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Topic: Apoenzyme

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Holoenzyme

Cofactor

Enzyme

Catalyst

Polymer

Polymerization

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	Homogeneous specific binding assay with carrier matrix incorporating specific binding partner - Patent 4447526
		Another scheme for determining a ligand is presented where the labeled conjugate is composed of a labeled binding partner of the ligand and upon binding to the ligand the label is affected in terms of its detectable response.
		In the present system, the label is flavin adenine dinucleotide (FAD), the prosthetic group of glucose oxidase, and the ability of the catalytically inactive apoenzyme to combine with its prosthetic group label to form active glucose oxidase is affected by binding of the labeled conjugate with its binding partner.
		Upon activation of the apoenzyme to glucose oxidase, a blue color formed due to the oxidation of glucose to hydrogen peroxide and subsequent conversion of TMB to its blue oxidized state in the presence of peroxidase.
	www.freepatentsonline.com /4447526.html (5861 words)

	tiredness article by James South
		The apoenzyme is a specific protein, with a unique shape and composition that enables it to process a specific biochemical in a specific way.
		The coenzyme is the "activator" of the apoenzyme.
		This is hardly surprising, given the key roles of coenzyme B1 in the glycolytic and Kreb's cycles and a demonstrable failure of an apoenzyme - transketolase - to be fully saturated with - i.e.
	www.smartnutrition.info /JamesSouth-tired.htm (5520 words)

	Enzymes (Site not responding. Last check: 2007-10-11)
		Apoenzyme: The polypeptide or protein part of the enzyme is called the apoenzyme and may be inactive in its original synthesized structure.
		The inactive form of the apoenzyme is known as a proenzyme or zymogen.
		The proenzyme may contain several extra amino acids in the protein which are removed, and allows the final specific tertiary structure to be formed before it is activated as an apoenzyme.
	www.elmhurst.edu /~chm/vchembook/570enzymes.html (646 words)

	Biotechterms.org
		This other piece is known as a cofactor and it may be removed from the enzyme under certain conditions.
		When this is done, the resulting inactive enzyme is known as an apoenzyme.
		The inactive apoenzyme becomes functionally active again if it is allowed to recombine with its cofactor.
	biotechterms.org /sourcebook/saveidretrieve.php3?id=132 (97 words)

	abstract54 (Site not responding. Last check: 2007-10-11)
		Reconstitution of the quinoprotein glucose dehydrogenase from its apoenzyme on
		The electrode modified with the long spacered PQQ was used as a support for the immobilization of glucose dehydrogenase (GDH) apoenzyme having affinity for PQQ which is its native cofactor.
		Therefore, although the enzymatic activity was reconstituted by the interaction of the apoenzyme binding site with the long spacered PQQ immobilized as a monolayer on the electrode surface, there was no direct electron transfer between the electrode surface and the PQQ redox site inside the holoenzyme.
	chem.ch.huji.ac.il /~eugeniik/abstract54.htm (248 words)

	Laboratory of Biomolecular Systems
		Comparison of the PNP apoenzyme with bovine PNP (BtPNP) complexed with immucillin-H also shows the gate movement and the helical transition in the same region.
		The purine interactions with PNP are mostly of hydrophobic nature with residues that are conserved throughout the PNP family, nevertheless several hydrogen bonds, between PNP and guanine are observed.
		The binding pocket for the purine in the apoenzyme shows two well-defined water molecules whose density of one water molecule overlaps with the purine ring in the superimposed guanine complex.
	www.biocristalografia.df.ibilce.unesp.br /pnp/pnp.php (2943 words)

	Enzymes and Life Processes
		This entire active complex is referred to as the holoenzyme; i.e., apoenzyme (protein portion) plus the cofactor (coenzyme, prosthetic group or metal-ion-activator) is called the holoenzyme.
		A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion.
		For example, nicotinamide adenine dinucleotide (NAD) is a coenzyme for a great number of dehydrogenase reactions in which it acts as a hydrogen acceptor.
	www.worthington-biochem.com /introBiochem/lifeProcesses.html (849 words)

	Reconstitution of Membrane-Integrated Quinoprotein Glucose Dehydrogenase Apoenzyme with PQQ and the Holoenzyme's ...
		The apoenzyme (lacking the cofactor pyrroloquinoline quinone, PQQ) was solubilized with Triton X-100 and purified to homogeneity.
		Reconstitution of the apoenzyme to full activity in the assay was achieved with a stoichiometric amount of PQQ in the presence of Mg
		The surprisingly low reactivity with glucose, in the absence of dye, as compared to the activity observed in the steady-state assay appeared to be due to formation of an anomalous enzyme form, mGDH*.
	pubs.acs.org /cgi-bin/abstract.cgi/bichaw/1998/37/i19/abs/bi9722610.html (379 words)

	Comparison of the Interaction of Cobalt Bovine Carbonic Anhydrase II with Acetazolamide and Methazolamide and the ... (Site not responding. Last check: 2007-10-11)
		Comparison of the Interaction of Cobalt Bovine Carbonic Anhydrase II with Acetazolamide and Methazolamide and the Reaction of Apoenzyme with Cobalt(II) Complexes of Acetazolamide and Methazolamide: Spectrophotometric Study -- Rubio et al.
		Comparison of the Interaction of Cobalt Bovine Carbonic Anhydrase II with Acetazolamide and Methazolamide and the Reaction of Apoenzyme with Cobalt(II) Complexes of Acetazolamide and Methazolamide
		the total amount of apoenzyme obtained after dialysis was determined.
	www.bambed.org /cgi/content/full/31/1/28 (1979 words)

	Cofactors and Prosthetic Groups (Site not responding. Last check: 2007-10-11)
		Any enzyme requiring a cofactor/prosthetic group will be inactive without it.
		When an enzyme is called an apoenzyme, the cofactor is not present.
		When the cofactor or prosthetic group is present we refer to the complex as the holoenzyme.
	www.chemistry.nmsu.edu /BCHE341/qna/cofactors.html (144 words)

	Introduction to Enzyme Activity
		The protein component of enzymes is termed the apoenzyme.
		The non-protein portion found in some enzymes and which frequently can be separated from the apoenzyme, is called the coenzyme.
		Other coenzymes include nicotinamide adenine dinucleotide (NAD+), flavin adenine dinucleotide (FAD), and coenzyme A. There are many metallo-proteins in which the metal ion (e.g., Cu++, Mg++, Zn++) is bonded either to the apoenzyme or to the coenzyme.
	faculty.uca.edu /~march/bio1/enzymes/introenz.htm (616 words)

	pauling.htm
		One mechanism, effective COT vitamins that serve as coenzymes, is that of shifting the equilibrium for the reaction of apoenzyme and coenzyme to give the active enzyme.
		Increase in concentration of the coenzyme can counteract the effect of the decrease in the value of the combining constant and lead to the formation of enough of the active enzyme to catalyze effectively the reaction of conversion of methylmalonic acid to succinic acid.
		An example is the intolerance to sulfa drugs associated with the substitution of arginine for histidine in the locus 58 in the alpha chain or 63 in the beta chain.
	www.orthomed.org /pauling.html (5254 words)

	Worthington Tyrosine Decarboxylase (Site not responding. Last check: 2007-10-11)
		Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide.
		By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined.
		The APOenzyme activity is measured in the presence of excess pyridoxal phosphate.
	www.worthington-biochem.com /TYD/cat.html (97 words)

	Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae -- Yamashita et al. 271 ... (Site not responding. Last check: 2007-10-11)
		The resulting apoenzyme was used in a reconstitution experiment.
		Absorption spectra of IDI and its apoenzyme.
		To determine the dissociation constants for the flavin coenzymes, various concentrations of the coenzymes were previously added to the assay mixture using the apoenzyme and without NADH, and the mixtures were placed on ice for 30 min and then used for enzyme assay by adding NADH.
	content.febsjournal.org /cgi/content/full/271/6/1087 (3616 words)

	dynamics of HIV1 protease
		We also investigated the structural changes in the apoenzyme and
		The two tryptophanes of the native apoenzyme were found
		dependence of phosphorescence in case of the apoenzyme and the
	www.netsci-journal.com /97v2/22.htm (176 words)

	Can We Predict our Risk of Getting Alzheimer's Disease (Site not responding. Last check: 2007-10-11)
		Study findings show men with an apoenzyme-epsilon4 (or APOE4) (apoenzyme: a protein that forms an active enzyme system by combining with a coenzyme.
		Men with an apoenzyme-epsilon4 (or APOE4) (apoenzyme: a protein that forms an active enzyme system by combining with a coenzyme.
		The combination then determines the specific substrate meaning the base on which an organism lives) allele (a group of genes appearing alternatively at the locusts – the position of a chromosome of a gene) had a significantly increased risk of AD of 2.39 (95% CI, 1.07, 5.31), after adjusting for age and education.
	www.alzheimersupport.com /articles/alz20.cfm (379 words)

	eMedicine - Riboflavin Deficiency : Article Excerpt by Nikolaos Tsiouris
		The less stable factor was named vitamin F (thiamine), while the heat-stable product was labeled vitamin G. They were later renamed vitamins B-1 and B-2, respectively.
		Two derivatives, riboflavin 5' phosphate (flavin mononucleotide [FMN]) and riboflavin 5' adenosine diphosphate (flavin adenine dinucleotide [FAD]), are the coenzymes that unite with specific apoenzyme proteins to form flavoprotein enzymes.
		Most of the flavin coenzyme systems help to regulate cellular metabolism, whereas others are specifically involved in carbohydrate or amino acid metabolism systems.
	www.emedicine.com /med/byname/riboflavin-deficiency.htm (422 words)

	Circulating Half-Life of PEGylated Recombinant Methioninase Holoenzyme Is Highly Dose Dependent on Cofactor ...
		MEGC-PEG-rMETase apoenzyme was determined, in the presence of
		Dose-dependent efficacy of PLP on plasma half-life of MEGC-PEG-rMETase holoenzyme (A) and apoenzyme (B) half-life.
		Osmotic pumps filled with PLP ranging from 5 to 500 mg/ml were implanted s.c.
	cancerres.aacrjournals.org /cgi/content/full/64/16/5775 (2842 words)

	BIO 205 Microbiology Lecture Outline (Site not responding. Last check: 2007-10-11)
		apoenzyme - inactive protein part of an enzyme
		Is there an advantage to using cofactors/coenzymes rather than simply producing a fully functional enzyme that does not require any "activator" molecule?
		holoenzyme - apoenzyme + coenzyme (or cofactor); active enzyme
	www.gwc.maricopa.edu /class/bio205/jcmlcX5.htm (565 words)

	Homogeneous, Nonradioactive, Enzymatic Assay for Plasma Pyridoxal 5-Phosphate -- Han et al. 48 (9): 1560 -- Clinical ...
		for endogenous PLP that might be present in the apoenzyme extract.
		The apoenzyme was stable at -80 °C for 1 year.
		apoenzyme from rebinding free PLP, the enzyme was precipitated
	www.clinchem.org /cgi/content/full/48/9/1560 (2400 words)

	A structural basis for the mechanism of aspartate-{beta}-semialdehyde dehydrogenase from Vibrio cholerae -- Blanco et ...
		solved, both as the apoenzyme (Hadfield et al.
		apoenzyme, and retains essentially the same conformation in
		cholerae apoenzymes that distance is approximately 13.5 Å.
	www.proteinscience.org /cgi/content/full/12/1/27 (3515 words)

	Comparing protein-ligand interactions in solution and single crystals by Raman spectroscopy -- Altose et al. 98 (6): ...
		This experiment was done by subtracting the spectrum of the apoenzyme
		apoenzyme was stored as a precipitate in the presence of 70% saturated
		Spectra of the holoenzyme and apoenzyme samples at protein concentrations
	www.pnas.org /cgi/content/full/98/6/3006 (4172 words)

	Enzyme - Wikipedia, the free encyclopedia
		Enzymes that require a cofactor but do not have one bound are called apoenzymes.
		An apoenzyme together with its cofactor(s) is called a holoenzyme (i.e.
		Most cofactors are not covalently attached to an enzyme, but are very tightly bound.
	en.wikipedia.org /wiki/Apoenzyme (5868 words)

	Conformational Difference between PDE4 Apoenzyme and Holoenzyme
		Using a fluorescence resonance energy transfer (FRET)-based equilibrium binding assay, we identified that L-791,760, a fluorescent inhibitor, binds to the apoenzyme (free enzyme) and the holoenzyme (enzyme bound to Mg) with comparable affinities (K
		By measuring the displacement of the bound L-791,760, we have also identified that other inhibitors bind differentially with the apoenzyme and the holoenzyme depending upon their structure.
		The conformational-sensitive inhibitor (R)-rolipram binds to the holoenzyme and apoenzyme with affinities (K
	pubs.acs.org /cgi-bin/abstract.cgi/bichaw/2000/39/i21/abs/bi992432w.html (244 words)

	Characterization of a Highly Conserved FAD-binding Site in Human Monoamine Oxidase B -- Zhou et al. 273 (24): 14862 -- ...
		to the MAO B apoenzyme is a multistep process.
		Modification of the apoenzyme by flavinylation is obligatory for the generation of catalytic activity in many flavoproteins.
		in the apoenzyme that stabilizes the three-dimensional structure
	www.jbc.org /cgi/content/full/273/24/14862 (5216 words)

	Interactions among the seven Helicobacter pylori proteins encoded by the urease gene cluster -- Voland et al. 284 (1): ...
		Finally, the apoenzyme or active enzyme is associated
		This is achieved by the action of the four accessory proteins.
		required for incorporation of nickel ions into the apoenzyme (26).
	ajpgi.physiology.org /cgi/content/full/284/1/G96 (6154 words)

	Donor substrate regulation of transketolase -- Esakova et al. 271 (21): 4189 -- FEBS Journal (Site not responding. Last check: 2007-10-11)
		The donor substrate did not affect the interaction of the apoenzyme
		to the apoenzyme of TK (apoTK) in the presence of magnesium
		of this analogue to the apoenzyme using the spectrophotometric
	content.febsjournal.org /cgi/content/full/271/21/4189 (3251 words)

	eMedicine - Methylmalonic Acidemia : Article Excerpt by: Olaf A Bodamer, MD, PhD, FACMG (Site not responding. Last check: 2007-10-11)
		MMA encompasses a heterogeneous group of disorders that are characterized by accumulation of methylmalonic acid and its by-products in biological fluids.
		These disorders are due to a deficiency of the adenosylcobalamin-dependent enzyme methylmalonyl-CoA mutase (apoenzyme deficiency), a defect in intracellular cobalamin metabolism (coenzyme deficiency), transcobalamin II deficiency, intrinsic factor deficiency, or dietary cobalamin deficiency, which is found in vegetarians.
		A subset of children with defects of intracellular cobalamin metabolism also may have simultaneous homocystinuria.
	www.emedicine.com /ped/byname/methylmalonic-acidemia.htm (554 words)

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