Image Phosphate formula.svg thumb Phosphate See also Protein kinase In biochemistry , a kinase ref name pmid12471243 cite journal author Manning G, Whyte DB. et al. title The protein kinase complement of the human genome journal Science volume 298 issue 5600 pages 1912 1934 year 2002 pmid 12471243 doi 10.1126 science.1075762 url ref is a type of enzyme that transfers phosphate groups from High energy phosphate high energy donor molecules, such as adenosine triphosphate ATP , ref http nobelprize.org nobel prizes chemistry laureates 1997 illpres history.html History of ATP research milestones from an ATP related chemistry Nobel Prize site. ref to specific Substrate biochemistry substrate s, a process referred to as phosphorylation . Kinases are part of the larger family of phosphotransferase s. Kinases are not to be confused with phosphorylase s, which carry out phosphorolysis , the breaking of a bond using an inorganic phosphate group or with phosphatase s, which remove phosphate groups. Types One of the largest groups of kinases are protein kinase s, which act on and modify the activity of specific proteins. Kinases are used extensively to transmit signals and control complex processes in cells. More than five hundred different kinases have been identified in humans. Their enormous diversity, as well as their role in signaling, makes them an object of study. Various other kinases act on small molecules such as lipid s, carbohydrate s, amino acid s, and nucleotide s, either for signaling ... Reflist 2 See also Cyclin dependent kinase Ca2 calmodulin dependent protein kinase Ca sup 2 sup calmodulin dependent protein kinase Signal transduction G protein coupled receptor Kinases Category EC 2.7.1 an Quinasa ca Cinasa cs Kin za de Kinase es Quinasa fa fr Kinase gl Quinase ko io Kinazo id Kinase it Chinasi he nl Kinase ja oc Quinasa pl Kinazy pt Cinase ru sr Kinaza fi Kinaasi sv Kinas ta uk vi Kinase zh ... more details
MAP kinasekinasekinase or MAP3K or MEKK is a serine threonine specific protein kinase which acts upon MAP kinasekinase . In humans there are at least 19 genes MAP3K1 aka MEKK1 MAP3K2 MAP3K3 aka MAP3K3 MEKK3 MAP3K4 MAP3K5 aka ASK1 MAP3K6 aka ASK2 MAP3K7 aka MAP3K7 MEKK7 aka TAK1 MAP3K8 aka TPL2 or Tpl2 MAP3K9 MAP3K10 MAP3K11 aka MAP3K11 MEKK11 aka MLK3 MAP3K12 aka MUK MAP3K13 aka LZK MAP3K14 MAP3K15 MAP3K16 aka TAO1 or TAOK1 MAP3K17 aka TAO2 or TAOK2 RAF1 BRAF ARAF ZAK aka MLTK Perhaps the best characterized MAP3K are the members of the oncogenic RAF family RAF1, BRAF, ARAF , which are effectors of mitogenic ras signaling and which activate the MAPK ERK pathway ERK1 2 MAPK3 MAPK1 pathway , through activation of MEK1 MAP2K1 and MEK2 MAP2K2 . MEKK1 activates C Jun N terminal kinases MAPK8 JNK by phosphorylation of its activator SEK1 MAP2K4 . ref cite journal author Yan M title Activation of stress activated protein kinase by MEKK1 phosphorylation of its activator SEK1 year 1994 journal Nature volume 372 pages 798 800 pmid 7997270 issue 6508 author separator , display authors 1 last2 Dai first2 T last3 Deak first3 JC last4 Kyriakis first4 JM last5 Zon first5 LI last6 Woodgett first6 JR last7 Templeton first7 DJ doi 10.1038 372798a0 ref MAP3K3 directly regulates the C Jun N terminal kinases MAPK8 JNK and MAPK ERK pathway extracellular signal regulated protein kinase ERK pathways by activating SEK and MEK1 2 respectively it does not regulate the p38 mitogen activated protein kinases p38 pathway. ref cite journal author Ellinger Ziegelbauer H title Direct activation of the stress activated protein kinase SAPK and extracellular signal regulated protein kinase ERK pathways by an inducible mitogen activated protein Kinase ERK kinasekinase 3 MEKK derivative year 1997 journal J ... names. gallery External links MeshName MAP KinaseKinase Kinases EC number 2.7.11.25 References Reflist biochemistry stub MAP kinase activation Serine threonine specific protein kinases es MAP quinasa ... more details
Mitogen activated protein kinasekinasekinasekinase MAP4K is a family of proteins involved in cellular signal transduction . Expand list date May 2011 MAP4K1 aka HPK1 MAP4K2 aka GCK MAP4K3 MAP4K4 MAP4K5 Additional images gallery File Signal transduction pathways.svg Some signal transduction pathways. MAP4K s not labelled. File MAPKpathway.jpg MAPK pathway. Some or all of the MAP4K s in this image are labelled by other names, such as HPK1 and GCK. gallery See also Signal transduction MAP kinase MAP kinasekinase MAP kinasekinasekinase References references MAP kinase activation Serine threonine specific protein kinases biochemistry stub ... more details
enzyme Name dephospho reductase kinasekinase EC number 2.7.11.3 CAS number 72060 33 4 IUBMB EC number 2 7 11 3 GO code 0047848 image width caption In enzymology , a dephospho reductase kinasekinase EC number 2.7.11.3 is an enzyme that catalysis catalyzes the chemical reaction ATP dephospho hydroxymethylglutaryl CoA reductase NADPH kinase math rightleftharpoons math ADP hydroxymethylglutaryl CoA reductase NADPH kinase Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and dephospho hydroxymethylglutaryl CoA reductase NADPH kinase , whereas its two product chemistry products are adenosine diphosphate ADP and hydroxymethylglutaryl CoA reductase NADPH kinase . 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 dephospho hydroxymethylglutaryl CoA reductase NADPH kinase phosphotransferase . Other names in common use include AMP activated kinase , AMP activated protein kinasekinase , hydroxymethylglutaryl coenzyme A reductase kinasekinase , hydroxymethylglutaryl coenzyme A reductase kinasekinase , phosphorylating , reductase kinase , reductase kinasekinase , and STK30 . References reflist 1 cite journal author Beg ZH, Stonik JA, Brewer HB Jr year 1979 title Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3 hydroxy 3 methylglutaryl coenzyme A reductase journal Proc. Natl. Acad. Sci. U.S.A. volume 76 pages 4375&ndash 9 pmid 291971 doi 10.1073 pnas.76.9.4375 issue 9 pmc ... activated and phospholipid dependent protein kinase journal J. Biol. Chem. volume 260 pages 1682&ndash ... CoA reductase identification of the site phosphorylated by the AMP activated protein kinase in vitro ... 3 hydroxy 3 methylglutaryl CoA reductase prevents phosphorylation by AMP activated kinase and blocks ... more details
Casein kinase is a kinase enzyme. Casein kinase 1 Casein kinase 2 Short pages monitor This long comment was added to the page to prevent it from being listed on Special Shortpages. It and the accompanying monitoring template were generated via Template Long comment. Please do not remove the monitor template without removing the comment as well. biochemistry stub Category Enzymes ... more details
protein Name phosphomevalonate kinase caption image width HGNCid 9141 Symbol PMVK AltSymbols EntrezGene 10654 OMIM 607622 RefSeq NM 006556 UniProt Q15126 PDB ECnumber 2.7.4.2 Chromosome 1 Arm p Band 13 LocusSupplementaryData q23 Phosphomevalonate kinase is an enzyme in the mevalonate pathway. Image Mevalonate pathway.png 350px thumb center Mevalonate pathway External links MeshName Phosphomevalonate kinase biochemistry stub Kinases Mevalonate pathway de Phosphomevalonat Kinase ... more details
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
Image Ch4 kinases.jpg thumb 250px right Protein phosphorylation A protein kinase is a kinase enzyme that modifies ... genome contains about 500 protein kinase genes and they constitute about 2 of all human genes. ref name pmid12471243 cite journal author Manning G, Whyte DB. et al. title The protein kinase complement ... to 30 of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority ... H white . The chemical activity of a kinase involves transferring a phosphate group from a nucleoside ... dual specificity kinase s act on all three. ref cite journal author Dhanasekaran N, Premkumar Reddy ... kinases that phosphorylate other amino acids, including histidine kinase s that phosphorylate ... is highly regulated. Kinases are turned on or off by phosphorylation sometimes by the kinase itself ... relative to their substrates. Structure main Protein kinase domain The catalytic subunits of many ... cite journal author Hanks SK title Genomic analysis of the eukaryotic protein kinase superfamily ... cite journal author Hanks SK, Hunter T title Protein kinases 6. The eukaryotic protein kinase superfamily kinase catalytic domain structure and classification journal FASEB J. volume 9 issue 8 ... 7768349 issn ref ref name pmid1835513 cite journal author Hunter T title Protein kinase classification ... kinase catalytic domain sequence database identification of conserved features of primary structure ... Crystal structure of the catalytic subunit of cyclic adenosine monophosphate dependent protein kinase ... science.1862342 url issn ref Protein kinase groups The human protein kinase family is divided into the following groups AGC kinases containing Protein kinase A PKA , Protein kinase c PKC and Protein kinase g PKG . CaM Kinase CaM kinases containing the calcium calmodulin dependent protein kinases. Ck1 CK1 containing the casein kinase 1 group. CMGC containing Cyclin dependent kinase CDK , MAPK , GSK3 ... kinases. Tyrosine kinase TK containing the tyrosine kinases. TKL containing the tyrosine kinase like ... 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 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
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
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