacylglycerol kinase , MGK , monoglyceride kinase , and monoglyceride phosphokinase . This enzyme participates in glycerolipid metabolism . References reflist 1 cite journal author Pieringer R.A., Hokin L.E. date 1962 title Biosynthesis of lysophosphatdic acid from monoglyceride and adenosine triphosphate journal J. Biol. Chem. volume 237 pages 653&ndash 8 pmid 14486486 cite journal author Pieringer RA and Kunnes RS date 1965 title The biosynthesis of phosphatidic acid and lysophosphatidic acid by glyceride phosphokinase pathways in Escherichia coli journal J. Biol. Chem. volume 240 pages 2833&ndash 2838 pmid 14342303 url http www.jbc.org content 240 7 2833.full.pdf format PDF issue 7 enzyme stub Category EC 2.7.1 Category Enzymes of unknown structure ... more details
enzyme Name tropomyosin kinase EC number 2.7.11.28 CAS number 90804 56 1 IUBMB EC number 2 7 11 28 GO code 0050359 image width caption In enzymology , a tropomyosin kinase EC number 2.7.11.28 is an enzyme that catalysis catalyzes the chemical reaction ATP tropomyosin math rightleftharpoons math ADP O phosphotropomyosin Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and tropomyosin , whereas its two product chemistry products are adenosine diphosphate ADP and O phosphotropomyosin . This enzyme belongs to the family of transferase s, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in protein s protein serine threonine kinase s . The systematic name of this enzyme class is ATP tropomyosin O phosphotransferase . Other names in common use include tropomyosin kinase phosphorylating , and STK . References reflist 1 cite journal author deBelle I, Mak AS date 1987 title Isolation and characterization of tropomyosin kinase from chicken embryo journal Biochim. Biophys. Acta. volume 925 pages 17&ndash 26 pmid 3593768 issue 1 cite journal author Montgomery K, Mak AS date 1984 title In vitro phosphorylation of tropomyosin by a kinase from chicken embryo journal J. Biol. Chem. volume 259 pages 5555&ndash 60 pmid 6325440 issue 9 cite journal author Watson MH, Taneja AK, Hodges RS, Mak AS date 1988 title Phosphorylation of alpha alpha and beta beta tropomyosin and synthetic peptide analogues journal Biochemistry. volume 27 pages 4506&ndash 12 pmid 3166994 doi 10.1021 bi00412a043 issue 12 enzyme stub Category EC 2.7.11 Category Enzymes of unknown structure ... more details
enzyme Name hydroxymethylpyrimidine kinase EC number 2.7.1.49 CAS number 9026 55 5 IUBMB EC number 2 7 1 49 GO code 0008902 image width caption In enzymology , a hydroxymethylpyrimidine kinase EC number 2.7.1.49 is an enzyme that catalysis catalyzes the chemical reaction ATP 4 amino 5 hydroxymethyl 2 methylpyrimidine math rightleftharpoons math ADP 4 amino 5 phosphonooxymethyl 2 methylpyrimidine Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and 4 amino 5 hydroxymethyl 2 methylpyrimidine , whereas its two product chemistry products are adenosine diphosphate ADP and 4 amino 5 phosphonooxymethyl 2 methylpyrimidine . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ATP 4 amino 5 hydroxymethyl 2 methylpyrimidine 5 phosphotransferase . This enzyme is also called hydroxymethylpyrimidine kinase phosphorylating . This enzyme participates in thiamine metabolism . References reflist 1 cite journal author Lewin LM and Brown GM date 1961 title The biosynthesis of thiamine. III. Mechanism of enzymatic formation of the pyrophosphate ester of 2 methyl 4 amino 5 hydroxymethylpyrimidine journal J. Biol. Chem. volume 236 pages 2768&ndash 2771 enzyme stub Category EC 2.7.1 Category Enzymes of unknown structure ... more details
Image MAPKpathway.jpg right thumb 300px The mitogen activated protein kinase MAPK pathway. ref name pmid10558990 cite journal author Rossomando AJ, Payne DM, Weber MJ, Sturgill TW title Evidence that pp42, a major tyrosine kinase target protein, is a mitogen activated serine threonine protein kinase journal Proc Natl Acad Sci USA volume 86 issue 18 pages 6940 3 year 1989 pmid 2550926 doi 10.1073 pnas.86.18.6940 issn pmc 297966 ref ref name pmid2550926 cite journal author Bonni A, Brunet A, West AE, Datta SR, Takasu MA, Greenberg ME title Cell survival promoted by the Ras MAPK signaling pathway by transcription dependent and independent mechanisms journal Science volume 286 issue 5443 pages 1358 62 year 1999 pmid 10558990 doi 10.1126 science.286.5443.1358 issn ref ref name pmid11784851 cite journal author Chadee DN, Yuasa T, Kyriakis JM title Direct activation of mitogen activated protein kinasekinasekinase MEKK1 by the Ste20p homologue GCK and the adapter protein TRAF2 journal Mol. Cell. Biol. volume 22 issue 3 pages 737 49 year 2002 pmid 11784851 doi 10.1128 MCB.22.3.737 749.2002 issn pmc 133545 ref ref name pmid11242034 cite journal author Chang L, Karin M title Mammalian MAP kinase ... N terminal kinase pathway and apoptotic signaling review journal Int. J. Oncol. volume 16 issue 4 pages ... A, Zanke BW, Lassam N, Pawson T, Woodgett JR, Iscove NN title HPK1, a hematopoietic protein kinase .... MAP kinase signaling specificity journal Science volume 296 issue 5577 pages 2345 7 year ... of the diagram. Raf kinases are a family of three serine threonine specific protein kinase s that are related ... a Raf kinase related oncogene that enhances fibrosarcoma induction. The acronym RAF is derived from ... Raf kinases participate in the Ras subfamily RAS RAF mitogen activated protein kinasekinase MEK extracellular ... pathway mitogen activated protein kinase MAPK cascade . ref name pmid20674547 Activation of RAF kinases requires interaction with Ras subfamily RAS GTPases . The three RAF kinase family members are ARAF ... more details
enzyme Name glucosamine kinase EC number 2.7.1.8 CAS number 9031 90 7 IUBMB EC number 2 7 1 8 GO code 0047931 image width caption In enzymology , a glucosamine kinase EC number 2.7.1.8 is an enzyme that catalysis catalyzes the chemical reaction ATP D glucosamine math rightleftharpoons math ADP D glucosamine phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and D glucosamine , whereas its two product chemistry products are adenosine diphosphate ADP and D glucosamine phosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ATP D glucosamine phosphotransferase . Other names in common use include glucosamine kinase phosphorylating , ATP 2 amino 2 deoxy D glucose 6 phosphotransferase , and aminodeoxyglucose kinase . This enzyme participates in amino sugar aminosugars metabolism . References reflist 1 cite journal author BUEDING E, MACKINNON JA date 1955 title Hexokinases of Schistosoma mansoni journal J. Biol. Chem. volume 215 pages 495&ndash 506 pmid 13242546 issue 2 Category EC 2.7.1 Category Enzymes of unknown structure enzyme stub ... more details
enzyme Name hydroxylysine kinase EC number 2.7.1.81 CAS number 9073 58 9 IUBMB EC number 2 7 1 81 GO code 0047992 image width caption In enzymology , a hydroxylysine kinase EC number 2.7.1.81 is an enzyme that catalysis catalyzes the chemical reaction GTP 5 hydroxy L lysine math rightleftharpoons math GDP 5 phosphonooxy L lysine Thus, the two substrate biochemistry substrates of this enzyme are guanosine triphosphate GTP and 5 hydroxy L lysine , whereas its two product chemistry products are guanosine diphosphate GDP and 5 phosphonooxy L lysine . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is GTP 5 hydroxy L lysine O phosphotransferase . Other names in common use include hydroxylysine kinase phosphorylating , and guanosine triphosphate 5 hydroxy L lysine O phosphotransferase . This enzyme participates in lysine degradation . References reflist 1 cite journal author Hiles RA, Henderson LM date 1972 title The partial purification and properties of hydroxylysine kinase from rat liver journal J. Biol. Chem. volume 247 pages 646&ndash 51 pmid 4621658 issue 3 enzyme stub Category EC 2.7.1 Category Enzymes of unknown structure ... more details
enzyme Name pseudouridine kinase EC number 2.7.1.83 CAS number 62213 40 5 IUBMB EC number 2 7 1 83 GO code 0050225 image width caption In enzymology , a pseudouridine kinase EC number 2.7.1.83 is an enzyme that catalysis catalyzes the chemical reaction ATP pseudouridine math rightleftharpoons math ADP pseudouridine 5 phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and pseudouridine , whereas its two product chemistry products are adenosine diphosphate ADP and pseudouridine 5 phosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ATP pseudouridine 5 phosphotransferase . This enzyme is also called pseudouridine kinase phosphorylating . This enzyme participates in pyrimidine metabolism . References reflist 1 cite journal author Solomon LR, Breitman TR date 1971 title Pseudouridine kinase of escherichia coli a new enzyme journal Biochem. Biophys. Res. Commun. volume 44 pages 299&ndash 304 pmid 4334133 issue 2 doi 10.1016 0006 291X 71 90599 7 enzyme stub Category EC 2.7.1 Category Enzymes of unknown structure ... more details
enzyme Name thiamin kinase EC number 2.7.1.89 CAS number 62213 38 1 IUBMB EC number 2 7 1 89 GO code 0019165 image width caption In enzymology , a thiamine kinase EC number 2.7.1.89 is an enzyme that catalysis catalyzes the chemical reaction ATP thiamine math rightleftharpoons math ADP thiamine phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and thiamine , whereas its two product chemistry products are adenosine diphosphate ADP and thiamine phosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ATP thiamine phosphotransferase . Other names in common use include thiamin kinase phosphorylating , thiamin phosphokinase , ATP thiamin phosphotransferase , and thiamin kinase . This enzyme participates in thiamine metabolism . References reflist 1 cite journal author Iwashima A, Nishino H, Nose Y date 1972 title Conversion of thiamine to thiamine monophosphate by cell free extracts of Escherichia coli journal Biochim. Biophys. Acta. volume 258 pages 333&ndash 6 pmid 4550803 issue 1 enzyme stub Category EC 2.7.1 Category Enzymes of unknown structure ... more details
enzyme Name IkappaB kinase EC number 2.7.11.10 CAS number 159606 08 3 IUBMB EC number 2 7 11 10 GO code 0008384 image width caption The I B kinase IKK is an enzyme complex that is involved in propagating the cellular response to inflammation . ref name pmid17047224 Cite journal author H cker H, Karin M title Regulation and function of IKK and IKK related kinases journal Sci. STKE volume 2006 issue 357 pages re13 year 2006 month October pmid 17047224 doi 10.1126 stke.3572006re13 url issn ref The I B kinase enzyme complex is part of the upstream NF B signal transduction cascade. The I B inhibitor of kappa B protein inactivates the NF B transcription factor by masking the nuclear localization signal s NLS of NF B proteins and keeping them sequestered in an inactive state in the cytoplasm. ref name pmid9865693 Cite journal author Jacobs MD, Harrison SC title Structure of an IkappaBalpha NF kappaB complex journal Cell volume 95 issue 6 pages 749 58 year 1998 pmid 9865693 doi 10.1016 S0092 ..., Cao Z, Rothe M title Identification and characterization of an IkappaB kinase journal Cell volume ... of the IkappaB kinase IKK complex journal Oncogene volume 18 issue 49 pages 6867 74 year 1999 ... 150 genes some of which are anti apoptotic. Catalyzed reaction In enzymology , an IkappaB kinase ... atom of serine or threonine residues in protein s protein serine threonine kinase s . The systematic name of this enzyme class is ATP IkappaB protein phosphotransferase. Structure The I B kinase ... top protein Name CHUK conserved helix loop helix ubiquitous kinase caption image width HGNCid 1974 ... inhibitor of kappa light polypeptide gene enhancer in B cells, kinase beta caption image width HGNCid ... inhibitor of kappa light polypeptide gene enhancer in B cells, kinase gamma caption image width ... title The IkappaB kinase complex IKK contains two kinase subunits, IKKalpha and IKKbeta, necessary ... j.tibs.2004.11.009 issue 1 refend External links MeshName I kappa B Kinase DEFAULTSORT I b Kinase ... more details
enzyme Name guanylate kinase EC number 2.7.4.8 CAS number 9026 59 9 IUBMB EC number 2 7 4 8 GO code 0004385 image width caption Infobox protein family Symbol Guanylate kin Name guanylate kinase image PDB 1gky EBI.jpg width caption Structure of Guanylate Kinase. ref name pmid1314905 cite journal author Stehle T, Schulz GE title Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution journal J. Mol. Biol. volume 224 issue 4 pages 1127 41 year 1992 month April pmid 1314905 doi 10.1016 0022 2836 92 90474 X url ref Pfam PF00625 InterPro IPR008144 SMART PROSITE PDOC00670 SCOP 1gky TCDB OPM family OPM protein PDB PDB2 1ex6 , PDB2 1ex7 , PDB2 1gky , PDB2 1jxm , PDB2 1jxo , PDB2 1kgd , PDB2 1kjw , PDB2 1lvg , PDB2 1s4q , PDB2 1s96 , PDB2 1xzp , PDB2 1xzq , PDB2 1z6g , PDB2 1z8f , PDB2 1znw , PDB2 1znx , PDB2 1zny , PDB2 1znz , PDB2 2an9 , PDB2 2anb , PDB2 2anc , PDB2 2f3r , PDB2 2f3t , PDB2 2qor In enzymology , a guanylate kinase EC number 2.7.4.8 is an enzyme that catalysis catalyzes the chemical reaction Adenosine triphosphate ATP Guanosine monophosphate GMP math rightleftharpoons math Adenosine diphosphate ADP guanosine diphosphate GDP Thus, the two ... participates in purine metabolism . Guanylate kinase catalyzes the ATP dependent phosphorylation ... of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution journal J. Mol ... kinase and to the product of a Drosophila tumor suppressor gene journal Cell volume 68 issue ... determination of guanylate kinase from pig brain journal Eur. J. Biochem. volume 213 issue 1 pages ... kinase? journal Trends Biochem. Sci. volume 17 issue 3 pages 99 year 1992 month March pmid 1329277 ... d GMP phosphotransferase . Other names in common use include deoxyguanylate kinase, 5 GMP kinase, GMP kinase, guanosine monophosphate kinase, and ATP GMP phosphotransferase. References reflist Further ... and properties of guanylate kinase from Escherichia coli journal J. Biol. Chem. volume 241 pages 5452 ... more details
enzyme Name cytidylate kinase EC number 2.7.4.14 CAS number 37278 21 0 IUBMB EC number 2 7 4 14 GO code 0004127 image width caption In enzymology , a cytidylate kinase EC number 2.7.4.14 is an enzyme that catalysis catalyzes the chemical reaction ATP d CMP math rightleftharpoons math ADP d CDP Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and Deoxycytidine monophosphate dCMP , whereas its two product chemistry products are adenosine diphosphate ADP and dCDP . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with a phosphate group as acceptor. The systematic name of this enzyme class is ATP CMP phosphotransferase . Other names in common use include deoxycytidylate kinase , deoxycytidylate kinase , CMP kinase , CTP CMP phosphotransferase , dCMP kinase , deoxycytidine monophosphokinase , UMP CMP kinase , ATP UMP CMP phosphotransferase , and pyrimidine nucleoside monophosphate kinase . This enzyme participates in pyrimidine metabolism . 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 1CKE , PDB link 1KDO , PDB link 1KDP , PDB link 1KDR , PDB link 1KDT , PDB link 1Q3T , PDB link 1QF9 , PDB link 1TEV , PDB link 1UKE , PDB link 2CMK , PDB link 2FEM , PDB link 2FEO , PDB link 2H92 , PDB link 2UKD , PDB link 3UKD , PDB link 4UKD , and PDB link 5UKD . References reflist 1 cite journal author Hurwitz J date 1959 title The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material journal J. Biol. Chem. volume 234 pages 2351&ndash 2358 Boyer, P.D., Lardy, H. and Myrback, K. Eds. , The Enzymes, 2nd ed., vol. 6, Academic Press, New York, 1962, p. 139 149. cite journal author Ruffner BW Jr, Anderson EP date 1969 title Adenosine triphosphate uridine monophosphate cytidine monophosphate phosphotransferase from Tetrahymena ... more details
enzyme Name hydroxyethylthiazole kinase EC number 2.7.1.50 CAS number 9026 56 6 IUBMB EC number 2 7 1 50 GO code 0004417 image width caption Infobox protein family Symbol HK Name Hydroxyethylthiazole kinase family image PDB 1c3q EBI.jpg width caption crystal structure of native thiazole kinase in the monoclinic form Pfam PF02110 Pfam clan CL0118 InterPro IPR000417 SMART PROSITE MEROPS SCOP 1c3q TCDB OPM family OPM protein CAZy CDD In enzymology , a hydroxyethylthiazole kinase EC number 2.7.1.50 is an enzyme that catalysis catalyzes the chemical reaction ATP 4 methyl 5 2 hydroxyethyl thiazole math rightleftharpoons math ADP 4 methyl 5 2 phosphonooxyethyl thiazole Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and 4 methyl 5 2 hydroxyethyl thiazole , whereas its two product chemistry products are adenosine diphosphate ADP and 4 methyl 5 2 phosphonooxyethyl thiazole . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ATP 4 methyl 5 2 hydroxyethyl thiazole 2 phosphotransferase . Other names in common use include hydroxyethylthiazole kinase phosphorylating , and 4 methyl 5 beta hydroxyethyl thiazole kinase . This enzyme participates in thiamine metabolism . Thiamine pyrophosphate TPP , a required Cofactor biochemistry cofactor for many enzyme s in the cell, is synthesised de novo in Salmonella typhimurium . ref name pmid9244280 cite journal author Petersen LA, Downs DM title Identification and characterization of an operon in Salmonella typhimurium involved in thiamine biosynthesis journal J. Bacteriol. volume 179 issue 15 pages 4894 900 year 1997 month August pmid 9244280 pmc 179339 doi url ref In Saccharomyces cerevisiae , hydroxyethylthiazole kinase gene expression ... kinase from Saccharomyces cerevisiae journal J. Biol. Chem. volume 269 issue 48 pages ... more details
unreferenced date February 2011 mergeto triokinase date February 2011 Triose kinase is an enzyme in the liver that takes part in an alternate glycolysis glycolytic pathway. It phosphorylation phosphorylates a three carbon sugar or triose to allow it to continue along the standard glycolytic pathway. The preceding step, also differing from normal glycolysis, involves the conversion of fructose 1 phosphate to dihydroxyacetone phosphate and glyceraldehyde , essentially splitting a six carbon sugar into two three carbon sugars. The normal glycolytic reaction involves an additional phosphate on the glyceraldehyde i.e., glyceraldehyde 3 phosphate , from fructose 1,6 bisphosphate . Thus, the liver pathway must phosphorylate the triose. Triose kinase catalyzes this step using Adenosine triphosphate ATP . The following step in the pathway is the standard glycolytic step, catalyzed by triose phosphate isomerase . Category EC 2.7.1 Category Enzymes of known structure enzyme stub ... more details
Aurora kinases are serine threonine kinases that are essential for cell growth cell proliferation . The enzyme helps the dividing cell dispense its gene genetic materials to its daughter cells. More specifically, Aurora kinases play a crucial role in cellular division by controlling chromatid segregation. Defects in this segregation can cause genetic instability, a condition which is highly associated with tumorigenesis. ref Bolanos garcia V M. Aurora kinases. The International Journal of Biochemistry & Cell Biology 37 2005 1572 1577. ref Three Aurora kinases have been identified in mammalian cells to date. Besides being implicated as mitotic regulators, these three kinases have generated significant interest in the cancer research field due to their elevated expression profiles in many human cancers. ref Giet R, Prigent C. Aurora Ipl1p related kinases, a new oncogenic family of mitotic serine threonine kinases. Journal of Cell Science 112 1999 3591 3601. ref The human Aurora kinases present a similar domain organization, with a N terminal domain of 39 to 129 residues in length, a protein kinase domain and a short C terminal domain containing 15 to 20 residues. The N terminal domain of three proteins share low sequence conservation, which determines selectivity during protein protein interactions Bolanos Garcia, 2005 . Classes As, mentioned above, there are three classes of aurora kinases Aurora A kinase Aurora A aka Aurora 2 functions during prophase of mitosis and is required for correct function of the centrosome s the microtubule organising centres in eukaryotic cells . Aurora B kinase Aurora B aka Aurora 1 functions in the attachment of the mitotic spindle to the centromere. Aurora C kinase Aurora C Gene AURKC works in germ line cells and little is known about its function. See also Aurora inhibitor References reflist External links MeshName aurora kinase enzyme stub Serine threonine specific protein kinases de Aurorakinase ... more details
enzyme Name deoxyadenosine kinase EC number 2.7.1.76 CAS number 37278 12 9 IUBMB EC number 2 7 1 76 GO code 0004136 image width caption In enzymology , a deoxyadenosine kinase EC number 2.7.1.76 is an enzyme that catalysis catalyzes the chemical reaction ATP deoxyadenosine math rightleftharpoons math ADP dAMP Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and deoxyadenosine , whereas its two product chemistry products are adenosine diphosphate ADP and Deoxyadenosine monophosphate dAMP . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ATP deoxyadenosine 5 phosphotransferase . This enzyme is also called purine deoxyribonucleoside kinase . This enzyme participates in purine metabolism . 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 2JAQ . References reflist 1 cite journal author Chang CH, Brockman RW, Bennett LL Jr date 1982 title Purification and some properties of a deoxyribonucleoside kinase from L1210 cells journal Cancer. Res. volume 42 pages 3033&ndash 9 pmid 6284353 issue 8 cite journal author Krygier V, Momparler RL date 1968 title The regulatory properties of deoxyadenosine kinase journal Biochim. Biophys. Acta. volume 161 pages 578&ndash 80 pmid 5667299 issue 2 enzyme stub Category EC 2.7.1 Category Enzymes of known structure ... more details
enzyme Name erythritol kinase EC number 2.7.1.27 CAS number 9030 64 2 IUBMB EC number 2 7 1 27 GO code 0047878 image width caption In enzymology , an erythritol kinase EC number 2.7.1.27 is an enzyme that catalysis catalyzes the chemical reaction ATP erythritol math rightleftharpoons math ADP D erythritol 4 phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and erythritol , whereas its two product chemistry products are adenosine diphosphate ADP and D erythritol 4 phosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ATP erythritol 4 phosphotransferase . This enzyme is also called erythritol kinase phosphorylating . 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 1V5S . References reflist 1 cite journal author HOLTEN D, FROMM HJ date 1961 title Purification and properties of erythritol kinase from Propionibacterium pentosaceum journal J. Biol. Chem. volume 236 pages 2581&ndash 4 pmid 13908588 cite journal author HOLTEN D, FROMM HJ date 1961 title Purification and properties of erythritol kinase from Propionibacterium pentosaceum journal J. Biol. Chem. volume 236 pages 2581&ndash 4 pmid 13908588 enzyme stub Category EC 2.7.1 Category Enzymes of known structure ... more details
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