enzyme Name ATPadenylyltransferase EC number 2.7.7.53 CAS number 96697 71 1 IUBMB EC number 2 7 7 53 GO code 0003877 image width caption In enzymology , an ATPadenylyltransferase EC number 2.7.7.53 is an enzyme that catalysis catalyzes the chemical reaction ADP ATP math rightleftharpoons math phosphate P sub 1 sub ,P sub 4 sub bis 5 adenosyl tetraphosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP and adenosine triphosphate ATP , whereas its two product chemistry products are phosphate and P1,P4 bis 5 adenosyl tetraphosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ADP ATPadenylyltransferase . Other names in common use include bis 5 nucleosyl tetraphosphate phosphorylase NDP forming , diadenosinetetraphosphate alphabeta phosphorylase , adenine triphosphate adenylyltransferase , diadenosine 5 ,5 P1,P4 tetraphosphate alphabeta phosphorylase , ADP forming , and dinucleoside oligophosphate alphabeta phosphorylase . This enzyme participates in purine metabolism . References reflist 1 cite journal author Guranowski A, Blanquet S date 1985 title Phosphorolytic cleavage of diadenosine 5 ,5 P1,P4 tetraphosphate Properties of homogeneous diadenosine 5 ,5 P1,P4 tetraphosphate alpha, beta phosphorylase from Saccharomyces cerevisiae journal J. Biol. Chem. volume 260 pages 3542&ndash 7 pmid 2982863 issue 6 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name anthranilate adenylyltransferase EC number 2.7.7.55 CAS number 70248 64 5 IUBMB EC number 2 7 7 55 GO code 0047671 image width caption In enzymology , an anthranilate adenylyltransferase EC number 2.7.7.55 is an enzyme that catalysis catalyzes the chemical reaction ATP anthranilate math rightleftharpoons math diphosphate N adenylylanthranilate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and anthranilate , whereas its two product chemistry products are diphosphate and N adenylylanthranilate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP anthranilate N adenylyltransferase . This enzyme is also called anthranilic acid adenylyltransferase . References reflist 1 cite journal author Lerbs W, Luckner M date 1985 title Cyclopeptine synthetase activity in surface cultures of Penicillium cyclopium journal J. Basic. Microbiol. volume 25 pages 387&ndash 91 pmid 2995633 doi 10.1002 jobm.3620250611 issue 6 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name phenylalanine adenylyltransferase EC number 2.7.7.54 CAS number 98285 55 3 IUBMB EC number 2 7 7 54 GO code 0050173 image width caption In enzymology , a phenylalanine adenylyltransferase EC number 2.7.7.54 is an enzyme that catalysis catalyzes the chemical reaction ATP L phenylalanine math rightleftharpoons math diphosphate N adenylyl L phenylalanine Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and L phenylalanine , whereas its two product chemistry products are diphosphate and N adenylyl L phenylalanine . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP L phenylalanine adenylyltransferase . This enzyme is also called L phenylalanine adenylyltransferase . References reflist 1 cite journal author Lerbs W, Luckner M date 1985 title Cyclopeptine synthetase activity in surface cultures of Penicillium cyclopium journal J. Basic. Microbiol. volume 25 pages 387&ndash 91 pmid 2995633 doi 10.1002 jobm.3620250611 issue 6 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name glucose 1 phosphate adenylyltransferase EC number 2.7.7.27 CAS number 9027 71 8 IUBMB EC number 2 7 7 27 GO code 0008878 image width caption In enzymology , a glucose 1 phosphate adenylyltransferase EC number 2.7.7.27 is an enzyme that catalysis catalyzes the chemical reaction ATP alpha D glucose 1 phosphate math rightleftharpoons math diphosphate ADP glucose Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and alpha D glucose 1 phosphate , whereas its two product chemistry products are diphosphate and ADP glucose . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP alpha D glucose 1 phosphate adenylyltransferase . Other names in common use include ADP glucose pyrophosphorylase , glucose 1 phosphate adenylyltransferase , adenosine diphosphate glucose pyrophosphorylase , adenosine diphosphoglucose pyrophosphorylase , ADP glucose pyrophosphorylase , ADP glucose synthase , ADP glucose synthetase , ADPG pyrophosphorylase , ADP alpha D glucose 1 phosphate adenylyltransferase and AGPase . This enzyme participates in starch and sucrose 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 1YP2 , PDB link 1YP3 , and PDB link 1YP4 . References reflist 1 cite journal author Ghosh HP, Preiss J date 1966 title Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach leaf chloroplasts journal J. Biol. Chem. volume 241 pages 4491&ndash 504 pmid 5922972 issue 19 cite journal author Shen L and Preiss J date 1965 title Biosynthesis of bacterial glycogen. I. Purification and properties of the adenosine diphosphoglucose pyrophosphorylase of Arthrobacter species NRRL B1973 journal J. Biol. Chem. volume 240 pages ... more details
enzyme Name FMN adenylyltransferase EC number 2.7.7.2 CAS number 9026 37 3 IUBMB EC number 2 7 7 2 GO code 0003919 image width caption In enzymology , a FMN adenylyltransferase EC number 2.7.7.2 is an enzyme that catalysis catalyzes the chemical reaction ATP FMN math rightleftharpoons math diphosphate FAD Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and flavin mononucleotide FMN , whereas its two product chemistry products are diphosphate and FAD . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP FMN adenylyltransferase . This enzyme participates in riboflavin metabolism . Other names Other names in common use include FAD pyrophosphorylase riboflavin mononucleotide adenylyltransferase adenosine triphosphate riboflavin mononucleotide transadenylase adenosine triphosphate riboflavine mononucleotide transadenylase FAD synthetase riboflavin adenine dinucleotide pyrophosphorylase riboflavine References reflist 1 cite journal author GIRI KV, RAO NA, CAMA HR, KUMAR SA year 1960 title Studies on flavinadenine dinucleotide synthesizing enzyme in plants journal Biochem. J. volume 75 pages 381&ndash 6 pmid 13828163 pmc 1204435 cite journal author Schrecker AW and Kornberg A year 1950 title Reversible enzymatic synthesis of flavin adenine dinucleotide journal J. Biol. Chem. volume 182 pages 795&ndash 803 pmid 19994476 issue 2 Category EC 2.7.7 Category Enzymes of unknown structure enzyme stub de FAD Synthetase ... more details
enzyme Name sulfate adenylyltransferaseATP EC number 2.7.7.4 CAS number 9012 39 9 IUBMB EC number 2 7 7 4 GO code 0004781 image width caption Infobox protein family Symbol ATP sulfurylase Name ATP sulfurylase image PDB 1v47 EBI.jpg width caption crystal structure of atp sulfurylase from thermus thermophillus hb8 in complex with aps Pfam PF01747 Pfam clan InterPro IPR002650 SMART PROSITE MEROPS SCOP 1i2d TCDB OPM family OPM protein CAZy CDD In enzymology , a sulfate adenylyltransferase EC number 2.7.7.4 is an enzyme that catalysis catalyzes the chemical reaction ATP sulfate math rightleftharpoons math diphosphate adenylyl sulfate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and sulfate , whereas its two product chemistry products are diphosphate and adenylyl sulfate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP sulfate adenylyltransferase . Other names in common use include ATP sulfurylase , adenosine 5 triphosphate sulfurylase , adenosinetriphosphate sulfurylase , adenylylsulfate pyrophosphorylase , ATP sulfurylase , ATP sulfurylase , and sulfurylase . This enzyme participates in 3 metabolism metabolic pathways purine metabolism , selenoamino acid metabolism , and sulfur metabolism . Some sulfate adenylyltransferases are part of a bifunctional polypeptide polymer chain associated with adenosyl phosphosulfate kinase adenosyl phosphosulfate APS kinase . Both enzyme s are required for PAPS phosphoadenosine phosphosulfate synthesis from inorganic sulfate. ref name pmid8522184 cite journal author Rosenthal E, Leustek T title A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities journal Gene volume 165 issue 2 pages 243 ... , PDB link 1X6V , PDB link 1XJQ , PDB link 1XNJ , PDB link 1ZUN , and PDB link 2GKS . Applications ATP ... more details
enzyme Name polynucleotide adenylyltransferase EC number 2.7.7.19 CAS number 9026 30 6 IUBMB EC number 2 7 7 19 GO code 0004652 image width caption In enzymology , a polynucleotide adenylyltransferase EC number 2.7.7.19 is an enzyme that catalysis catalyzes the chemical reaction ATP RNAn math rightleftharpoons math diphosphate RNAn sup sup 1 Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and RNA , whereas its two product chemistry products are diphosphate and RNA with an extra adenosine nucleotide at its 3 end. Naming This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP polynucleotide adenylyltransferase . Other names in common use include NTP polymerase RNA adenylating enzyme AMP polynucleotidylexotransferase ATP polynucleotide adenylyltransferaseATP polynucleotidylexotransferase Poly A polymerase Poly A synthetase Polyadenylate nucleotidyltransferase Polyadenylate polymerase Polyadenylate synthetase Polyadenylic acid polymerase Polyadenylic polymerase Terminal riboadenylate transferase Poly A hydrolase RNA formation factors PF1 Adenosine triphosphate ribonucleic acid adenylyltransferase Function This enzyme is responsible for the addition of the 3 polyadenylation polyadenine tail to a newly synthesized pre messenger RNA pre mRNA molecule during the process of transcription genetics gene transcription . The protein is the final addition to a large protein complex that also contains smaller assemblies known as the cleavage and polyadenylation specificity factor CPSF and cleavage stimulatory factor CtSF and its binding is a necessary prerequisite to the cleavage of the 3 end of the pre mRNA. After cleavage of the 3 signaling region that directs the assembly of the complex, PAP adds the polyadenine tail to the new 3 end. The rate at which PAP adds adenine nucleotide s is dependent ... more details
enzyme Name aldose 1 phosphate adenylyltransferase EC number 2.7.7.36 CAS number 37278 27 6 IUBMB EC number 2 7 7 36 GO code 0047346 image width caption In enzymology , an aldose 1 phosphate adenylyltransferase EC number 2.7.7.36 is an enzyme that catalysis catalyzes the chemical reaction ADP alpha D aldose 1 phosphate math rightleftharpoons math phosphate ADP aldose Thus, the two substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP and alpha D aldose 1 phosphate , whereas its two product chemistry products are phosphate and ADP aldose . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ADP alpha D aldose 1 phosphate adenylyltransferase . Other names in common use include sugar 1 phosphate adenylyltransferase , ADPaldose phosphorylase , adenosine diphosphosugar phosphorylase , ADP sugar phosphorylase , adenosine diphosphate glucose orthophosphate adenylyltransferase , and ADP aldose 1 phosphate adenylyltransferase . References reflist 1 cite journal author Dankert M, Goncalves IRJ and Recondo E date 1964 title Adenosine diphosphate glucose orthophosphate adenylyltransferase in wheat germ journal Biochim. Biophys. Acta volume 81 issue 1 pages 78&ndash 85 doi 10.1016 0926 6569 64 90337 2 cite journal author Passeron S, Recondo E and Dankert M date 1964 title Biosynthesis of adenosine diphosphate D hexoses journal Biochim. Biophys. Acta volume 89 pages 372&ndash 374 pmid 14205499 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name ribose 5 phosphate adenylyltransferase EC number 2.7.7.35 CAS number 9054 55 1 IUBMB EC number 2 7 7 35 GO code 0047345 image width caption In enzymology , a ribose 5 phosphate adenylyltransferase EC number 2.7.7.35 is an enzyme that catalysis catalyzes the chemical reaction ADP D ribose 5 phosphate math rightleftharpoons math phosphate ADP ribose Thus, the two substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP and D ribose 5 phosphate , whereas its two product chemistry products are phosphate and ADP ribose . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ADP D ribose 5 phosphate adenylyltransferase . Other names in common use include ADP ribose phosphorylase , and adenosine diphosphoribose phosphorylase . References reflist 1 cite journal author Evans WR, San Pietro A date 1966 title Phosphorolysis of adenosine diphosphoribose journal Arch. Biochem. Biophys. volume 113 pages 236&ndash 44 pmid 4287446 doi 10.1016 0003 9861 66 90178 0 issue 1 cite journal author Stern AI, Avron M date 1966 title An adenosine 5 diphosphate ribose orthophosphate adenylyltransferase from Euglena gracilis journal Biochim. Biophys. Acta. volume 118 pages 577&ndash 91 pmid 5970863 issue 3 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name streptomycin 3 adenylyltransferase EC number 2.7.7.47 CAS number 52660 23 8 IUBMB EC number 2 7 7 47 GO code 0009012 image width caption In enzymology , a streptomycin 3 adenylyltransferase EC number 2.7.7.47 is an enzyme that catalysis catalyzes the chemical reaction ATP streptomycin math rightleftharpoons math diphosphate 3 adenylylstreptomycin Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and streptomycin , whereas its two product chemistry products are diphosphate and 3 adenylylstreptomycin . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP streptomycin 3 adenylyltransferase . Other names in common use include streptomycin adenylate synthetase , streptomycin adenyltransferase , streptomycin adenylylase , streptomycin adenylyltransferase , streptomycin spectinomycin adenylyltransferase , AAD 3 , and aminoglycoside 3 adenylyltransferase . References reflist 1 cite journal author Harwood JH, Smith DH date 1969 title Resistance factor mediated streptomycin resistance journal J. Bacteriol. volume 97 pages 1262&ndash 71 pmid 4887506 issue 3 pmc 249843 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
ATP may refer to Adenosine triphosphate , coenzyme used as an energy carrier in the cells of all known organisms Adenosine Tri Phosphate band , a Japanese alternative rock pop band Association of Tennis Professionals , a men s professional tennis association Arbejdsmarkedets Till gspension , the largest pension program in Denmark ATP Oil and Gas , a Texas based oil and gas company that operates in the Gulf of Mexico and the North Sea All Tomorrow s Parties music festival , a music festival which takes place in Great Britain Alberta Theatre Projects , a Canadian theatre production company ATP Recordings , a record label affiliated with the All Tomorrow s Parties festival Airline Transport Pilot License , a type of pilot s license BAe ATP , a British Aerospace turboprop passenger aircraft designed for the short range market Automatic Train Protection , a British train protection system Automated theorem proving , the proving of mathematical theorems by a computer program Advanced Technology Program , a United States Government program American Technical Publishers , an employee owned publishing company located in Orland Park, Illinois ATP, IATA airport code of Aitape Airport in Papua New Guinea disambiguation bg bs ATP vor ca ATP cs ATP da ATP de ATP et ATP es ATP eo ATP eu ATP argipena fa ATP fr ATP gl ATP ko ATP hr ATP id ATP it ATP jv ATP lb ATP hu ATP egy rtelm s t lap ms ATP nl ATP ja ATP no ATP andre betydninger pl ATP pt ATP ro ATP ru ATP stq ATP sk ATP sl ATP sr sh ATP fi ATP sv ATP th ATP tr ATP vi ATP zh ATP ... more details
, stabilization and some properties of ATP glutamine synthetase adenylyltransferase from ...Correct title Glutamate ammonia ligase adenylyltransferase reason bracket enzyme Name glutamate ammonia ligase adenylyltransferase EC number 2.7.7.42 CAS number 9077 66 1 IUBMB EC number 2 7 7 42 GO code 0008882 image width caption In enzymology , a glutamate ammonia ligase adenylyltransferase EC number 2.7.7.42 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate ammonia ligase ADP forming math rightleftharpoons math diphosphate adenylyl L glutamate ammonia ligase ADP forming Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and L glutamate ammonia ligase ADP forming , whereas its two product chemistry products are diphosphate and adenylyl L glutamate ammonia ligase ADP forming . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP L glutamate ammonia ligase ADP forming adenylyltransferase . Other names in common use include glutamine synthetase adenylyltransferase , ATP glutamine synthetase adenylyltransferase , and adenosine triphosphate glutamine synthetase adenylyltransferase . 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 1V4A . References reflist 1 cite journal author Ebner E, Wolf D, Gancedo C, Elsasser S, Holzer H date 1970 title ATP glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties journal Eur. J. Biochem. volume 14 pages 535&ndash 44 pmid 4920894 doi 10.1111 j.1432 1033.1970.tb00320.x issue 3 cite journal author Kingdon HS, Shapiro BM, Stadtman ER date 1967 title Regulation of glutamine synthetase. 8. ATP glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations ... more details
enzyme Name nicotinate nucleotide adenylyltransferase EC number 2.7.7.18 CAS number 9026 98 6 IUBMB EC number 2 7 7 18 GO code 0004515 image width caption In enzymology , a nicotinate nucleotide adenylyltransferase EC number 2.7.7.18 is an enzyme that catalysis catalyzes the chemical reaction ATP nicotinate ribonucleotide math rightleftharpoons math diphosphate deamido NAD sup sup Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and nicotinate ribonucleotide , whereas its two product chemistry products are diphosphate and deamido NAD . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP nicotinate ribonucleotide adenylyltransferase . Other names in common use include deamido NAD pyrophosphorylase , nicotinate mononucleotide adenylyltransferase , deamidonicotinamide adenine dinucleotide pyrophosphorylase , NaMN ATase , and nicotinic acid mononucleotide adenylyltransferase . This enzyme participates in nicotinate and nicotinamide metabolism . Structural studies As of late 2007, 9 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1K4K , PDB link 1K4M , PDB link 1KAM , PDB link 1KAQ , PDB link 1YUL , PDB link 1YUM , PDB link 1YUN , PDB link 2H29 , and PDB link 2H2A . References reflist 1 cite journal author IMSANDE J date 1961 title Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli journal J. Biol. Chem. volume 236 pages 1494&ndash 7 pmid 13717628 enzyme stub Category EC 2.7.7 Category Enzymes of known structure ... more details
enzyme Name nicotinamide nucleotide adenylyltransferase EC number 2.7.7.1 CAS number 9032 70 6 IUBMB EC number 2 7 7 1 GO code 0000309 image width caption In enzymology , a nicotinamide nucleotide adenylyltransferase EC number 2.7.7.1 is an enzyme that catalysis catalyzes the chemical reaction ATP nicotinamide ribonucleotide math rightleftharpoons math diphosphate NAD sup sup Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and nicotinamide ribonucleotide , whereas its two product chemistry products are diphosphate and nicotinamide adenine dinucleotide NAD sup sup . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP nicotinamide nucleotide adenylyltransferase . Other names in common use include NAD pyrophosphorylase , adenosine triphosphate nicotinamide mononucleotide transadenylase , ATP NMN adenylyltransferase , diphosphopyridine nucleotide pyrophosphorylase , nicotinamide adenine dinucleotide pyrophosphorylase , nicotinamide mononucleotide adenylyltransferase , and NMN adenylyltransferase . This enzyme participates in nicotinate and nicotinamide metabolism . The human version of this protein is NMNAT1 . Structural studies As of late 2007, 11 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EJ2 , PDB link 1GZU , PDB link 1HYB , PDB link 1KKU , PDB link 1KQN , PDB link 1KQO , PDB link 1KR2 , PDB link 1M8F , PDB link 1M8G , PDB link 1M8J , and PDB link 1M8K . References reflist 1 cite journal author ATKINSON MR, JACKSON JF, MORTON RK date 1961 title Nicotinamide mononucleotide adenylyltransferase of pig liver nuclei. The effects of nicotinamide mononucleotide concentration and pH on dinucleotide synthesis ... de Nicotinamidnukleotid Adenylyltransferase ... more details
enzyme Name pantetheine phosphate adenylyltransferase EC number 2.7.7.3 CAS number 9026 99 7 IUBMB EC number 2 7 7 3 GO code 0004595 image 1vlh.png width caption Phosphopantetheine adenylyltransferase from Thermotoga maritima . 4 Phosphopantetheine shown as spheres. Protein Data Bank PDB PDBe 1vlh In enzymology , a pantetheine phosphate adenylyltransferase EC number 2.7.7.3 is an enzyme that catalysis catalyzes the chemical reaction ATP 4 Phosphopantetheine math rightleftharpoons math diphosphate 3 dephospho CoA Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and Phosphopantetheine 4 Phosphopantetheine , whereas its two product chemistry products are diphosphate and 3 dephospho CoA . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ATP pantetheine 4 phosphate adenylyltransferase . Other names in common use include dephospho CoA pyrophosphorylase , pantetheine phosphate adenylyltransferase , dephospho coenzyme A pyrophosphorylase , and 3 dephospho CoA pyrophosphorylase . This enzyme participates in pantothenate and coa biosynthesis . 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 1B6T , PDB link 1GN8 , PDB link 1H1T , PDB link 1O6B , PDB link 1OD6 , PDB link 1QJC , PDB link 1TFU , and PDB link 1VLH . References reflist 1 cite journal author HOAGLAND MB, NOVELLI GD date 1954 title Biosynthesis of coenzyme A from phospho pantetheine and of pantetheine from pantothenate journal ... of pantetheine phosphate adenylyltransferase journal Biochem. Biophys. Res. Commun. volume ... A, Lewendon A, Shaw WV date 1999 title Purification and characterization of phosphopantetheine adenylyltransferase ... JJ date Pt 6 title Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli ... more details
enzyme Name adenylylsulfate ammonia adenylyltransferase EC number 2.7.7.51 CAS number 79121 94 1 IUBMB EC number 2 7 7 51 GO code 0047352 image width caption In enzymology , an adenylylsulfate ammonia adenylyltransferase EC number 2.7.7.51 is an enzyme that catalysis catalyzes the chemical reaction adenylyl sulfate NH sub 3 sub math rightleftharpoons math adenosine 5 phosphoramidate sulfate. Thus, the two substrate biochemistry substrates of this enzyme are adenylyl sulfate and ammonia NH sub 3 sub , whereas its two product chemistry products are adenosine 5 phosphoramidate and sulfate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is adenylyl sulfate ammonia adenylyltransferase . Other names in common use include APSAT , and adenylylsulfate ammonia adenylyltransferase . References reflist 1 cite journal author Fankhauser H, Garber L and Schiff JA date 1979 title Adenylyl sulfate APS ammonia adenylyl transferase APSAT forming adenosine 5 phosphoramidate APA from APS and ammonia journal Plant Physiol. volume 63S pages 162 cite journal author Fankhauser H and Schiff JA date 1980 title Further purification and properties of adenylyl sulfate APS ammonia adenylyl transferase APSAT from Chlorella journal Plant Physiol. volume 65S pages 17 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
enzyme Name sulfate adenylyltransferase ADP EC number 2.7.7.5 CAS number 9027 70 7 IUBMB EC number 2 7 7 5 GO code 0004780 image width caption In enzymology , a sulfate adenylyltransferase ADP EC number 2.7.7.5 is an enzyme that catalysis catalyzes the chemical reaction ADP sulfate math rightleftharpoons math phosphate adenylyl sulfate Thus, the two substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP and sulfate , whereas its two product chemistry products are phosphate and adenylyl sulfate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is ADP sulfate adenylyltransferase . Other names in common use include ADP sulfurylase , sulfate adenosine diphosphate adenylyltransferase , and adenosine diphosphate sulfurylase . This enzyme participates in sulfur metabolism . References reflist 1 cite journal author Grunberg Manago M, Del Campillo Campbell A, Dondon L, Michelson AM date 1966 title Yeast ADP sulfurylase catalyzing an exchange between orthophosphate and the terminal phosphate of nucleoside diphosphates journal Biochim. Biophys. Acta. volume 123 pages 1&ndash 16 pmid 5964041 issue 1 cite journal author ROBBINS PW, LIPMANN F date 1957 title Isolation and identification of active sulfate journal J. Biol. Chem. volume 229 pages 837&ndash 51 pmid 13502346 issue 2 enzyme stub Category EC 2.7.7 Category Enzymes of unknown structure ... more details
ATP Records may refer to ATP World Tour records , a list of records related to the Association of Tennis Professionals ATP Recordings , a British record label disambig ... more details
refimprove date October 2009 The ATP test is a process of rapidly measuring actively growing microorganisms through detection of adenosine triphosphate , or ATP. ATP testing method ATP is a molecule found in and around living cell biology cells , and as such it gives a direct measure of biological concentration and health. ATP is quantified by measuring the light produced through its reaction with the naturally occurring firefly enzyme luciferase using a photometer luminometer . The amount of light produced is directly proportional to the amount of living organisms present in the sample. ATP tests can be used to Control biological treatment reactors Guide biocide dosing programs Determine drinking water cleanliness Manage Fermentation biochemistry fermentation processes Assess soil activity Determine corrosion deposit process type Measure equipment or product sanitation 1st generation testing vs . 2nd generation testing 1st generation ATP tests are derived from hygiene monitoring uses where samples are relatively free of interferences. 2nd Generation tests are specifically designed for water, wastewater and industrial applications where, for the most part, samples contain a variety of components that can interfere with the ATP assay. How ATP is measured Within a water sample containing microorganisms, there are two types of ATP Intracellular ATPATP contained within living biological cells. Extracellular ATPATP located outside of biological cells that has been released from dead or stressed organisms. Accurate measurement of these two types of ATP is critical to utilizing ATP based measurements. Being able to accurately measure these different types of ATP offers the ability to assess biological health and activity, and subsequently control water and wastewater processes. See also Adenosine triphosphate External links http www.academy.luminultra.com images stories docs TLD science of atp monitoring.pdf The Science Behind ATP Monitoring. References reflist 2 Category ... more details
The Association of Tennis Professionals ATP Bologna can refer to two men s professional tennis tournaments held in Bologna , Italy the ATP Bologna Indoor , an indoor carpet court event held from 1978 81 the ATP Bologna Outdoor , an outdoor clay court event held from 1985 98 Sportindex ... more details
unreferenced date February 2012 main ATP Tour The ATP defined the ATP Race as an easy to understand, simple to follow annual race from season start to season end. Every player starts at zero at the beginning of the year and the player who accumulates the most points by season s end is the World Number 1 and claims that the Race is the mathematical method of ranking male professional tennis players on a calendar year basis. According to the ATP Every player, regardless of his performances in the previous year, starts with zero points. Players count 18 performances in their Indesit INDESIT ATP 2005 Race total. Players eligible to enter the Grand Slams and Tennis Masters Series events must count those events and their best five other results from the International Series events. The Tennis Masters Cup will count as an additional 19th tournament for the eight players who qualify. During the 2009 ATP rebranding, the ATP Race ranking system was discarded in favour of solely having the calendar year ranking system. Points Distribution ATP Race Points Distribution List of ATP Race champions class wikitable Year Champion Points 2000 flagicon BRA Gustavo Kuerten 839 2001 flagicon AUS Lleyton Hewitt 897 2002 flagicon AUS Lleyton Hewitt 2 873 2003 flagicon USA Andy Roddick 907 2004 flagicon SUI Roger Federer 1,267 2005 flagicon SUI Roger Federer 2 1,345 2006 flagicon SUI Roger Federer 3 1,674 2007 flagicon SUI Roger Federer 4 1,436 2008 flagicon ESP Rafael Nadal 1,335 2009 flagicon SUI Roger Federer 5 1,055 See also ATP World Tour records ATP World Tour Awards ATP World Tour Masters 1000 List of ATP number 1 ranked players Tennis statistics Tennis male players statistics External links http www.atptennis.com 3 en rankings ATP Rankings ATP seasons Category ATP Tour fr ATP Race ... more details
image Atp synthase.PNG right thumb 300px Molecular model of ATP synthase by X ray diffraction method enzyme Name atp synthase EC number 3.6.3.14 IUBMB EC number 3 6 3 14 CAS number 9000 83 3 GO code 0046961 image width caption ATP synthase EC number 3.6.3.14 is an important enzyme that provides energy for the cell to use through the synthesis of adenosine triphosphate ATP . adenosine triphosphate ATP ... is ATP synthase ADP P sub i sub ATP Synthase ATP Energy is often released in the form of protium ... within the mitochondria , ATP synthase consists of 2 regions the F sub O sub portion is within the membrane. The F sub 1 sub portion of the ATP synthase is above the membrane, inside the matrix ... author Mccarty RE title A PLANT BIOCHEMIST S VIEW OF H ATPases AND ATP SYNTHASES journal J. Exp ... sub unit of ATP synthase. These functional regions consist of different protein subunits refer to tables. F sub 1 sub ATP Synthase structure The F sub 1 sub particle is large and can be seen in the transmission ... activity was further associated with the creation of ATP by a long series of experiments in many laboratories. class wikitable style text align center F sub 1 sub ATP SYNTHASE SUBUNITS Subunit Human Gene ATP synthase alpha beta subunits alpha ATP5A1 , ATPAF2 ATP synthase alpha beta subunits beta ATP5B , ATPAF1 , C16orf7 ATP synthase gamma subunit gamma ATP5C1 ATP synthase delta subunit delta ATP5D ATP synthase epsilon ATP5E F sub O sub ATP Synthase Structure The F sub O sub region of ATP synthase ... ATP8 8 or A6L . class wikitable style text align center F sub O sub ATP SYNTHASE MAIN SUBUNITS Subunit Human Gene ATP synthase subunits A A ATP6 ATP synthase subunit B B ATP5F1 ATP synthase subunit ... Paul Boyer developed the binding change, or flip flop, mechanism, which postulated that ATP synthesis is coupled with a conformational change in the ATP synthase generated by rotation of the gamma subunit ..., crystallized the F sub 1 sub catalytic domain of ATP synthase. The structure, at the time the largest ... more details
Refimprove date December 2009 ATP hydrolysis is the reaction by which chemical energy that has been stored and transported in the High energy phosphate high energy phosphoanhydridic bonds in adenosine triphosphate ATP Adenosine triphosphate is released, for example in the muscles, to produce work. The product is adenosine diphosphate ADP Adenosine diphosphate and an inorganic phosphate , orthophosphate Pi . ADP can be further hydrolyzed to give energy, adenosine monophosphate AMP Adenosine monophosphate , and another orthophosphate Pi . ATP hydrolysis is the final link between the energy derived from food or sunlight and useful work such as muscle contraction, the establishment of ion gradients across membranes, and biosynthetic processes necessary to maintain life. The description and typical textbook labeling of ATP phosphanhydridic bonds as high energy . . bonds can be very misleading to students. These bonds are in fact relatively weak. They do involve high energy electrons but the bonds themselves are quite easy to break. As noted below, energy is released by the hydrolysis of ATP ... and becomes more stable. Hydrolysis of the phosphate groups in ATP is especially exergonic , because ... the products ADP and P sub i sub much lower in energy than the reactant ATP . The negative charge density associated with the three adjacent phosphate units of ATP also destabilizes the molecule, making .... The actual value of G for ATP hydrolysis varies, primarily depending on Mg sup 2 sup concentration ..., approximately 60 percent of the energy released from the hydrolysis of one Mole unit mole of ATP produces ... 2008 Due to the acid base properties of ATP, ADP, and inorganic phosphate, the hydrolysis of ATP ... library crofts bioph354 atp hydrolysis.html ref Under certain conditions, high levels of ATP hydrolysis ... of ATP Image Adenosindiphosphat protoniert.svg 200px thumb Structure of ADP Image Ortho resonance.svg ... References reflist DEFAULTSORT Atp Hydrolysis Category Cellular respiration Category Exercise physiology ... more details
The ATP Bolzano was a men s tennis tournament played in Bolzano , Italy . The event was played as part of the ATP World Series of the ATP Tour in 1992 and 1993. It was played on indoor carpet courts. Singles class wikitable style font size 90 Year width 200 Champions width 200 Runners up width 125 Score 1992 flagicon SWE Thomas Enqvist flagicon FRA Arnaud Boetsch 6 2, 1 6, 7 6 1993 flagicon USA Jonathan Stark flagicon FRA C dric Pioline 6 3, 6 2 Doubles class wikitable style font size 90 Year width 200 Champions width 200 Runners up width 125 Score 1992 flagicon SWE Anders J rryd br flagicon NOR Bent Ove Pedersen flagicon NED Tom Nijssen br flagicon TCH Cyril Suk 6 1, 6 7, 6 3 1993 flagicon NED Hendrik Jan Davids br flagicon RSA 1928 Piet Norval flagicon RSA 1928 David Adams tennis David Adams br flagicon RUS Andrei Olhovskiy 6 3, 6 2 References ATP Tour http www.atptennis.com 5 en vault ATP World Series tournaments DEFAULTSORT Bolzano Category Carpet court tennis tournaments Category Indoor tennis tournaments Category Tennis tournaments in Italy Category ATP Tour de ATP Bozen it ATP Bolzano nl ATP toernooi van Bolzano ... more details
enzyme Name ATP deaminase EC number 3.5.4.18 CAS number 37289 21 7 IUBMB EC number 3 5 4 18 GO code 0047692 image width caption In enzymology , an ATP deaminase EC number 3.5.4.18 is an enzyme that catalysis catalyzes the chemical reaction ATP H sub 2 sub O math rightleftharpoons math ITP NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and water H sub 2 sub O , whereas its two product chemistry products are ITP and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is ATP aminohydrolase . This enzyme is also called adenosine triphosphate deaminase . References reflist 1 cite journal author Chung ST, Aida K date Tokyo title Purification and properties of ATP deaminase from Microsporum audouini journal J. volume Biochem. pages 1&ndash 9 pmid 6048966 issue 1 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
Encyclopedia
top
