image Atp synthase.PNG right thumb 300px Molecular model of ATPsynthase by X ray diffraction method enzyme Name atpsynthase EC number 3.6.3.14 IUBMB EC number 3 6 3 14 CAS number 9000 83 3 GO code 0046961 image width caption ATPsynthase EC number 3.6.3.14 is an important enzyme that provides energy ... sequence is ATPsynthase ADP P sub i sub ATPSynthaseATP This energy is often in the form of protium ... Located within the mitochondria , ATPsynthase consists of 2 regions the F sub O sub portion is within the membrane. The F sub 1 sub portion of the ATPsynthase is above the membrane, inside the matrix ... sub unit of ATPsynthase. These functional regions consist of different protein subunits refer to tables. F sub 1 sub ATPSynthase structure The F sub 1 sub particle is large and can be seen in the transmission .... class wikitable style text align center F sub 1 sub ATPSYNTHASE SUBUNITS Subunit Human Gene ATPsynthase alpha beta subunits alpha ATP5A1 , ATPAF2 ATPsynthase alpha beta subunits beta ATP5B , ATPAF1 , C16orf7 ATPsynthase gamma subunit gamma ATP5C1 ATPsynthase delta subunit delta ATP5D ATPsynthase epsilon ATP5E F sub O sub ATPSynthase Structure The F sub O sub region of ATPsynthase ..., and MT ATP8 8 or A6L . class wikitable style text align center F sub O sub ATPSYNTHASE MAIN SUBUNITS Subunit Human Gene ATPsynthase subunits A A ATP6 ATPsynthase subunit B B ATP5F1 ATPsynthase subunit ... is coupled with a conformational change in the ATPsynthase generated by rotation of the gamma subunit ... catalytic domain of ATPsynthase. The structure, at the time the largest asymmetric protein structure ..., Na , K ATPase. Image ATPsyn.gif thumb 220px right Mechanism of ATPsynthase. ATP is shown in red ... via the F sub O sub region of ATPsynthase. A portion of the F sub O sub the ring of ATPsynthase .... The ATPsynthase subunit C c ring is tightly attached to the asymmetric central stalk consisting ... 3 sub to the non rotating portion of F sub O sub . The structure of the intact ATPsynthase is currently ... more details
enzyme Name ATP citrate synthase EC number 2.3.3.8 CAS number 9027 95 6 IUBMB EC number 2 3 3 8 GO code 0003878 image width caption In enzymology , an ATP citrate synthase EC number 2.3.3.8 is an enzyme that catalysis catalyzes the chemical reaction ADP phosphate acetyl CoA oxaloacetate math rightleftharpoons math ATP citrate CoA The 4 substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP , phosphate , acetyl CoA , and oxaloacetate , whereas its 3 product chemistry products are adenosine triphosphate ATP , citrate , and coenzyme A CoA . This enzyme belongs to the family of transferase s, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl CoA oxaloacetate C acetyltransferase pro S carboxymethyl forming, ADP phosphorylating . Other names in common use include ATP citric lyase , ATP citrate oxaloacetate lyase pro S CH2COO acetyl CoA , ATP dephosphorylating , acetyl CoA oxaloacetate acetyltransferase isomerizing , ADP phosphorylating , adenosine triphosphate citrate lyase , citrate cleavage enzyme , citrate ATP lyase , citric cleavage enzyme , and ATP citrate pro S lyase . This enzyme participates in citrate cycle tca cycle and reductive carboxylate cycle co2 fixation . References reflist 1 cite journal author Lill U, Schreil A, Eggerer H date 1982 title Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase journal Eur. J. Biochem. volume 125 pages 645&ndash 50 pmid 6749502 doi 10.1111 j.1432 1033.1982.tb06731.x issue 3 cite journal author Srere PA and Lipmann F date 1953 title An enzymatic reaction between citrate, adenosine triphosphate and coenzyme A journal J. Am. Chem. Soc. volume 75 pages 4874 doi 10.1021 ja01115a547 issue 19 transferase stub Category EC 2.3.3 Category Enzymes of unknown structure it ATP citrato sintasi ... more details
merge ATP5C1 discuss Talk THIS PAGE Merger proposal date February 2011 Pfam box Symbol ATP synt Name ATPsynthase image PDB 1bmf EBI.jpg width caption Structure of F1 ATPase. ref name pmid8065448 cite journal author Abrahams JP, Leslie AG, Lutter R, Walker JE title Structure at 2.8 A resolution of F1 ATPase from bovine heart mitochondria journal Nature volume 370 issue 6491 pages 621 8 year 1994 month August pmid 8065448 doi 10.1038 370621a0 url ref Pfam PF00231 InterPro IPR000131 SMART PROSITE PDOC00138 SCOP 1bmf TCDB OPM family OPM protein PDB PDB3 1fs0 G 19 248 PDB3 1w0k G 26 297 PDB3 1h8e G 26 297 PDB3 1cow G 26 297 PDB3 1e1q G 26 297 PDB3 1w0j G 26 297 PDB3 1h8h G 26 297 PDB3 1bmf G 26 297 PDB3 1e1r G 26 297 PDB3 1efr G 26 297 PDB3 1nbm G 26 297 Gamma subunit of ATPsynthase F1 complex forms the central shaft that connects the F0 rotary motor to the F1 catalytic core. F ATPsynthase s also known as F1F0 ATPase, or H transporting two sector ATPase EC number 3.6.3.14 are composed of two linked complexes the F1 ATPase complex is the catalytic core and is composed of 5 subunits alpha, beta, gamma, ATPsynthase delta subunit delta , epsilon , while the F0 ATPase complex is the biological membrane membrane embedded proton channel that is composed of at least 3 subunits A C , nine in mitochondria A G, F6, F8 . The human ATPsynthase gamma subunit is encoded by the gene ATP5C1 . Molecular Interactions Both the F1 and F0 complexes are rotary motors that are coupled back to back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha 3 ... cite journal author Junge W, Feniouk BA title Regulation of the F0F1 ATPsynthase the conformation ... for assembly and catalysis . References reflist InterPro content IPR000131 DEFAULTSORT AtpSynthase ... gradient to push the F1 rotor in reverse in order to drive ATP synthesis ref name PUB00009752 cite ... to hydrolyse ATP to create a proton gradient. The ATPase F1 complex gamma subunit forms the central ... more details
merge ATP50 discuss Talk THIS PAGE Merger proposal date February 2011 Pfam box Symbol OSCP Name ATPsynthase delta OSCP subunit image PDB 1abv EBI.jpg width caption Structure of the N terminal domain of the delta subunit of the E. coli ATPsynthase. ref name pmid9164460 cite journal author Wilkens S, Dunn SD, Chandler J, Dahlquist FW, Capaldi RA title Solution structure of the N terminal domain of the delta subunit of the E. coli ATPsynthase journal Nat. Struct. Biol. volume 4 issue 3 pages 198 201 year 1997 month March pmid 9164460 doi 10.1038 nsb0397 198 url ref Pfam PF00213 InterPro IPR000711 SMART PROSITE PDOC00327 SCOP 1abv TCDB 3.A.2 OPM family OPM protein PDB PDB3 2a7u B 7 135 PDB3 1abv 7 106 PDB3 2bo5 A 37 143 ATPsynthase delta subunit is a subunit of bacteria l and chloroplast ATPase , or OSCP oligomycin sensitivity conferral protein in mitochondrial ATPase note that in mitochondria there is a different delta subunit, InterPro IPR001469 . The OSCP delta subunit appears to be part of the peripheral stalk that holds the F1 complex alpha3beta3 catalytic core stationary against the torque of the rotating central stalk, and links subunit A of the F0 complex with the F1 complex. In mitochondria, the peripheral stalk consists of OSCP, as well as F0 components F6, B and D. In bacteria and chloroplasts the peripheral stalks have different subunit compositions delta and two copies of F0 component B bacteria , or delta and F0 components B and B chloroplasts ref name PUB00020607 cite journal author Walker JE, Runswick MJ, Neuhaus D, Montgomery MG, Carbajo RJ, Kellas FA title Structure of the F1 binding domain of the stator of bovine F1Fo ATPaseand how it binds an alpha subunit ... ref . Human delta subunit of ATPsynthase is coded by gene ATP5O . References reflist Further reading 1 . Structure and arrangement of the delta subunit in the E. coli ATPsynthase ECF1F0 . Wilkens ... IPR000711 DEFAULTSORT AtpSynthase Delta Subunit Category Protein domains Category Protein families ... more details
rotation in ATPsynthase journal FEBS Lett. volume 555 issue 1 pages 29 34 year 2003 pmid 14630314 doi ... reflist InterPro content DEFAULTSORT AtpSynthase Subunit C Category Protein domains Category Protein ...Pfam box Symbol ATP synt C Name image 2bl2.gif width 250 caption V type sodium ATPase from Enterococcus hirae . Calculated hydrocarbon boundaries of the lipid bilayer are shown by red and blue dots Pfam PF00137 InterPro IPR002379 SMART Prosite PDOC00526 SCOP 1aty TCDB OPM family 5 OPM protein 2bl2 PDB PDB3 2bl2 C 14 79 PDB3 1yce S 13 81 PDB3 1wu0 A 3 72 PDB3 1c17 D 8 77 PDB3 1j7f D 8 77 PDB3 1c99 A 8 77 PDB3 1a91 8 77 PDB3 1l6t A 8 77 PDB3 1c0v A 8 77 PDB3 1aty 9 77 PDB3 1ijp A 8 77 ATPase, subunit C of F0 V0 complex is the main transmembrane subunit of V type , A type and F type ATPsynthase s. ATPases or ATP synthases are membrane bound enzyme complexes ion transporters that combine ATP synthesis and or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can differ in function ATP synthesis and or hydrolysis , structure F , V and A ATPases contain rotary motors and in the type ... of A , F , and V type ATP synthases and ATPases reversals in function and changes in the H ATP ..., chloroplasts and bacterial plasma membranes are the prime producers of ATP, using the proton ... ATPase V1V0 ATPases are primarily found in eukaryotic vacuoles, catalysing ATP hydrolysis to transport ... surface enzymes that hydrolyse a range of NTPs, including extracellular ATP. The F ATPases or F1F0 ATPases ... contains the catalytic core that synthesizes hydrolyses ATP, and the F0 or V0 complex that forms the membrane ... across the membrane and one that drives ATP synthesis hydrolysis ref name PUB00009752 cite ... more details
Image PBB Protein ATP5B image.jpg thumb 250px left A part of F1 ATPsynthase complex alpha, beta and gamma subunits PDB 1bmf Pfam box Symbol ATP synt ab N Name ATPsynthase alpha beta family, beta barrel ... 63 129 PDB3 1e16 A 4 70 PDB3 1e1i A 4 70 PDB3 1v0i A 26 91 PDB3 2bn9 A 21 92 Pfam box Symbol ATP synt ab Name ATPsynthase alpha beta family, nucleotide binding domain image width caption Pfam PF00006 ... 364 Pfam box Symbol ATP synt ab C Name ATPsynthase alpha beta chain, C terminal domain image width ... 1e1i A 361 454 PDB3 1nvz A 362 466 ATPase s or ATPsynthase s are membrane bound enzyme complexes ion transporter s that combine Adenosine triphosphate ATP synthesis and or hydrolysis with the transport ... of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can differ in function ATP synthesis and or hydrolysis , structure ... PUB00020603 cite journal author Muller V, Cross RL title The evolution of A , F , and V type ATP synthases and ATPases reversals in function and changes in the H ATP coupling ratio journal FEBS Lett. volume ... plasma membranes are the prime producers of ATP, using the proton gradient generated by oxidative ... found in eukaryotic vacuoles, catalysing ATP hydrolysis to transport solutes and lower pH in organelles ... of nucleoside triphosphate s, including extracellular ATP. The alpha and beta or A and B subunits ... the catalytic core that synthesizes hydrolyses ATP, and the F0, V0 or A0 complex that forms the membrane ... across the membrane and one that drives ATP synthesis hydrolysis ref name PUB00009752 cite ... undergo a sequence of conformational changes leading to the formation of ATP from ADP, which are induced ... Understanding ATP synthesis structure and mechanism of the F1 ATPase Review journal Mol. Membr. Biol ... domain domains , centred around the ATP binding pocket, and based on structure and function ... more details
PBB geneid 498 ATPsynthase subunit alpha, mitochondrial is an enzyme that in humans is encoded by the ATP5A1 gene . ref name pmid1830491 cite journal author Kataoka H, Biswas C title Nucleotide sequence of a cDNA for the alpha subunit of human mitochondrial ATPsynthase journal Biochim Biophys Acta volume 1089 issue 3 pages 393 5 year 1991 month Sep pmid 1830491 pmc doi ref ref name entrez cite web title Entrez Gene ATP5A1 ATPsynthase, H transporting, mitochondrial F1 complex, alpha subunit 1, cardiac ... of mitochondrial ATPsynthase. Mitochondrial ATPsynthase catalyzes ATP synthesis, using an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATPsynthase ... spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATPsynthase ... and cell type specific expression of the human ATPsynthase alpha subunit. journal Biochim. Biophys ... required for the terminal steps of oxidative metabolism alpha and gamma subunits of ATPsynthase and the phosphate ... the alpha subunit of the mitochondrial ATPsynthase complex in a human retinoblastoma cell line ... analysis of Y79 and FISH mapping indicate the amplified human mitochondrial ATPsynthase alpha subunit ... G title Energy transduction in ATPsynthase. journal Nature volume 391 issue 6666 pages 510 3 year 1998 ... motor of ATPsynthase. journal Nature volume 396 issue 6708 pages 279 82 year 1998 pmid 9834036 ... ATPsynthase on the surface of human endothelial cells. journal Proc. Natl. Acad. Sci. U.S.A. volume ... author Moser TL, Kenan DJ, Ashley TA, et al. title Endothelial cell surface F1 F0 ATPsynthase is active in ATP synthesis and is inhibited by angiostatin. journal Proc. Natl. Acad. Sci. U.S.A. volume ... of the C terminal domain of p43 and the alpha subunit of ATPsynthase. Its functional implication ... M, et al. title Association of ATPsynthase alpha chain with neurofibrillary degeneration in Alzheimer ... doi 10.1038 ncb1086 cite journal author Cross RL title Molecular motors turning the ATP motor. journal ... more details
Refimprove date August 2007 In biochemistry , a synthase is an enzyme that catalyse s a Biosynthesis synthesis process. Following the Enzyme Commission number EC number classification, they belong to the group of ligase s, with lyase s catalysing the reverse reaction. Note that, originally, biochemical nomenclature distinguished synthetases and synthases. Under the original definition, synthases do not use energy from nucleoside triphosphates such as ATP, GTP, CTP, TTP, and UTP , whereas synthetases do use nucleoside triphosphates. However, the Joint Commission on Biochemical Nomenclature JCBN dictates that synthase can be used with any enzyme that catalyzes synthesis whether or not it uses nucleoside triphosphates , whereas synthetase is to be used synonymously with ligase . ref http www.chem.qmul.ac.uk iubmb newsletter misc synthase.html ref Examples ATPsynthase Citrate synthase Tryptophan synthase Pseudouridine synthase Fatty acid synthase Cellulose synthase UDP forming Cellulose synthase GDP forming References references Enzymes Category Lyases Enzyme stub de Synthasen fr Synthase lt Sintaz pl Syntazy sv Syntas zh ... 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 disambig bs ATP vor bg 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 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
protein Name Citrate synthase caption image width HGNCid 2422 Symbol CS AltSymbols EntrezGene 1431 OMIM ... The enzyme citrate synthase E.C. 2.3.3.1 previously 4.1.3.7 exists in nearly all living cells ... Weigand, Georg, and Steven J. Remington 1986 . Citrate Synthase Structure, Control, and Mechanism ...?cookieSet 1 ref Citrate synthase is localized within eukaryotic cells in the mitochondrial ... cytoplasmic ribosomes , then transported into the mitochondrial matrix. Citrate synthase is commonly used as a quantitative enzyme marker for the presence of intact mitochondria . Citrate synthase catalysis ... J. Remington 1986 . Citrate Synthase Structure, Control, and Mechanism. Ann. rev. Biophys. Biophys ... Synthase open form .png thumb 200px left The Active Site of Citrate Synthase open form Image Citrate synthase Closed form.png thumb 200px left The Active Site of Citrate Synthase closed form Citrate synthase s 437 amino acid residues are organized into two main subunits, each consisting of 20 alpha helices. These alpha helices compose approximately 75 of citrate synthase s tertiary structure , while ... acids of citrate synthase s active site in its open state the substrate is absent . ref PDB ID 1CSC ... display the tertiary structure of citrate synthase in its opened and closed form. The enzyme changes ... Changes of Citrate Synthase. Eur J Biochem. 120, 155 160 http www.blackwell synergy.com doi pdf 10.1111 j.1432 1033.1981.tb05683.x ref Mechanism Citrate Synthase has three key amino acids in its active ... and Co. Pages 608 609. ref Image Citrate Synthase Mechanism Drew Beck revised OH.png thumb 800px none Mechanism for Citrate Synthase including residues involved This http bcs.whfreeman.com lehninger ... synthase s mechanism from Lehninger s Principles of Biochemistry page. ref Lehninger 2005 . Principles ... by high ratios of adenosine triphosphate ATP Adenosine diphosphate ADP , acetyl CoA CoA, and NADH NAD , as high concentrations of ATP, acetyl CoA, and NADH show that the energy supply is high ... more details
and are not affected by the oligomeric state. The ATP binding site and CTP binding site in the synthase domain are located at the tetramer interface. It is for this reason that ATP and UTP are required ...enzyme Name CTP synthase EC number 6.3.4.2 CAS number 9023 56 7 IUBMB EC number 6 3 4 2 GO code 0003883 image CTP chemical structure.png width caption Cytidine triphosphate CTP synthase or CTP synthetase ... Enzyme Structure File CTP synthase dimer.jpg thumb 200px left upright alt Dimeric form of CTP synthase .... Active CTP synthase exists as a homeotetrameric enzyme. At low enzyme concentrations and in the absence of ATP and UTP, CTP synthase exists as inactive monomer. As enzyme concentration increases, it polymerizes first to a dimer such as the form shown to the left and, in the presence of ATP and UTP ... 6349684 ref The enzyme contains two major domains, responsible for the aminotransferase and synthase ... title Structure of the dimeric form of CTP synthase fromSulfolobus solfataricus year 2011 last1 Lauritsen ... pmc 3034608 ref Two isozymes with CTP synthase activity exist in humans, encoded by the following genes CTP synthase 1 CTPS CTP synthase 1 CTPS2 CTP synthase 2 Enzyme Mechanism CTP synthase catalyzes ... ATP UTP glutamine ADP Pi CTP glutamate It is the rate limiting enzyme for the synthesis of cytosine ... Adv Exp Med Biol volume 486 issue pmid 11783495 ref The reaction proceeds by the ATP dependent phosphorylation ... domain to produce ammonia. This is then channeled through the interior of the enzyme to the synthase ... Cytidine Triphosphate Synthetase, a Nucleotide Regulated Glutamine Amidotransferase ATP Dependent ... Biochemistry volume 28 issue 21 pmid 2532543 ref File Ctp synthase mechanism.jpg 500px center Regulation CTP synthase is precisely regulated by the intracellular concentrations of CTP and UPT, and both hCTPS1 and hCTPS2 have been seen to be maximally active at physiological concentrations of ATP ... synthase kinase 3 GSK3 in response to low serum conditions. ref name pmid17681942 cite journal pages ... more details
enzyme Name homoglutathione synthase EC number 6.3.2.23 CAS number 113875 72 2 IUBMB EC number 6 3 2 23 GO code 0047983 image width caption In enzymology , a homoglutathione synthase EC number 6.3.2.23 is an enzyme that catalysis catalyzes the chemical reaction ATP gamma L glutamyl L cysteine beta alanine math rightleftharpoons math ADP phosphate gamma L glutamyl L cysteinyl beta alanine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , gamma L glutamyl L cysteine , and beta alanine , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and gamma L glutamyl L cysteinyl beta alanine . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is gamma L glutamyl L cysteine beta alanine ligase ADP forming . Other names in common use include homoglutathione synthetase , and beta alanine specific hGSH synthetase . References reflist 1 cite journal author Macnicol PK date 1987 title Homoglutathione and glutathione synthetases of legume seedlings partial purification and substrate specificity journal Plant Sci. volume 53 pages 229&ndash 235 doi 10.1016 0168 9452 87 90159 2 issue 3 ligase stub Category EC 6.3.2 Category Enzymes of unknown structure ... more details
enzyme Name dethiobiotin synthase EC number 6.3.3.3 CAS number 37259 75 9 IUBMB EC number 6 3 3 3 GO code 0004141 image width caption In enzymology , a dethiobiotin synthase EC number 6.3.3.3 is an enzyme that catalysis catalyzes the chemical reaction ATP 7,8 diaminononanoate CO sub 2 sub math rightleftharpoons math ADP phosphate dethiobiotin The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 7,8 diaminononanoate , and carbon dioxide CO sub 2 sub , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and dethiobiotin . This enzyme belongs to the family of ligase s, specifically the cyclo ligases, which form carbon nitrogen bonds. The systematic name of this enzyme class is 7,8 diaminononanoate carbon dioxide cyclo ligase ADP forming . This enzyme is also called desthiobiotin synthase . This enzyme participates in biotin metabolism . Structural studies As of late 2007, 14 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1A82 , PDB link 1BS1 , PDB link 1BYI , PDB link 1DAD , PDB link 1DAE , PDB link 1DAF , PDB link 1DAG , PDB link 1DAH , PDB link 1DAI , PDB link 1DAK , PDB link 1DAM , PDB link 1DBS , PDB link 1DTS , and PDB link 2QMO . References reflist 1 cite journal author Krell K, Eisenberg MA date 1970 title The purification and properties of dethiobiotin synthetase journal J. Biol. Chem. volume 245 pages 6558&ndash 66 pmid 4921568 issue 24 cite journal author Yang H C, Tani Y and Ogata K date 1970 title Synthesis of biotin vitamers from biotin diaminocarboxylic acid or 7,8 diaminopelargonic acid by a purified enzyme of Pseudomonas graveolens journal Agric. Biol. Chem. volume 34 pages 1748&ndash 1750 doi 10.1271 bbb1961.34.1748 issue 11 ligase stub Category EC 6.3.3 Category Enzymes of known structure ... more details
enzyme Name NAD sup sup synthase EC number 6.3.1.5 CAS number 9032 69 3 IUBMB EC number 6 3 1 5 GO code 0008795 image width caption orphan date October 2009 In enzymology , a NAD sup sup synthase EC number 6.3.1.5 is an enzyme that catalysis catalyzes the chemical reaction ATP deamido NAD sup sup NH sub 3 sub math rightleftharpoons math AMP diphosphate NAD sup sup The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , deamido NAD deamido NAD sup sup , and ammonia NH sub 3 sub , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and nicotinamide adenine dinucleotide NAD sup sup . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D ammonia or amine ligases amide synthases . The systematic name of this enzyme class is deamido NAD sup sup ammonia ligase AMP forming . Other names in common use include NAD sup sup synthetase , NAD sup sup synthase , nicotinamide adenine dinucleotide synthetase , and diphosphopyridine nucleotide synthetase . This enzyme participates in nicotinate and nicotinamide metabolism and nitrogen metabolism . 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 1WXE , PDB link 1WXF , PDB link 1WXG , PDB link 1WXH , PDB link 1WXI , PDB link 1XNG , PDB link 1XNH , PDB link 2E18 , PDB link 2PZ8 , PDB link 2PZA , and PDB link 2PZB . References reflist 1 cite journal author Spencer RL, Preiss J date 1967 title Biosynthesis of diphosphopyridine nucleotide. The purification and the properties of diphospyridine nucleotide synthetase from Escherichia coli b journal J. Biol. Chem. volume 242 pages 385&ndash 92 pmid 4290215 issue 3 ligase stub Category EC 6.3.1 Category NADH dependent enzymes Category Enzymes of known structure ... more details
enzyme Name 1 aminocyclopropane 1 carboxylate synthase EC number 4.4.1.14 CAS number 72506 68 4 IUBMB ... Structure of ACC Synthase File ACCsynthasecomplexwPLP.png thumb 300px ACC Synthase Complex with PLP File ACS & PLP complex with labeled 278 and 152 residues.png thumb 300px ACC Synthase Complex with PLP Catalytic Domain Aminocyclopropane 1 carboxylic acid synthase ACC synthase, ACS EC 4.4.1.14 is an enzyme ... methyl cycle and a useful molecule for methyl transfer. ACC synthase, like other PLP dependent enzymes ... of 1 aminocyclopropane 1 carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ..., Li N, Ke H title Crystal structures of 1 aminocyclopropane 1 carboxylate ACC synthase in complex with aminoethoxyvinylglycine ... jbc.M103840200 url ref In enzymology , a 1 aminocyclopropane 1 carboxylate synthase EC number ... use include 1 aminocyclopropanecarboxylate synthase , 1 aminocyclopropane 1 carboxylic acid synthase , 1 aminocyclopropane 1 carboxylate synthetase , aminocyclopropanecarboxylic acid synthase , aminocyclopropanecarboxylate synthase , ACC synthase , and S adenosyl L methionine methylthioadenosine lyase ... catalyzed by 1 aminocyclopropane 1 carboxylic acid synthase ACS is the committed and rate limiting step ... of 1 aminocyclopropane 1 carboxylate synthase journal J. Exp. Bot. volume 56 issue 418 pages 2203 ... G, McCarthy DL, Gut H, Gr tter MG, Kirsch JF title Apple 1 aminocyclopropane 1 carboxylate synthase ... favorable and prevent the ACC synthase catalyzed reaction with SAM. ref cite journal author Huai Q, Xia ... ACC synthase in complex with aminoethoxyvinylglycine and pyridoxal 5 phosphate provide new insight into catalytic ... from the methionine at the expense of one molecule of ATP per molecule of S AdoMet synthesized. S AdoMet ... limiting step of ethylene synthesis is the conversion of S AdoMet to ACC by ACC synthase un der most conditions. MTA is the by product generated along with ACC production by ACC synthase. Recycling ... regulation of both ACC synthase and ACC oxidase is indicated by dashed arrows. Reversible ... more details
enzyme Name tetrahydrofolylpolyglutamate synthase EC number 6.3.2.17 CAS number 63363 84 8 IUBMB EC number 6 3 2 17 GO code 0004326 image width caption In enzymology , a tetrahydrofolate synthase EC number 6.3.2.17 is an enzyme that catalysis catalyzes the chemical reaction ATP tetrahydropteroyl gamma Glu n L glutamate math rightleftharpoons math ADP phosphate tetrahydropteroyl gamma Glu n sup sup 1 The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , tetrahydropteroyl gamma Glu n , and L glutamate , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and tetrahydropteroyl gamma Glu n 1 . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is tetrahydropteroyl gamma polyglutamate L glutamate gamma ligase ADP forming . Other names in common use include folylpolyglutamate synthase , folate polyglutamate synthetase , formyltetrahydropteroyldiglutamate synthetase , N10 formyltetrahydropteroyldiglutamate synthetase , folylpoly gamma glutamate synthase , folylpolyglutamyl synthetase , folylpoly gamma glutamate synthase , folylpolyglutamate synthetase , folylpoly gamma glutamate synthetase dihydrofolate synthetase , FPGS , tetrahydrofolylpolyglutamate synthase , tetrahydrofolate L glutamate gamma ligase ADP forming , tetrahydropteroyl gamma Glu n L glutamate gamma ligase , and ADP forming . This enzyme participates in folate biosynthesis . Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1FGS , PDB link 1JBV , PDB link 1JBW , PDB link 2GC5 , PDB link 2GC6 , PDB link 2GCA , and PDB link 2GCB . References reflist 1 cite journal author Cichowicz DJ, Foo SK, Shane B date 1981 title Folylpoly gamma glutamate synthesis by bacteria and mammalian cells journal Mol. Cell ... more details
enzyme Name carnosine synthase EC number 6.3.2.11 CAS number 9023 61 4 IUBMB EC number 6 3 2 11 GO code 0047730 image width caption In enzymology , a carnosine synthase EC number 6.3.2.11 is an enzyme that catalysis catalyzes the chemical reaction ATP L histidine beta alanine math rightleftharpoons math AMP diphosphate carnosine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L histidine , and beta alanine , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and carnosine . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is L histidine beta alanine ligase AMP forming . Other names in common use include carnosine synthetase , carnosine anserine synthetase , homocarnosine carnosine synthetase , and carnosine homocarnosine synthetase . This enzyme participates in 4 metabolism metabolic pathways urea cycle and metabolism of amino groups , alanine and aspartate metabolism , histidine metabolism , and beta alanine metabolism . References reflist 1 cite journal author KALYANKAR GD, MEISTER A date 1959 title Enzymatic synthesis of carnosine and related beta alanyl and gamma aminobutyryl peptides journal J. Biol. Chem. volume 234 pages 3210&ndash 8 pmid 14404206 cite journal author Stenesh JJ and Winnick T date 1960 title Carnosine anserine synthetase of muscle. 4. Partial purification of the enzyme and further studies of alanyl peptide synthesis journal Biochem. J. volume 77 pages 575&ndash 581 pmid 16748858 issue 3 pmc 1205078 ligase stub Category EC 6.3.2 Category Enzymes of unknown structure ... more details
enzyme Name glutathione synthase EC number 6.3.2.3 CAS number 9023 62 5 IUBMB EC number 6 3 2 3 GO code 0004363 image width caption In enzymology , a glutathione synthase EC number 6.3.2.3 is an enzyme that catalysis catalyzes the chemical reaction ATP gamma L glutamyl L cysteine glycine math rightleftharpoons math ADP phosphate glutathione The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , gamma L glutamyl L cysteine , and glycine , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and glutathione . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is gamma L glutamyl L cysteine glycine ligase ADP forming . Other names in common use include glutathione synthetase , and GSH synthetase . This enzyme participates in glutamate metabolism and glutathione metabolism . At least one compound, Phosphinate is known to enzyme inhibitor inhibit this enzyme . Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1GLV , PDB link 1GSA , PDB link 1GSH , PDB link 1M0T , PDB link 1M0W , PDB link 2GLT , and PDB link 2HGS . References reflist 1 cite journal author Law MY and Halliwell B date 1986 title Purification and properties of glutathione synthetase from Spinacia oleracea leaves journal Plant Sci. volume 43 pages 185&ndash 191 doi 10.1016 0168 9452 86 90016 6 issue 3 cite journal author Macnicol PK date 1987 title Homoglutathione and glutathione synthetases of legume seedlings partial purification and substrate specificity journal Plant Sci. volume 53 pages 229&ndash 235 doi 10.1016 0168 9452 87 90159 2 issue 3 ligase stub Category EC 6.3.2 Category Enzymes of known structure ... more details
enzyme Name glutathionylspermidine synthase EC number 6.3.1.8 CAS number 9077 09 2 IUBMB EC number 6 3 1 8 GO code 0008885 image width caption In enzymology , a glutathionylspermidine synthase EC number 6.3.1.8 is an enzyme that catalysis catalyzes the chemical reaction glutathione spermidine ATP math rightleftharpoons math glutathionylspermidine ADP phosphate The 3 substrate biochemistry substrates of this enzyme are glutathione , spermidine , and adenosine triphosphate ATP , whereas its 3 product chemistry products are glutathionylspermidine , adenosine diphosphate ADP , and phosphate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D ammonia or amine ligases amide synthases . The systematic name of this enzyme class is gamma L glutamyl L cysteinyl glycine spermidine ligase ADP forming spermidine is numbered so that atom N 1 is in the amino group of the aminopropyl part of the molecule . This enzyme is also called glutathione spermidine ligase ADP forming . This enzyme participates in glutathione metabolism . It employs one cofactor biochemistry cofactor , magnesium . 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 2IO7 , PDB link 2IO8 , PDB link 2IO9 , PDB link 2IOA , and PDB link 2IOB . References reflist 1 cite journal author Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH year 1992 title Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata journal Protein. Sci. volume 1 pages 874&ndash 83 pmid 1304372 doi 10.1002 pro.5560010705 issue 7 pmc 2142158 cite journal author Bollinger JM Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT year 1995 title Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase amidase journal J. Biol. Chem. volume 270 pages ... more details
Spermine synthase is an enzyme that converts spermidine into spermine . External links MeshName Spermine synthase EC number 2.5.1.22 Gene SMS Alkyl and aryl transferases Category Enzymes Biochem stub ... more details
enzyme Name dihydrofolate synthase EC number 6.3.2.12 CAS number 37318 62 0 IUBMB EC number 6 3 2 12 GO code 0008841 image width caption In enzymology , a dihydrofolate synthase EC number 6.3.2.12 is an enzyme that catalysis catalyzes the chemical reaction ATP 7,8 dihydropteroate L glutamate math rightleftharpoons math ADP phosphate 7,8 dihydropteroylglutamate The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 7,8 dihydropteroate , and L glutamate , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and 7,8 dihydropteroylglutamate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is 7,8 dihydropteroate L glutamate ligase ADP forming . Other names in common use include dihydrofolate synthetase , 7,8 dihydrofolate synthetase , H2 folate synthetase , 7,8 dihydropteroate L glutamate ligase ADP , dihydrofolate synthetase folylpolyglutamate synthetase , folylpoly gamma glutamate synthetase dihydrofolate synthase , FHFS , FHFS FPGS , dihydropteroate L glutamate ligase ADP forming , and DHFS . This enzyme participates in folate biosynthesis . 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 1W78 , PDB link 1W7K , and PDB link 2BMB . References reflist 1 cite journal author GRIFFIN MJ, BROWN GM date 1964 title THE BIOSYNTHESIS OF FOLIC ACID. III. ENZYMATIC FORMATION OF DIHYDROFOLIC ACID FROM DIHYDROPTEROIC ACID AND OF TETRAHYDROPTEROYLPOLYGLUTAMIC ACID COMPOUNDS FROM TETRAHYDROFOLIC ACID journal J. Biol. Chem. volume 239 pages 310&ndash 6 pmid 14114858 cite journal author Bognar AL, Osborne C, Shane B, Singer SC, Ferone R date 1985 title Folylpoly gamma glutamate synthetase dihydrofolate synthetase Cloning and high expression of the Escherichia coli folC gene ... more details
The main function of trypanothione synthase is to use the free energy generated from ATP hydrolysis ...enzyme Name trypanothione synthase EC number 6.3.1.9 CAS number 130246 69 4 IUBMB EC number 6 3 1 9 GO code 0047479 image Trypanothione Synthase.jpg width caption In enzymology , a trypanothione synthase EC number 6.3.1.9 is an enzyme that catalysis catalyzes the chemical reaction glutathione glutathionylspermidine ATP math rightleftharpoons math N sub 1 sub ,N sub 8 sub bis glutathionyl spermidine ADP phosphate The 3 substrate biochemistry substrates of this enzyme are glutathione , glutathionylspermidine , and adenosine triphosphate ATP , whereas its 3 product chemistry products are N1,N8 bis ... synthase is found as a 74.4 KDa monomer consisting of 652 residues with two catalytic domains. ref name Fyfe ref name Oza3 Its C terminal domain is a synthetase and has an ATP grasp family ... into the structure of trypanothione synthase must be done in order to fully understand the enzyme ... reactions, trypanothione synthase from trypanosoma cruzi was found to have an amidase activity that was only ... fold. In parasitic kinetoplastids trypanothione synthase activity is key to survival. Due to the need ... metabolism. It was observed that induced knockout of trypanothione synthase through RNA ... cell death after knocking out trypanothione synthase, it was shown that after two hours of being ... did not contain working trypanothione synthase had a much higher death rate than wild type T. brucei ... and Mg sup 2 sup ATP bind to the enzyme in a ternary complex where glutathione becomes activated by ATP and forms glutathionyl phosphate. ref name Comini2 ADP then leaves the active site and the activated ... with glutathionylspermidine to form trypanothione. Regulation The regulation of trypanothione synthase ... allow the synthase domain to block the amidase active site are highly conserved among different species ... synthase could be a novel way of preventing and curing these diseases through disruption of the parasites ... more details
Phytoene synthase is a transferase enzyme involved in the biosynthesis of carotenoid s. It catalyzes the conversion of geranylgeranyl pyrophosphate to phytoene . ref http www.curehunter.com public keywordSummaryC073128 phytoene synthase.do Phytoene synthase ref References reflist Category EC 2.5.1 transferase stub ... more details
enzyme Name aerobactin synthase EC number 6.3.2.27 CAS number 94047 30 0 IUBMB EC number 6 3 2 27 GO code 0050565 image width caption In enzymology , an aerobactin synthase EC number 6.3.2.27 is an enzyme that catalysis catalyzes the chemical reaction 4 ATP citrate 2 N sub 6 sub acetyl N sub 6 sub hydroxy L lysine 2 H sub 2 sub O math rightleftharpoons math 4 ADP 4 phosphate aerobactin The 4 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , citrate , N6 acetyl N6 hydroxy L lysine , and water H sub 2 sub O , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and aerobactin . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is citrate N6 acetyl N6 hydroxy L lysine ligase ADP forming . This enzyme is also called citrate 6 N acetyl 6 N hydroxy L lysine ligase ADP forming . This enzyme participates in lysine degradation . References reflist 1 cite journal author Appanna DL, Grundy BJ, Szczepan EW and Viswanatha T date 1984 title Aerobactin synthesis in a cell free system of Aerobacter aerogenes 62 1 journal Biochim. Biophys. Acta volume 801 pages 437&ndash 443 cite journal author Gibson F, Magrath DI date 1969 title The isolation and characterization of a hydroxamic acid aerobactin formed by Aerobacter aerogenes 62 I journal Biochim. Biophys. Acta. volume 192 pages 175&ndash 84 pmid 4313071 issue 2 cite journal author Maurer PJ and Miller M date 1982 title Microbial iron chelators total synthesis of aerobactin and its constituent amino acid, N6 acetyl N6 hydroxylysine journal J. Am. Chem. Soc. volume 104 pages 3096&ndash 3101 doi 10.1021 ja00375a025 issue 11 cite journal author de Lorenzo V, Bindereif A, Paw BH, Neilands JB date 1986 title Aerobactin biosynthesis and transport genes of plasmid ColV K30 in Escherichia coli K 12 journal J. Bacteriol. volume 165 pages 570&ndash ... more details
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