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Topic: ATP synthetase

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	Electron Storage
		ATP is made of adenosine and ribose bonded to three phosphate groups through phosphate ester bonds.
		ATP synthetase converts the free energy of the proton gradient to chemical energy in the form of ATP.
		ATP synthetase (multicolors) has two components: a proton channel (magenta) which allows diffusion of protons down a concentration gradient, from the intermembrane space, and a catalytic component (F1) to catalyze the formation of ATP in six alpha beta subunits (multicolors) in graphic on the left.
	www.elmhurst.edu /~chm/vchembook/593energystore.html (760 words)

	ELECTRON TRANSPORT (Site not responding. Last check: 2007-11-01)
		The ATP synthetase (ATP synthase, H+ ATPase) is a large, lollipop shaped protein-enzyme -carrier that is situated in the inner membrane of mitochondria (also in prokaryotic cell membranes and chloroplast inner membranes).
		The theory is consistent with the fact that ATP synthetase molecules always seem to be oriented in one direction in electron micrographs.
		ATP synthetase plus an artificial charge and H+ gradient plus ADP and phosphate can be used to make ATP (this is not a straight forward experiment because of the difficulty in inducing such gradients).
	www.mrs.umn.edu /~goochv/CellBio/lectures/et/et.html (963 words)

	ATPase Information Center - calcium atpase
		ATPases are a class of enzymes that atpase inhibitor catalyze the decomposition of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and na k atpase function a free phosphate ion.
		Transmembrane ATPases harness the chemical potential energy of ATP, because they perform mechanical work: they transport solutes in a direction opposite to their thermodynamically preferred direction of movement—that is, from the side of the membrane where they are in low concentration to chloroplast atpase the side where they are atpase immobilization in high concentration.
		ATP synthetase can also function atpase controls production of atp in cell cytosol in reverse; that is, use energy released by ATP hydrolysis to pump protons against their thermodynamic gradient.
	www.scipeeps.com /Sci-Biochemistry_Topics_A/ATPase.html (416 words)

	Function of Conserved Residues of Human Glutathione Synthetase: IMPLICATIONS FOR THE ATP-grasp ENZYMES -- Dinescu et ...
		Glutathione synthetase is an enzyme that belongs to the glutathione
		of glutathione synthetase deficiency is caused by mutations
		and pyruvate phosphate dikinase) from the glutathione synthetase
	www.jbc.org /cgi/content/full/279/21/22412 (4502 words)

	Chemical Compound Outline (Part I)
		The emission of light by an organism or population of organisms involves the oxidation of luciferin in the presence of ATP and the enzyme luciferase.
		ATP is synthesized in all living cells by the addition of a phosphate to ADP (adenosine diphosphate).
		Most of the ATP in eukaryotic cells of animals is made inside cellular organelles called mitochondria from the oxidation of glucose, a process called cellular respiration.
	waynesword.palomar.edu /chemid1.htm (15712 words)

	ATPase - EvoWiki (Site not responding. Last check: 2007-11-01)
		An ATPase is an enzyme that breaks down ATP (adenosine triphosphate) into ADP (adenosine diphosphate) plus a phosphate ion.
		ATP is a major, but not the only, energy currency in a cell.
		A particularly important ATPase is the bacterial F1F0 ATP synthetase, also known as the F1F0-ATP synthase or F1F0-ATPase.
	wiki.cotch.net /index.php?title=ATPase&redirect=no (147 words)

	Evolving the Bacterial Flagellum Through Mutation and Cooption: Part VI
		When Matzke proposes that the F0F1 ATP synthetase was coopted “in toto into a primitive gated pore,” it is not clear whether he envisions that the split into alpha and beta subunits has already occurred.
		In the ATP synthetase, the N-terminal region of delta interacts with the N-terminal region of alpha and the C-terminal region of delta interacts with the C terminal region of F0b.
		The a subunit of the ATP synthetase (F0a) is an integral membrane protein that works in conjunction with the c subunit.
	www.idthink.net /biot/flag6/index.html (13395 words)

	Bioenergetics
		This step is energetically possible because the free energy released by tightly binding the ATP to the active centre compensates for the instability of the new phospho anhydride bond.
		Energy is transmitted to the catalytic subunits in the ATP synthase F1 headpiece by the rotation of the camshaft.
		Normally the energy from the proton gradient is used to manufacture ATP, but it is equally possible in vitro to do things the other way round, and use the hydrolysis of ATP to drive the camshaft, and ultimately pump protons back through the turbine and into the extramitochondrial compartment.
	www.bmb.leeds.ac.uk /illingworth/oxphos/atpase.htm (770 words)

	Aspartyl-tRNA Synthetase-tRNA-ATP Complex (Site not responding. Last check: 2007-11-01)
		The ATP adopts a bent conformation which is stabilized by the conserved arg531 of motif 3 and a magnesium ion which is coordinated to the pyrophosphate group and to two class II conserved acidic residues.
		The anti parallel beta sheet surface in contacting the ATP is characterised by the large number of gly residues present (positions 340, 482, 524, 526 and 528).
		The adenine base of ATP is firmly held by pi-electron interactions with phe338 on one side and arg531 on the other.
	www-ccmr-nmr.bioc.cam.ac.uk /~mlm23/asprs.html (1350 words)

	Self Instructional on Glycolysis and Respiration
		ATP is an abbreviation for the nucleotide Adenosine triphosphate.
		The energy released by the conversion of ATP to ADP is used in the manufacture of ATP during the process of glycolysis.
		The ATP synthetase gets the energy necessary for the formation of the high energy phosphate bond from the rush of protons through the channel it creates across the mitochondrial membrane.
	homepages.ius.edu /GKIRCHNE/Glycolysis.htm (3616 words)

	XXIII
		H+ pass from thylakoid space through ATP Synthetase into the stroma and synthetase using potential energy to produce ATP.
		ATP and NADPH produced by light reactions are used to fix and reduce CO2 in production of carbohydrate.
		Through a sequence of reactions, 6 molecules of 3-P-Glycerate (produced from 3 molecules of Ribulose Diphosphate and 3 CO) are reduced and rearranged at the expense of 9 ATP and 6 NADPH to produce 1 molecule of glyceraldehyde-3-Phos.
	www.sci.sdsu.edu /classes/biology/bio202/TFrey/Photosynthesis.html (810 words)

	Partial purification and characterization of a non-cyanobacterial cyanophycin synthetase from Acinetobacter ...
		Staining was done with Serva Blue R. Purification of cyanophycin synthetase, assay of cyanophycin synthetase activity and determination of protein concentration.
		Dependency on pH of cyanophycin synthetase activity and of binding of the enzyme to cyanophycin.
		Krehenbrink, M., Oppermann-Sanio, F. and Steinbüchel, A. Evaluation of non-cyanobacterial genome sequences for occurrence of genes encoding proteins homologous to cyanophycin synthetase and cloning of an active cyanophycin synthetase from Acinetobacter sp.
	mic.sgmjournals.org /cgi/content/full/150/8/2599 (4657 words)

	S-Adenosylmethionine Synthetase Is Overexpressed in Murine Neuroblastoma Cells Resistant to Nucleoside Analogue ...
		S-Adenosylmethionine Synthetase Is Overexpressed in Murine Neuroblastoma Cells Resistant to Nucleoside Analogue Inhibitors of S-Adenosylhomocysteine Hydrolase: A Novel Mechanism of Drug Resistance -- Dwivedi et al.
		A significant increase in the expression of the catalytic subunit
		Expression of AdoMet synthetase subunits in wild-type (wMNB) and nucleotide analogue-resistant murine neuroblastoma (rMNB-MDL) cells.
	cancerres.aacrjournals.org /cgi/content/full/59/8/1852 (3211 words)

	Microbial metabolism
		The ETS and ATP synthetase occur on the inner mitochondrial membrane of eukaryotes and on the plasma membrane of prokaryotes.
		As two phosphorylated 3-carbon molecules are formed from each molecule of glucose 4 molecules of ATP are actually formed at this point.
		ATP synthetase, associated with the channels, phosphorylates ADP to ATP.
	www.ccsf.edu /Departments/Biology/ctoebe/metab.htm (1775 words)

	CiteULike: Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine ... (Site not responding. Last check: 2007-11-01)
		Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution.
		The crystal structures showed that the ATP molecules were hydrolyzed to ADP and Pi by the enzyme.
		The enzyme hydrolyzed ATP to ADP and Pi in 72 h under the same conditions as the crystallization of the enzyme.
	www.citeulike.org /user/swm26/article/274070 (761 words)

	text
		The mechanism of this reaction, the ATP synthetase, has only become clearer in the last few years, and is still not completely understood.
		This distortion forces the ADP and Pi together on one propeller blade, while the ATP that just had been formed on another propeller blade is distorted in the opposite way to release the ATP.
		And so there are two methods of producing ATP from glucose metabolism: Oxidative phosphorylation and the "regular", direct phosphorylation of ADP from phosphorylated intermediates that was seen during glycolysis, or in the GTP-forming step in the Krebs Cycle.
	www.columbia.edu /itc/biology/chasin/lecture9/lec9_00.htm (3737 words)

	Altered Pathway Routing in a Class of Salmonella enterica Serovar Typhimurium Mutants Defective in Aminoimidazole ...
		AIR synthetase activity was assayed by detecting formation of AIR using a previously described modification of the Bratton-Marshall
		The groove, which runs into the plane of the page, is bracketed by the ATP-binding loop (labeled ATP, at the front), initially identified by crystallography and affinity labeling (27), and an inorganic sulfate (at the back), proposed to locate the binding site for FGAM (21).
		Isolation of a multifunctional protein with aminoimidazole ribonucleotide synthetase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase activities: characterization of aminoimidazole ribonucleotide synthetase.
	jb.asm.org /cgi/content/full/183/7/2234 (4400 words)

	The Biochemistry Book - Mitochondria
		They have a major advantage in that the ATP synthetase and the ATPase are on the outside of the membrane, there is therefore no barrier to substrate or other interacting molecules.
		The synthesis (hydrolysis) of AP occurs on the side of the membrane with knobs; the complex which performs this (ATP Synthase Complex) consits of at least 9 Different Polypeptides.
		Photoafinity Analogues of ATP (bind covalently on U.V. irradiation), associated mainly with the ß subunit.
	members.tripod.com /~Kato_2/mitochon.htm (423 words)

	Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase -- Girard et al. 12 (7): 603 ...
		ATP to APS to yield PAPS (adenosine 3'-phosphate 5'-phosphosulfate),
		The amino-terminal part of human PAPS synthetase is homologous to APS kinases from bacteria, yeast, and plants, whereas the carboxy-terminal part is very similar to ATP sulfurylases from yeast, fungi, and plants.
		Hu: human PAPS synthetase (aa 241–624); At1, At2, and At3: Arabidopsis thaliana ATP sulfurylases 1 (aa 65–463; GenBank N°U05218), 2 (aa 79–476; GenBank N°U06276), and 3 (aa 67–465; GenBank N°U06275); St1 and St2: Solanum tuberosum ATP sulfurylases 1 (aa 26–424; GenBank N°X75041) and 2 (aa 65–463; GenBank N°X79053).
	www.fasebj.org /cgi/content/full/12/7/603 (5652 words)

	Photosynthesis, Respiration, and the ATP-ADP Cycle
		ATP consists of three parts, adenine, ribose, and (3) phosphate groups.
		In the energy production cycle in the chloroplasts and mitochondria, energy is stored when ATP is produced from ADP and a phosphate group "P".
		The process (the game of catch) will be repeated until the students have clearly demonstrated their knowledge of the phosphate loss, phosphate gain process.
	www.iit.edu /~smile/bi9614.html (705 words)

	Dudy Bar Zvi's publications
		Role of tight nucleotide binding in the regulation of the chloroplast ATP synthetase activities.
		Role of tightly bound ADP in the regulation of the chloroplast ATP synthetase activities.
		Differential inhibition of the Pi-ATP exchange in relation to ATP synthesis and hydrolysis by modification of chloroplast thylakoid membranes with glutaraldehyde.
	www.bgu.ac.il /life/Faculty/Bar_zvi/publications.html (746 words)

	Untitled Document (Site not responding. Last check: 2007-11-01)
		The formation of ATP by condensation between ADP and inorganic phosphate is a highly endothermic reaction.
		The ATP synthetase is located in the primary particles on the inner face of the crista membrane; isolated primary particles catalyse hydrolysis of ATP to ADP and phosphate, and you will sometimes see ATP synthetase referred to as an ATPase.
		If there is no ADP available to bind to the empty site, then rotation of the central part of the ATP synthetase is not possible, and protons cannot cross the stalk of the primary particle.
	www.ucl.ac.uk /~ucbcdab/oxphos/ATPsynth.htm (229 words)

	The General Considerations Regarding Cellular Energy Metabolism Page
		ATP and GTP are both molecules with a string or 3 phosphate groups stuck on them.
		For this reason, we call the third phosphate bond a "high energy phosphate bond." A lot of energy is released from ATP and GTP when the high energy bond holding the third phosphate in place is broken.
		Notice that in glycolysis, there is a net gain of 2 ATP from the breakdown of 1 glucose molecule.
	faculty.etsu.edu /currie/metabolism.htm (1693 words)

	Cloning and Functional Characterization of Human Selenophosphate Synthetase, an Essential Component of Selenoprotein ...
		Comparison of the human and bacterial selenophosphate synthetase peptide sequences reveals a high homology glycine-rich sequence that is similar to conserved sequences found in many ATP/GTP binding proteins and protein kinases(25, 26, 27, 28).
		Following ATP binding to selenophosphate synthetase, ATP is hydrolyzed to produce AMP and a pyrophosphate-enzyme intermediate(9, 10).
		Arg also bind more ATP for a longer period of time than wild-type selD (Table 1, and data not shown) suggesting that glycine residues at position 269 and 271 may be involved in ATP hydrolysis (Table 1).
	www.jbc.org /cgi/content/full/270/37/21659 (5151 words)

	Biology 101 Lecture notes, 2 February, 1998
		The mechanism can be likened to a water wheel, where the flow of protons resembles a flow of water downhill, and the turning of the wheel is the turning of ADP toward phosphate to cause the bond to form.
		ADP, by binding to ATP synthetase, provides an outlet for the protons that have accumulated in the intermembrane space.
		By binding to ATP synthetase, ADP permits protons to enter the matrix through a special channel, using the released energy to create a covalent bond between ADP and phosphate.
	www.cbs.dtu.dk /staff/dave/roanoke/bio101ch08.htm (763 words)

	Department of Chemistry and Biochemistry - Chem*4520 Metabolic Processes
		Carbamoyl phosphate synthetase I exists in the mitochondrion, and uses NH directly to produce carbamoyl phosphate for the urea cycle.
		Carbamoyl phosphate synthetase II acts in the cytoplasm, and uses glutamine as the N donor to produce carbamoyl phosphate for pyrimidine synthesis.
		This means that carbamate never enters the surrounding medium, and is presented to the ATP at site 3 at a high effective concentration.
	www.chembio.uoguelph.ca /educmat/chm452/lectur30.htm (564 words)

	The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and ...
		The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid
		In addition, a structure of the complex of asparaginyl-tRNA synthetase with ATP shows exactly the same configuration of three divalent cations as previously observed in the seryl-tRNA synthetase−ATP complex, showing that this a general feature of class II synthetases.
		The structural similarity of asparaginyl- and aspartyl-tRNA synthetases as well as that of both enzymes to the ammonia-dependent asparagine synthetase suggests that these three enzymes have evolved relatively recently from a common ancestor.
	www.nature.com /emboj/journal/v17/n10/abs/7591002a.html (308 words)

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