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Topic: Isomerase

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	Isomerase - Wikipedia, the free encyclopedia
		In biochemistry, an isomerase is any enzyme that catalyses the interconversion of isomers.
		The names of isomerases are formed as "substrate isomerase" (for example, enoyl CoA isomerase), or as "substrate type of isomerase" (for example, phosphoglucomutase).
		Isomerases are classified as EC 5 in the EC number classification of enzymes.
	en.wikipedia.org /wiki/Isomerase (121 words)

	[No title]
		Xylose isomerase is stable in the pH range of 6.5 to 8.5 at 30 (C for at least 2 h in the absence of metal ions.
		Alcohols and acetone The effect of acetone on the activity of xylose isomerase is not as strong as that of ethanol.
		Proteases Arthrobacter xylose isomerase was resistant to trypsin, chymotrypsin and elastase at 37 (C. Thermolysin cleaved specifically and quantitatively at Thr-347—Leu-348 between helices 10 and 11 to remove 47 residues from the C-terminus of each 43.3 kDa subunit.
	www.tkk.fi /Yksikot/Bioprosessitekniikka/Kem-70.415/PASTINEN_THESIS.DOC (5410 words)

	Title of Invention: Glucose isomerase enzymes and t heir use
		These glucose isomerases are obtained by expression of a gene encoding said enzyme, having an amino acid sequence which differs at least in one amino acid from the wildtype glucose isomerase.
		According to a preferred embodiment the stabilization of the tetrameric structure of glucose isomerase is achieved by strengthening the interaction between the dimers in the tetramer.
		Glucose isomerase final concentration in the assay was +0.01 mg/ml, and precisely determined, prior to dilution in the enzymatic assay mixture, by absorption spectroscopy using an extinction coefficient of 1.08 at 278 nm for a solution of enzyme of 1.0 mg/ml.
	www.nal.usda.gov /bic/Biotech_Patents/1994patents/05376536.html (11695 words)

	PIN1 - protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1
		Furthermore, KRMP1 interacted with the mitotic peptidyl-prolyl isomerase Pin1 in vivo, and an in vitro interaction was detected between the tail domain of KRMP1 and the WW domain of Pin1.
		Overexpression of the prolyl isomerase Pin1, which binds to the hyperphosphorylated forms of Cdc25, Myt1, and Wee1 found at M-phase, is known to block the initiation of mitosis in egg extracts.
		The WW domain-containing iso-prolyl isomerase named Pin1, a protein known to be essential for cell cycle progression, was shown to be active in restoration of the microtubule-binding activity of Tau, a protein of neurofibrillar tangles found in the brains of Alzheimer's patients.
	www.ihop-net.org /UniPub/iHOP/gg/91042.html (3861 words)

	Title of Invention: Xylose isomerase gene of Thermu s aquaticus
		The present invention relates to xylose isomerase genes of Thermus bacteria, especially Thermus aquaticus (hereinafter abbreviated as T. aquaticus), xylose isomerase produced by genetic engineering using the genes, a process for preparation of a xylose isomerase and a process for preparation of highly concentrated fructose using the xylose isomerase.
		Moreover, it was found that the xylose isomerase of T. aquaticus made by the genetic engineering method was unexpectedly different from the native xylose isomerase obtained from T. aquaticus and had excellent characteristics compared to the native one (see, Journal of General Microbiology (1990), 136, 679-686).
		As described in the Examples, purification of the present xylose isomerase is performed as follows: Transformants that have been transformed with the present xylose isomerase gene are cultured and the resulting cells are harvested by centrifugation.
	www.nal.usda.gov /bic/Biotech_Patents/1995patents/05411886.html (4763 words)

	Immobilization of glucose isomerase - Patent 4208482
		Immobilized glucose isomerase is prepared by mixing 0.5 to 1.5 parts by weight whole microbial cells containing glucose isomerase with one part by weight agar, combining the resultant mixture with an organic solvent, recovering discrete particles of agar gel with the whole microbial cells entrapped therein and drying the agar gel particles.
		In the conversion of glucose to fructose using glucose isomerase, because of the economics involved in producing glucose isomerase, it is of the utmost importance to use the isomerase under conditions whereby maximum yields of fructose are produced using minimum quantities of glucose isomerase.
		This invention relates to immobilized glucose isomerase and to a process of preparing same in which the immobilization is effected by means of entrapping whole cell glucose isomerase in spherical particles of agar gel.
	www.freepatentsonline.com /4208482.html (3216 words)

	Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase
		Isopentenyl diphosphate isomerase (IPP isomerase; EC 5.3.3.2) is a key enzyme for generating isoprenoid diversity and is responsible for the isomerization of the carbon−carbon double bond of IPP to create the potent electrophile DMAPP (Agranoff et al., 1960).
		IPP isomerase catalyses the interconversion of IPP and DMAPP by a stereoselective antarafacial [1.3] transposition of hydrogen (Figure 1) (Cornforth et al., 1966; Cornforth and Popjak, 1969; Poulter and Rilling, 1981).
		In addition to the crucial role of IPP isomerase in the isoprenoid pathway, the catalytic mechanism of this enzyme is also of great interest, as enzymatic protonation of unactivated olefins is rarely encountered in nature.
	www.nature.com /emboj/journal/v20/n7/full/7593656a.html (5540 words)

	Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced ...
		Recently, it was found that co-expression of a mutated PDI lacking its isomerase activity accelerates folding of human lysozyme expressed in yeast, leading to increases both in the amount of intracellular enzyme with the native conformation and in its secretion (Hayano et al., 1995).
		The isomerase activity is not only involved in the formation of native disulfides, but also in preventing disulfide cross-linking during refolding leading to aggregation.
		Puig A and Gilbert HF (1994) Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme.
	www.nature.com /emboj/journal/v16/n3/full/7590060a.html (5830 words)

	Structure/Function Relationships Responsible for Coenzyme Specificity and the Isomerase Activity of Human Type 1 ...
		of isomerase on the same enzyme protein (2, 8).
		Isomerase activity was measured by the initial absorbance increase
		The oxygen atoms are orange, nitrogen atoms are purple, carbon atoms are gray, and phosphorus atoms are lavender.
	www.jbc.org /cgi/content/full/278/37/35483 (3417 words)

	Formation of Protoanemonin from 2-Chloro-cis,cis-Muconate by the Combined Action of Muconate Cycloisomerase and ... (Site not responding. Last check: 2007-10-12)
		Reaction scheme for the transformation of 2CM by muconate cycloisomerase and muconolactone isomerase (A) and the transformation of 2CM muconate by mixtures of muconate or chloromuconate cycloisomerase (MCI and CMCI) and muconolactone isomerase (MLI) (B).
		isomerase in the reaction mixture increases the velocity of
		Muconolactone isomerase of the 3-oxoadipate pathway catalyzes dechlorination of 5-chloro-substituted muconolactones.
	jb.asm.org /cgi/content/full/184/19/5402 (3506 words)

	Hydratase/isomerase superfamily of enzymes
		-enoyl-CoA isomerases, were suggested to be, in addition to their evolutionary relationship, also mechanistically related, since both the hydratase-1 and the isomerase reactions involve protonation or deprotonation at the α-carbon (C2) of the substrate (Fig.
		-enoyl-CoA isomerase, a proton is abstracted from the α-methylene group of the substrate and subsequently donated to the γ -carbon (C4), resulting in a shift of the double bond from the β,γ -position to the α,β -conformation (Fig.
		The amino acid residue responsible for the protonation of the γ -carbon in the isomerization reaction is not known, the proton could be donated by a water molecule or the deprotonation and the protonation could be accomplished by the same residue.
	herkules.oulu.fi /isbn9514266579/html/i5482.html (5874 words)

	Protein Disulfide Isomerase (Site not responding. Last check: 2007-10-12)
		Protein disulfide isomerase is localized in the lumen of the ER at a concentration of approximately 10 mg/ml and is enriched in secretory cells.
		Protein disulfide isomerase is a component of prolyl-4-hydroxylase (an alpha2beta2 tetramer where the beta subunits are protein disulfide isomerase), an enzyme that catalyzes the hydroxylation of prolines in procollagen during the synthesis of collagen.
		Protein disulfide isomerase is also a component of microsomal triacylglycerol transfer protein (a heterodimer of PDI and a 97kDa subunit), that is believed to catalyze the transfer of neutral lipid onto nascent lipoprotein particles.
	www.cryst.bbk.ac.uk /PPS95/us/darren-f/PDI.html (317 words)

	RETINENE ISOMERASE -- Hubbard 39 (6): 935 -- The Journal of General Physiology (Site not responding. Last check: 2007-10-12)
		"retinene isomerase." It is soluble in neutral phosphate buffer,
		is irradiated in the presence of isomerase, the rate of formation
		isomerase is specific for all-trans and neo-b retinene.
	www.jgp.org /cgi/content/abstract/39/6/935 (270 words)

	Xylose Isomerase hydride shift catalysis
		Xylose isomerase is one of the most widely used commercial enzymes, being used to convert glucose to fructose by the drinks industry (or xylose to xylulose).
		The active site of xylose isomerase is known from crystal structures to require two metal ions per active site for catalysis.
		The isomerisation was originally thought to proceed via a cis-ene diol intermediate but under this mechanism the proton which moves during the isomerisation would exchange with the solvent and this is not observed for the xylose isomerase reaction.
	people.man.ac.uk /~mbdssmav/posters/mn/post_1.htm (922 words)

	Thiol-Disulfide Isomerization in Thrombospondin: Effects of Conformation and Protein Disulfide Isomerase -- Huang et ...
		Additional evidence for the correlation of EDTA-conformation and thiol-disulfide exchange was the enhanced conversion of thrombospondin to its EDTA-conformation in the presence of protein disulfide isomerase and the inability of thrombospondin pretreated with NEM to attain the EDTA-conformation.
		After purification of TSP, there was no isomerization under those conditions, but isomerization of purified TSP occurred when protein disulfide isomerase was added, when the temperature was increased to 37°C or when the pH was increased to 8.4.
		A possible explanation is the reported presence of protein disulfide isomerase in the supernatant solution of activated platelets.
	www.bloodjournal.org /cgi/content/full/89/9/3205 (5544 words)

	The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the ... (Site not responding. Last check: 2007-10-12)
		The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide -- Koivunen et al.
		The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide
		Puig, A. and Gilbert, H.F. Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme.
	embojournal.npgjournals.com /cgi/content/full/18/1/65 (6641 words)

	Identification of an Archaeal Type II Isopentenyl Diphosphate Isomerase in Methanothermobacter thermautotrophicus -- ... (Site not responding. Last check: 2007-10-12)
		archaeal IPP isomerase might be a novel enzyme (33).
		Isopentenyldiphosphate:dimethylallyldiphosphate isomerase: construction of a high-level heterologous expression system for the gene from Saccharomyces cerevisiae and identification of an active-site nucleophile.
		Catalytic mechanism of Escherichia coli isopentenyl diphosphate isomerase involves Cys-67, Glu-116, and Tyr-104 as suggested by crystal structures of complexes with transition state analogues and irreversible inhibitors.
	jb.asm.org /cgi/content/full/186/6/1811?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&fulltext=biosynthesis&searchid=1080591491709_3972&stored_search=&FIRSTINDEX=0&volume=186&issue=6&journalcode=jb (3756 words)

	Both the Immunosuppressant SR31747 and the Antiestrogen Tamoxifen Bind to an Emopamil-Insensitive Site of Mammalian ...
		7 sterol isomerase in the case of tamoxifen.
		Kolaczkowski M, van der Rest M, Cybularz-Kolaczkowska A, Soumillion JP, Konings WN and Goffeau A (1996) Drugs, ionophoretic peptides, and steroids as substrates of the yeast multidrug transporter Pdr5p.
		Mikhailidis DP and Spyropoulos KA (1996) The effect of tamoxifen on lipid and haemostatic predictors of ischaemic heart disease.
	jpet.aspetjournals.org /cgi/content/full/285/3/1296 (4076 words)

	ARS \| Publication request: A Survey for Phosphoglucose Isomerase with Lysyl Aminopeptidase Activity in Vibrionaceae and ...
		Since a variety of Vibrio species cause disease in humans and fish, a survey was conducted to determine the prevalence of this enzyme in other members of the Vibrio family and in non-Vibrio human pathogens.
		This enzyme, known as phosphoglucose isomerase with a lysyl aminopeptidase activity (PGI-LysAP), was identified in chemically-purified cultures of all members from the Vibrio family.
		Technical Abstract: Phosphoglucose isomerase (PGI) with a novel lysyl aminopeptidase (LysAP) activity was recently purified and characterized from Vibrio vulnificus.
	www.ars.usda.gov /research/publications/publications.htm?SEQ_NO_115=168946 (403 words)

	EPA: Federal Register: Phosphomannose Isomerase and the Genetic Material Necessary for Its Production in All Plants; ... (Site not responding. Last check: 2007-10-12)
		The petition requested that 40 CFR part 180 be amended by establishing an exemption from the requirement of a tolerance for residues in or on all plant commodities of phosphomannose isomerase and the genetic material necessary for its production in all plants.
		Therefore, EPA expects acute oral toxicity with high doses of purified protein and specific criteria on protein degradation and similarity analyses to provide adequate information to reach a finding of a reasonable certainity of no harm in the aggregate for a PIP protein or an inert ingredient associated with a PIP.
		Phosphomannose isomerase (PMI) protein and the genetic material necessary for its production in plants are exempt from the requirement of a tolerance when used as plant-incorporated protectant inert ingredients in plant commodities.
	www.epa.gov /fedrgstr/EPA-PEST/2004/May/Day-14/p10877.htm (4076 words)

	Prolyl Hydroxylase, Protein Disulfide Isomerase and Other Proteins (Site not responding. Last check: 2007-10-12)
		This timely resource analyzes the function of specific enzymes in the complex processes of protein conformation, assembly, and stability - comprehensively addressing the folding of proteins to natural states as well as cotranslational and postranslational modifications that effect function.
		Protein Disulfide Isomerase from Soybean: Isolation, Structure, and Function in Protein Folding.
		Protein Disulfide Isomerase and the Complications of Protein Folding.
	www.chipsbooks.com /prolyl.htm (305 words)

	Triose Phosphate Isomerase: Genetic Music
		One of the two sugars is glyceraldehyde-3-phosphate and the other is a related sugar that can be converted to glyceraldehyde-3-phosphate by the action of triose phosphate isomerase.
		This conversion allows all products of the initial glucose molecule to be further metabolized for maximum energy yield.
		The music begins with a slow section that samples the amino acids of the protein at fairly long intervals.
	whozoo.org /mac/Music/tpi.htm (279 words)

	InterPro: IPR000297 PpiC-type peptidyl-prolyl cis-trans isomerase
		Peptidylprolyl isomerase (5.2.1.8) is an enzyme that accelerates protein folding by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides [ 1 ].
		P0A265 Peptidyl-prolyl cis-trans isomerase C (EC 5.2.1.8) (PPIase C) (Rotamase C) (Parvulin)
		Rahfeld J.U. Rucknagel K.P. Schelbert B. Ludwig B. Hacker J. Mann K. Fischer G. Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases.
	www.ebi.ac.uk /interpro/IEntry?ac=IPR000297 (2735 words)

	SmanTPIBlast
		>gi1351281spP48501TPIS_SCHMA TRIOSEPHOSPHATE ISOMERASE (TIM) gi283520pirA38233 triose-phosphate isomerase (EC 5.3.1.1) - fluke (Schistosoma mansoni) gi161129gbAAA29941.1
		(XM_032607) triosephosphate isomerase 1 [Homo sapiens] gi136060spP00938TPIS_HUMAN Triosephosphate isomerase (TIM) gi68420pirISCZT1 triose-phosphate isomerase (EC 5.3.1.1) 1 - chimpanzee gi2144541pirISHUT triose-phosphate isomerase (EC 5.3.1.1) - human gi37247embCAA49379.1
		(M10036) triosephosphate isomerase (EC 5.3.1.1) [Homo sapiens] gi1200507gbAAB51316.1
	www.library.csi.cuny.edu /~davis/assignments/SmanTPIBlast.htm (383 words)

	Alternatives to the Isomerase-dependent Pathway for the beta -Oxidation of Oleic Acid Are Dispensable in Saccharomyces ...
		-enoyl-CoA isomerase) in the degradation pathway of unsaturated fatty acids with double bonds at even-numbered positions.
		Dci1p-enriched Cell Extracts Contain Di-isomerase and Isomerase Activities-- To determine the enzymatic properties of Dci1p, it was overexpressed in the corresponding dci1
		Molecular Identification and Characterization of the Arabidopsis {Delta}3,5,{Delta}2,4-Dienoyl-Coenzyme A Isomerase, a Peroxisomal Enzyme Participating in the {beta}-Oxidation Cycle of Unsaturated Fatty Acids
	www.jbc.org /cgi/content/full/274/35/24514 (4836 words)

	CELLULAR METABOLISM AND FERMENTATION
		Glyceraldehyde phosphate (GAP, also known as phosphoglyceraldehyde, PGAL) is the more readily used of the two.
		Dihydroxyacetone phosphate can be converted into GAP by the enzyme Isomerase.
		The end of the glycolysis process yields two pyruvic acid (3-C) molecules, and a net gain of 2 ATP and two NADH per glucose.
	www.estrellamountain.edu /faculty/farabee/biobk/BioBookGlyc.html (1147 words)

	EC 5.3.1.9 (Site not responding. Last check: 2007-10-12)
		Nakagawa, Y. and Noltmann, E.A. Isolation of crystalline phosphoglucose isomerase from brewers' yeast.
		Noltmann, E.A. Isolation of crystalline phosphoglucose isomerase from rabbit muscle.
		Ramasarma, T. and Giri, K.V. Phosphoglucose isomerase of green gram (Phaseolus radiatus).
	www.chem.qmul.ac.uk /iubmb/enzyme/EC5/3/1/9.html (126 words)

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