Image pkb.jpg thumb right 250px Typical Pyruvate Kinase Structure, small X ray Crystallography Derived small Pyruvate kinase List of EC numbers EC 2 EC 2.7.1 Phosphotransferases with an Alcohol Group as Acceptor EC 2.7.1 .40 is an enzyme involved in glycolysis . It catalyst catalyzes the transfer of a phosphate ... of pyruvate and one molecule of adenosine triphosphate ATP . Reaction The pyruvate kinase reaction Image ... dehydrogenase to reduce pyruvate to lactate. In humans, there are two pyruvate kinase isozymes type ... kinase activity is regulated by Its own Substrate biochemistry substrate PEP and fructose 1,6 bisphosphate ... Citation&list uids 22182754 doi 10.1016 j.abb.2011.11.020 ref Liver pyruvate kinase is also regulated indirectly by epinephrine and glucagon , through protein kinase A . This protein kinase phosphorylates liver pyruvate kinase to deactivate it. Muscle pyruvate kinase is not inhibited by epinephrine activation of protein kinase A. Glucagon signals fasting no glucose available . Thus, glycolysis is inhibited ... of pyruvate kinase. These controls prevent pyruvate kinase from being active at the same ... of this enzyme cause the disease known as pyruvate kinase deficiency . In this condition, a lack of pyruvate kinase slows down the process of glycolysis. This effect is especially devastating in cells ... cells , which in a state of pyruvate kinase deficiency rapidly become deficient in ATP and can undergo hemolysis . Therefore, pyruvate kinase deficiency can cause hemolytic anemia . Role in gluconeogenesis Pyruvate kinase also serves as a regulatory enzyme for gluconeogenesis , a biochemical pathway in which the liver generates glucose from pyruvate and other substrates. When pyruvate kinase ... or more occasions. In some cases, the same organism will have both Pyruvate kinase and PPDK. ref ... ref See also PKLR PKM2 Tumor M2 PK References references External links MeshName Pyruvate kinase ... kinase it Piruvato chinasi nl Pyruvaatkinase pl Kinaza pirogronianowa fi Pyruvaattikinaasi sv Pyruvatkinas ... more details
Pantothenate kinase PanK CoaA is the first enzyme in the Coenzyme A biosynthetic pathway. It phophorylates pantothenate Vitamin B5 vitamin B sub 5 sub to form 4 phosphopantothenate. Types Three distinct types of PanK has been identified PanK I found in bacteria , PanK II mainly found in eukaryotes, but also in the Staphylococci and PanK III, also known as CoaX found in bacteria . Eukaryotic PanK II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. Genes Gene PANK1 , Gene PANK2 , Gene PANK3 , Gene PANK4 . PANK2 is associated with Pantothenate kinase associated neurodegeneration , formerly called Hallervorden Spatz syndrome. it also leads to brain fever and finally leads to death External links MeshName Pantothenate kinase EC number 2.7.1.33 enzyme stub Kinases Metabolism of vitamins, coenzymes, and cofactors Category EC 2.7.1 de Pantothenatkinase fr Pantoth nate kinase ja ... more details
Polynucleotide kinase or PNK is a T7 phage T7 bacteriophage or bacteriophage T4 T4 bacteriophage enzyme that catalyzes the transfer of a gamma phosphate from Adenosine triphosphate ATP to the free hydroxyl end of the 5 DNA or RNA . The resulting product could be used to end label DNA or RNA, or in a ligation reaction. External links http www.vivo.colostate.edu hbooks genetics biotech enzymes pnk.html Vivo http www.neb.com nebecomm products productM0236.asp New England Biolabs T4 PNK page Other Languages DEFAULTSORT Polynucleotide Kinase Category Enzymes Cell biology stub fr Polynucl otide kinase ... more details
enzyme Name alkylglycerone kinase EC number 2.7.1.84 CAS number 52227 80 2 IUBMB EC number 2 7 1 84 GO code 0047650 image width caption In enzymology , an alkylglycerone kinase EC number 2.7.1.84 is an enzyme that catalysis catalyzes the chemical reaction ATP O alkylglycerone math rightleftharpoons math ADP O alkylglycerone phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and O alkylglycerone , whereas its two product chemistry products are adenosine diphosphate ADP and O alkylglycerone 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 O alkylglycerone phosphotransferase . Other names in common use include alkyldihydroxyacetone kinase phosphorylating , and alkyldihydroxyacetone kinase . References reflist 1 cite journal author Chae K, Piantadosi C, Snyder F date 1973 title Reductase, phosphatase, and kinase activities in the metabolism of alkyldihydroxyacetone phosphate and alkyldihydroxyacetone journal J. Biol. Chem. volume 248 pages 6718&ndash 23 pmid 4147653 issue 19 enzyme stub Category EC 2.7.1 Category Enzymes of unknown structure ... more details
enzyme Name ceramide kinase EC number 2.7.1.138 CAS number 123175 68 8 IUBMB EC number 2 7 1 138 GO code 0001729 image width caption In enzymology , a ceramide kinase EC number 2.7.1.138 is an enzyme that catalysis catalyzes the chemical reaction ATP ceramide math rightleftharpoons math ADP ceramide 1 phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and ceramide , whereas its two product chemistry products are adenosine diphosphate ADP and ceramide 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 ceramide 1 phosphotransferase . This enzyme is also called acylsphingosine kinase . This enzyme participates in sphingolipid metabolism . References reflist 1 cite journal author Bajjalieh SM, Martin TF, Floor E date 1989 title Synaptic vesicle ceramide kinase. A calcium stimulated lipid kinase that co purifies with brain synaptic vesicles journal J. Biol. Chem. volume 264 pages 14354&ndash 60 pmid 2547795 issue 24 enzyme stub Category EC 2.7.1 Category Enzymes of unknown structure ... more details
enzyme Name glycerone kinase EC number 2.7.1.29 CAS number 9027 47 8 IUBMB EC number 2 7 1 29 GO code 0004371 image width caption In enzymology , a glycerone kinase EC number 2.7.1.29 is an enzyme that catalysis catalyzes the chemical reaction ATP glycerone math rightleftharpoons math ADP glycerone phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and glycerone , whereas its two product chemistry products are adenosine diphosphate ADP and glycerone 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 glycerone phosphotransferase . Other names in common use include dihydroxyacetone kinase , acetol kinase , and acetol kinase phosphorylating . This enzyme participates in glycerolipid 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 1OI2 , PDB link 1OI3 , PDB link 1UN8 , PDB link 1UN9 , PDB link 1UOD , and PDB link 1UOE . References reflist 1 cite journal author Sellinger OZ and Miller ON date 1957 title Phosphorylation of acetol by homogenates of rat liver journal Fed. Proc. volume 16 pages 245&ndash 246 enzyme stub Category EC 2.7.1 Category Enzymes of known structure ... more details
enzyme Name inosine kinase EC number 2.7.1.73 CAS number 37237 46 0 IUBMB EC number 2 7 1 73 GO code 0008906 image width caption In enzymology , an inosine kinase EC number 2.7.1.73 is an enzyme that catalysis catalyzes the chemical reaction ATP inosine math rightleftharpoons math ADP IMP Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and inosine , whereas its two product chemistry products are adenosine diphosphate ADP and Inosine monophosphate IMP . 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 inosine 5 phosphotransferase . Other names in common use include inosine guanosine kinase , and inosine kinase phosphorylating . This enzyme participates in purine metabolism . References reflist 1 cite journal author Pierre KJ, LePage GA date 1968 title Formation of inosine 5 monophosphate by a kinase in cell free extracts of Ehrlich ascites cells in vitro journal Proc. Soc. Exp. Biol. Med. volume 127 pages 432&ndash 40 pmid 5645030 issue 2 enzyme stub Category EC 2.7.1 Category Enzymes of unknown structure ... more details
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
A number of ships have been named Aurora , including SS Aurora 1846 SS Aurora 1889 , an Italian tanker sunk in 1941. SS Aurora 1919 ship SY Aurora See also MV Aurora , a number of motor vessels with this name. shipindex ... 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
Aurora Township may refer to Aurora Township, Kane County, Illinois Aurora Township, Cloud County, Kansas Aurora Township, Minnesota Aurora Township, Benson County, North Dakota Aurora, Ohio , formerly Aurora Township, Portage County, Ohio geodis Category Township name disambiguation pages de Aurora Township ... 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
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