protein Name G protein coupled receptor kinase 1 caption image width HGNCid 10013 Symbol GRK1 AltSymbols RHOK EntrezGene 6011 OMIM 180381 RefSeq NM 002929 UniProt Q15835 PDB ECnumber 2.7.11.14 Chromosome 13 Arm q Band 34 LocusSupplementaryData Rhodopsin kinase is a serine threonine specific protein kinase involved in phototransduction . See also Rhodopsin Beta adrenergic receptor kinase G protein coupled receptor kinases External links MeshName Rhodopsin kinase biochemistry stub Serine threonine specific protein kinases Eye proteins ... more details
enzyme Name NADH kinase EC number 2.7.1.86 CAS number 62213 39 2 IUBMB EC number 2 7 1 86 GO code 0042736 image width caption In enzymology , a NADH kinase EC number 2.7.1.86 is an enzyme that catalysis catalyzes the chemical reaction ATP NADH math rightleftharpoons math ADP NADPH Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and nicotinamide adenine dinucleotide NADH , whereas its two product chemistry products are adenosine diphosphate ADP and nicotinamide adenine dinucleotide phosphate NADPH . 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 NADH 2 phosphotransferase . Other names in common use include reduced nicotinamide adenine dinucleotide kinase phosphorylating , DPNH kinase , reduced diphosphopyridine nucleotide kinase , and NADH kinase . This enzyme has at least one effector biology effector , Acetate . References reflist 1 cite journal author Griffiths MM, Bernofsky C date 1972 title Purification and properties of reduced diphosphopyridine nucleotide kinase from yeast mitochondria journal J. Biol. Chem. volume 247 pages 1473&ndash 8 pmid 4335000 issue 5 enzyme stub Category EC 2.7.1 Category NADPH dependent enzymes Category Enzymes of unknown structure ... more details
Pfam box Symbol Thymidylate kin Name Thymidylate kinase Pfam PF02223 InterPro IPR000062 PROSITE PDOC01034 PDB PDB 1e2d PDB 1e2e PDB 1e2f PDB 1e2g PDB 1e2q PDB 1e98 PDB 1e99 PDB 1e9a PDB 1e9b PDB 1e9c Thymidylate kinase EC number 2.7.4.9 dTMP kinase catalyzes the phosphorylation of Thymidine monophosphate thymidine 5 monophosphate dTMP to form thymidine 5 diphosphate dTDP in the presence of ATP and magnesium ATP thymidine 5 phosphate math rightleftharpoons math ADP thymidine 5 diphosphate Thymidylate kinase is a ubiquitous enzyme of about 25 Kd and is important in the dTTP synthesis pathway for DNA synthesis. The function of dTMP kinase in eukaryotes comes from the study of a cell cycle mutant, cdc8, in Saccharomyces cerevisiae Saccharomyces cerevisiae . Structural and functional analyses suggest that the cDNA codes for authentic human dTMP kinase. The mRNA levels and enzyme activities corresponded to cell cycle progression and cell growth stages. ref name PUB00016913 cite journal author Li C, Huang SH, Tang A, Drisco B, Zhang SQ, Seeger R, Jong A title Human dTMP kinase gene expression and enzymatic activity coinciding with cell cycle progression and cell growth journal DNA Cell Biol. volume 13 issue 5 pages 461 471 year 1994 pmid 8024690 doi 10.1089 dna.1994.13.461 ref Subfamilies Predicted thymidylate kinase, TKRP1 InterPro IPR014505 Human proteins containing this domain DTYMK See also Thymidine kinase Thymidylate synthase References reflist InterPro content IPR000062 DEFAULTSORT Thymidylate Kinase Category Protein families protein stub ... more details
Image EIF2regulation.jpg thumb Regulation of translation initiation via phosphorylation of Ser51 in eIF2 s subunit ref name pmid11042214 cite journal author Nika J, Rippel S, Hannig EM title Biochemical analysis of the eIF2beta gamma complex reveals a structural function for eIF2alpha in catalyzed nucleotide exchange journal J. Biol. Chem. volume 276 issue 2 pages 1051 6 year 2001 month January pmid 11042214 doi 10.1074 jbc.M007398200 url ref . eIF 2 is a kinase enzyme that phosphorylates eIF 2 . ref MeshName eIF 2 Kinase ref There are four forms in mammals EIF2AK1 heme regulated inhibitor kinase EIF2AK1 HRI EIF2AK2 the double stranded RNA dependent kinase Protein kinase R PKR EIF2AK3 PEK PERK EIF2AK4 EIF2AK4 GCN2 These are all responsible for the phosphorylation of the alpha subunit of eIF 2 at serine 51, one of the best characterized mechanisms for down regulating protein synthesis in eukaryote s in response to various cellular stress response s. References reflist Category Enzymes Serine threonine specific protein kinases Genetic translation enzyme stub ... more details
enzyme Name Polo kinase EC number 2.7.11.21 CAS number IUBMB EC number 2 7 11 21 GO code image width caption In enzymology , a polo kinase EC number 2.7.11.21 is a kinase enzyme i.e. one that catalysis catalyzes the chemical reaction ATP a protein math rightleftharpoons math ADP a phosphoprotein Thus, the two substrate biochemistry substrates of these enzymes are adenosine triphosphate ATP and protein , whereas their two product chemistry products are adenosine diphosphate ADP and phosphoprotein . These enzymes belong 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 polo like kinase enzyme class is ATP protein phosphotransferase Spindle apparatus spindle pole dependent . Examples and other names in common use include Cdc5 , Cdc5p , Plk , PLK , PLK1 Plk1 , Plo1 , POLO kinase , polo serine threonine kinase , polo like kinase , polo like kinase 1 , serine threonine specific Drosophila kinase polo , and STK21 . These enzymes participate in 3 metabolism metabolic pathways cell cycle , cell cycle yeast , and progesterone mediated oocyte maturation . 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 2OGQ , PDB link 2OJS , PDB link 2OJX , PDB link 2OU7 , and PDB link 2OWB . References reflist 1 cite journal author C, Karess RE, Glover DM, Sunkel CE date 1991 title polo encodes a protein kinase homolog required ... of a protein kinase encoding mouse gene, Plk, related to the polo gene of Drosophila 1993 cite ... and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle ... like kinase Plo1 to the spindle pole body and a functional spindle assembly checkpoint journal J. Cell ... author Ohkura H date 2003 title Phosphorylation polo kinase joins an elite club journal Curr. Biol ... more details
enzyme Name glycerol kinase EC number 2.7.1.30 CAS number IUBMB EC number GO code image width caption protein Name glycerol kinase caption image width HGNCid 4289 Symbol GK AltSymbols EntrezGene 2710 OMIM 300474 RefSeq NM 000167 UniProt P32189 PDB ECnumber 2.7.1.30 Chromosome X Arm p Band 21.3 LocusSupplementaryData Glycerol kinase is a phosphotransferase enzyme involved in triglyceride s and glycerophospholipid s synthesis. Glycerol kinase catalyzes the transfer of a phosphate from adenosine triphosphate ATP to glycerol thus forming glycerol phosphate ATP glycerol ADP sn glycerol 3 phosphate . Adipocytes lack glycerol kinase so they cannot metabolize the glycerol produced during triacyl glycerol degradation. This glycerol is instead shuttled to the liver via the blood where it is phosphorylated by glycerol kinase to glycerol phosphate converted to DHAP dihydroxyacetone phosphate which can participate in glycolysis or gluconeogenesis . 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 Structure Glycerol Kinase alternative name, ATP glycerol 3 phosphotransferase or Glycerokinase adopts a rnase H ribonuclease H like fold consisting of an alpha beta 2 layer sandwich of CATH family 3.30.420.40. As of 2010 03 , there were 20 structures of this protein in the PDB, most of which are homodimeric. See also glycerol kinase External links MeshName Glycerol Kinase References reflist Biochemistry, Champe, P.C., Harvey, R.A., Ferrier, D.R., 3rd ed., 2005. Kinases transferase stub de Glycerinkinasen ... more details
enzyme Name deoxynucleoside kinase EC number 2.7.1.145 CAS number 52227 81 3 IUBMB EC number 2 7 1 145 GO code 0019136 image width caption In enzymology , a deoxynucleoside kinase EC number 2.7.1.145 is an enzyme that catalysis catalyzes the chemical reaction ATP 2 deoxynucleoside math rightleftharpoons math ADP 2 deoxynucleoside 5 phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and 2 deoxynucleoside , whereas its two product chemistry products are adenosine diphosphate ADP and 2 deoxynucleoside 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 deoxynucleoside 5 phosphotransferase . Other names in common use include multispecific deoxynucleoside kinase , ms dNK , multisubstrate deoxyribonucleoside kinase , multifunctional deoxynucleoside kinase , D. melanogaster deoxynucleoside kinase , and Dm dNK . 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 1OE0 , PDB link 1OT3 , PDB link 1ZM7 , PDB link 1ZMX , and PDB link 2JCS . References reflist 1 cite journal author Munch Petersen B, Piskur J, Sondergaard L date 1998 title Four deoxynucleoside kinase activities from Drosophila melanogaster are contained within a single monomeric enzyme, a new multifunctional deoxynucleoside kinase journal J. Biol. Chem. volume 273 pages 3926&ndash 31 pmid 9461577 doi 10.1074 jbc.273.7.3926 issue 7 cite journal author Munch Petersen B, Knecht W, Lenz C, Sondergaard L, Piskur J date 2000 title Functional expression of a multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster and its C terminal deletion mutants journal J. Biol. Chem. volume 275 pages 6673&ndash 9 pmid 10692477 doi 10.1074 jbc.275.9.6673 issue 9 enzyme stub Category ... more details
orphan date March 2010 enzyme Name tagatose kinase EC number 2.7.1.101 CAS number 39434 00 9 IUBMB EC number 2 7 1 101 GO code 0050317 image width caption In enzymology , a tagatose kinase EC number 2.7.1.101 is an enzyme that catalysis catalyzes the chemical reaction ATP D tagatose math rightleftharpoons math ADP D tagatose 6 phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and D tagatose , whereas its two product chemistry products are adenosine diphosphate ADP and D tagatose 6 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 tagatose 6 phosphotransferase . Other names in common use include tagatose 6 phosphate kinase phosphorylating , D tagatose 6 phosphate kinase , and tagatose 6 phosphate kinase . This enzyme participates in galactose 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 2FIQ . References reflist 1 cite journal author Szumioo T year 1981 title A novel enzyme, tagatose kinase, from Mycobacterium butyricum journal Biochim. Biophys. Acta. volume 660 pages 366 70 pmid 6269638 issue 2 Category EC 2.7.1 Category Enzymes of known structure enzyme stub ... more details
enzyme Name undecaprenol kinase EC number 2.7.1.66 CAS number 9068 22 8 IUBMB EC number 2 7 1 66 GO code 0009038 image width caption In enzymology , an undecaprenol kinase EC number 2.7.1.66 is an enzyme that catalysis catalyzes the chemical reaction ATP undecaprenol math rightleftharpoons math ADP undecaprenyl phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and undecaprenol , whereas its two product chemistry products are adenosine diphosphate ADP and undecaprenyl 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 undecaprenol phosphotransferase . Other names in common use include isoprenoid alcohol kinase , isoprenoid alcohol phosphokinase , C55 isoprenoid alcohol phosphokinase , isoprenoid alcohol kinase phosphorylating , C55 isoprenoid alcohol kinase , C55 isoprenyl alcohol phosphokinase , and polyisoprenol kinase . This enzyme participates in peptidoglycan biosynthesis . References reflist 1 cite journal author Higashi Y, Siewert G, Strominger JL date 1970 title Biosynthesis of the peptidoglycan of bacterial cell walls. XIX Isoprenoid alcohol phosphokinase journal J. Biol. Chem. volume 245 pages 3683&ndash 90 pmid 4248528 issue 14 enzyme stub Category EC 2.7.1 Category Enzymes of unknown structure ... more details
enzyme Name pyruvate dehydrogenase cytochrome EC number 1.2.2.2 CAS number 9079 84 9 IUBMB EC number 1 2 2 2 GO code 0008985 image width caption In enzymology , a pyruvate dehydrogenase cytochrome EC number 1.2.2.2 is an enzyme that catalysis catalyzes the chemical reaction pyruvate ferricytochrome b sub 1 sub H sub 2 sub O math rightleftharpoons math acetate CO sub 2 sub ferrocytochrome b sub 1 sub The 3 substrate biochemistry substrates of this enzyme are pyruvate , ferricytochrome b1 , and water H sub 2 sub O , whereas its 3 product chemistry products are acetate , carbon dioxide CO sub 2 sub , and ferrocytochrome b1 . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is pyruvate ferricytochrome b1 oxidoreductase . Other names in common use include pyruvate dehydrogenase , pyruvic dehydrogenase , pyruvic cytochrome b1 dehydrogenase , pyruvate ubiquinone 8 oxidoreductase , and pyruvate oxidase ambiguous . This enzyme participates in pyruvate metabolism . It has 2 cofactor biochemistry cofactors FAD , and Thiamin diphosphate . References reflist 1 cite journal author Williams FR and Hager LP date 1961 title A crystalline flavin pyruvate oxidase journal J. Biol. Chem. volume 236 pages PC36&ndash PC37 cite journal author Koland JG, Gennis RB date 1982 title Identification of an active site cysteine residue in Escherichia coli pyruvate oxidase journal J. Biol. Chem. volume 257 pages 6023&ndash 7 pmid 7042705 issue 11 1.2 enzyme stub Category EC 1.2.2 Category Flavin enzymes Category Thiamin diphosphate enzymes Category Enzymes of unknown structure it Piruvato deidrogenasi citocromo ... more details
enzyme Name R 3 amino 2 methylpropionate pyruvate transaminase EC number 2.6.1.40 CAS number 37279 00 8 IUBMB EC number 2 6 1 40 GO code 0047305 image width caption In enzymology , a R 3 amino 2 methylpropionate pyruvate transaminase EC number 2.6.1.40 is an enzyme that catalysis catalyzes the chemical reaction R 3 amino 2 methylpropanoate pyruvate math rightleftharpoons math 2 methyl 3 oxopropanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are R 3 amino 2 methylpropanoate and pyruvate , whereas its two product chemistry products are 2 methyl 3 oxopropanoate and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is R 3 amino 2 methylpropanoate pyruvate aminotransferase . Other names in common use include D 3 aminoisobutyrate pyruvate transaminase , beta aminoisobutyrate pyruvate aminotransferase , D 3 aminoisobutyrate pyruvate aminotransferase , D 3 aminoisobutyrate pyruvate transaminase , R 3 amino 2 methylpropionate transaminase , and D beta aminoisobutyrate pyruvate aminotransferase . References reflist 1 cite journal author Kakimoto Y, Taniguchi K, Sano I year 1969 title D beta aminoisobutyrate pyruvate aminotransferase in mammalian liver and excretion of beta aminoisobutyrate by man journal J. Biol. Chem. volume 244 pages 335&ndash 40 pmid 5773299 issue 2 cite journal author Tamaki N, Sakata SF, Matsuda K year 2000 title Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver journal Methods Enzymol. volume 324 pages 376&ndash 89 pmid 10989446 doi 10.1016 S0076 6879 00 24247 X Category EC 2.6.1 Category Enzymes of unknown structure transferase stub ... more details
enzyme Name glycerate kinase EC number 2.7.1.31 CAS number 9026 61 3 IUBMB EC number 2 7 1 31 GO code 0008887 image width caption Pfam box Symbol Glyc kinase Name Glycerate kinase Pfam PF02595 InterPro IPR004381 PROSITE PDB PDB 1to6 In enzymology , a glycerate kinase EC number 2.7.1.31 is an enzyme that catalysis catalyzes the chemical reaction ATP R glycerate math rightleftharpoons math ADP 3 phospho R glycerate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and R glycerate , whereas its two product chemistry products are adenosine diphosphate ADP and 3 phospho R glycerate . 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 R glycerate 3 phosphotransferase . Other names in common use include glycerate kinase phosphorylating , D glycerate 3 kinase , D glycerate kinase , glycerate 3 kinase , GK , D glyceric acid kinase , and ATP D glycerate 2 phosphotransferase . This enzyme participates in 3 metabolism metabolic pathways serine glycine threonine metabolism, glycerolipid metabolism, and glyoxylate dicarboxylate 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 1TO6 , PDB link 1X3L , and PDB link 2B8N . References reflist 1 cite journal author Doughty CC, Hayashi JA, Guenther HL date 1966 title Purification and properties of D glycerate 3 kinase from Escherichia coli journal J. Biol. Chem. volume 241 pages 568&ndash 72 pmid 5325263 issue 3 cite journal author ICHIHARA A, GREENBERG DM date 1957 title Studies on the purification and properties of D glyceric acid kinase of liver journal J. Biol. Chem. volume 225 pages 949&ndash 58 pmid 13416296 issue 2 enzyme stub Category EC 2.7.1 Category Enzymes of known structure ... 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 Arginine pyruvate transaminase EC number 2.6.1.84 CAS number IUBMB EC number 2 6 1 84 GO code image width caption Orphan date February 2009 In enzymology , an arginine pyruvate transaminase EC number 2.6.1.84 is an enzyme that catalysis catalyzes the chemical reaction L arginine pyruvate math rightleftharpoons math 5 guanidino 2 oxopentanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are L arginine and pyruvate , whereas its two product chemistry products are 5 guanidino 2 oxopentanoate and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L arginine pyruvate aminotransferase . Other names in common use include arginine pyruvate transaminase , and AruH . References reflist 1 cite journal author Yang Z, Lu CD date 2007 title Characterization of an arginine pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1 journal J. Bacteriol. volume 189 pages 3954&ndash 9 pmid 17416668 doi 10.1128 JB.00262 07 issue 11 pmc 1913410 cite journal author Yang Z, Lu CD date 2007 title Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa journal J. Bacteriol. volume 189 pages 3945&ndash 53 pmid 17416670 doi 10.1128 JB.00261 07 issue 11 pmc 1913404 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name lysine pyruvate 6 transaminase EC number 2.6.1.71 CAS number 114189 79 6 IUBMB EC number 2 6 1 71 GO code 0050065 image width caption In enzymology , a lysine pyruvate 6 transaminase EC number 2.6.1.71 is an enzyme that catalysis catalyzes the chemical reaction L lysine pyruvate math rightleftharpoons math L 2 aminoadipate 6 semialdehyde L alanine Thus, the two substrate biochemistry substrates of this enzyme are L lysine and pyruvate , whereas its two product chemistry products are L 2 aminoadipate 6 semialdehyde and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L lysine pyruvate aminotransferase . Other names in common use include lysine pyruvate aminotransferase , and Lys AT . References reflist 1 cite journal author Schmidt H, Bode R and Birnbaum D date 1988 title A novel enzyme, L lysine pyruvate aminotransferase, catalyses the first step of lysine catabolism in Pichia guilliermondii journal FEMS Microbiol. Lett. volume 49 pages 203&ndash 206 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... 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
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