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  • 1
    Keywords: Life sciences ; Medicine ; Toxicology ; Biotechnology ; Food science ; Veterinary Medicine ; Biochemistry ; Life sciences ; Biochemistry, general ; Molecular Medicine ; Pharmacology/Toxicology ; Food science ; Biotechnology ; Veterinary Medicine ; Springer eBooks
    Description / Table of Contents: 3.4.11.24 aminopeptidase S -- 3.4.17.23 angiotensin-converting enzyme 2 -- 3.4.22.69 SARS coronavirus main proteinase -- 3.4.22.70 sortase A -- 3.4.22.71 sortase B -- 3.4.23.50 human endogenous retrovirus K Endopeptidase -- 3.4.23.51 HycI peptidase -- 3.4.24.87 ADAMTS13 endopeptidase -- 3.4.25.2 HslU-HslV peptidase -- 3.5.1.99 fatty acid amide hydrolase -- 3.5.1.100 (R)-amidase -- 3.5.1.101 L-proline amide hydrolase -- 3.5.1.102 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5’- monophosphate deformylase -- 3.5.1.103 N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-a- D-glucopyranoside deacetylase -- 3.5.1.104 peptidoglycan-N-acetylglucosamine Deacetylase -- 3.5.1.105 chitin disaccharide deacetylase -- 3.5.1.106 N-formylmaleamate deformylase -- 3.5.1.107 maleamate amidohydrolase -- 3.5.1.108 UDP-3-O-acyl-N-acetylglucosamine Deacetylase -- 3.5.2.19 streptothricin hydrolase -- 3.5.99.8 5-nitroanthranilic acid aminohydrolase -- 3.6.1.53 Mn2+-dependent ADP-ribose/CDP-alcohol Diphosphatase -- 3.6.1.54 UDP-2,3-diacylglucosamine diphosphatase -- 3.6.4.12 DNA helicase -- 3.6.4.13 RNA helicase -- 3.7.1.11 cyclohexane-1,2-dione hydrolase -- 3.7.1.12 cobalt-precorrin 5A hydrolase -- 3.7.1.13 -hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4- dienoate hydrolase -- 4.1.1.87 malonyl-S-ACP decarboxylase -- 4.1.1.88 biotin-independent malonate decarboxylase -- 4.1.1.89 biotin-dependent malonate decarboxylase -- 4.1.1.90 peptidyl-glutamate 4-carboxylase -- 4.1.2.43 3-hexulose-6-phosphate synthase -- 4.1.2.44 benzoyl-CoA-dihydrodiol lyase -- 4.1.2.45 trans-o-hydroxybenzylidenepyruvate hydratase-aldolase -- 4.1.2.46 aliphatic (R)-hydroxynitrile lyase -- 4.1.3.41 3-hydroxy-D-aspartate aldolase -- 4.1.99.13 (6-4)DNA photolyase -- 4.1.99.14 spore photoproduct lyase -- 4.1.99.15 S-specific spore photoproduct lyase -- 4.2.1.114 methanogen homoaconitase -- 4.2.1.115 UDP-N-acetylglucosamine 4,6-dehydratase (inverting) -- 4.2.1.116 3-hydroxypropionyl-CoA dehydratase -- 4.2.1.117 2-methylcitrate dehydratase (2-methyl-transaconitate forming) -- 4.2.1.118 3-dehydroshikimate dehydratase -- 4.2.1.119 enoyl-CoA hydratase 2 -- 4.2.1.120 4-hydroxybutanoyl-CoA dehydratase -- 4.2.1.121 colneleate synthase -- 4.2.3.28 ent-cassa-12,15-diene synthase -- 4.2.3.29 ent-sandaracopimaradiene synthase -- 4.2.3.30 ent-pimara-8(14),15-diene synthase -- 4.2.3.31 ent-pimara-9(11),15-diene synthase -- 4.2.3.32 levopimaradiene synthase -- 4.2.3.33 stemar-13-ene synthase -- 4.2.3.34 stemod-13(17)-ene synthase -- 4.2.3.35 syn-pimara-7,15-diene synthase -- 4.2.3.36 terpentetriene synthase -- 4.2.3.37 epi-isozizaene synthase -- 4.2.3.38 a-bisabolene synthase -- 4.2.3.39 epi-cedrol synthase -- 4.2.3.40 (Z)-g-bisabolene synthase -- 4.2.3.41 elisabethatriene synthase -- 4.2.3.42 aphidicolan-16b-ol synthase -- 4.2.3.43 fusicocca-2,10(14)-diene synthase -- 4.2.3.44 isopimara-7,15-diene synthase -- 4.2.3.45 phyllocladan-16a-ol synthase -- 4.2.3.46 a-farnesene synthase -- 4.2.3.47 b-farnesene synthase -- 4.2.3.48 (3S,6E)-nerolidol synthase -- 4.2.3.49 (3R,6E)-nerolidol synthase -- 4.2.99.20 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase -- 4.2.99.21 isochorismate lyase -- 4.3.1.26 chromopyrrolate synthase -- 4.3.1.27 threo-3-hydroxy-D-aspartate ammonia-lyase -- 4.3.99.2 carboxybiotin decarboxylase -- 4.99.1.8 heme ligase -- 5.1.99.5 hydantoin racemase -- 5.3.1.27 6-phospho-3-hexuloisomerase -- 5.3.1.28 D-sedoheptulose 7-phosphate isomerase -- 5.5.1.14 syn-copalyl-diphosphate synthase -- 5.5.1.15 terpentedienyl-diphosphate synthase -- 5.5.1.16 halimadienyl-diphosphate synthase -- 5.99.1.4 2-hydroxychromene-2-carboxylate isomerase -- 6.1.1.27 O-phospho-L-serine-tRNA ligase -- 6.2.1.35 ACP-SH:acetate ligase -- 6.2.1.36 3-hydroxypropionyl-CoA synthase -- 6.3.1.13 L-cysteine:1D-myo-inositol 2-amino-2-deoxy-a-D-glucopyranoside ligase -- 6.3.1.14 diphthine-ammonia ligase -- 6.3.2.31 coenzyme F420-0:L-glutamate ligase -- 6.3.2.32 coenzyme g-F420-2:a-L-glutamate ligase -- 6.3.2.33 coenzyme g-F420-2:a-L-glutamate ligase -- 6.3.2.33 tetrahydrosarcinapterin synthase -- 6.3.2.34 coenzyme F420-1:g-L-glutamate ligase -- 6.3.2.35 D-alanine-D-serine ligase -- 6.3.2.36 4-phosphopantoate-b-alanine ligase
    Abstract: Springer Handbook of Enzymes provides data on enzymes sufficiently well characterized. It offers concise and complete descriptions of some 5,000 enzymes and their application areas. Data sheets are arranged in their EC-Number sequence and the volumes themselves are arranged according to enzyme classes. This new, second edition reflects considerable progress in enzymology: many enzymes are newly classified or reclassified. Each entry is correlated with references and one or more source organisms. New datafields are created: application and engineering (for the properties of enzymes where the sequence has been changed). The total amount of material contained in the Handbook has more than doubled so that the complete second edition consists of 39 volumes as well as a Synonym Index. In addition, starting in 2009, all newly classified enzymes are treated in Supplement Volumes. Springer Handbook of Enzymes is an ideal source of information for researchers in biochemistry, biotechnology, organic and analytical chemistry, and food sciences, as well as for medicinal applications
    Pages: : digital.
    Edition: Second Edition.
    ISBN: 9783642362606
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  • 2
    Keywords: Life sciences ; Medicine ; Toxicology ; Biotechnology ; Food science ; Veterinary Medicine ; Biochemistry ; Life sciences ; Biochemistry, general ; Molecular Medicine ; Pharmacology/Toxicology ; Food science ; Biotechnology ; Veterinary Medicine ; Springer eBooks
    Description / Table of Contents: 1.1.1.295℗ momilactone-A synthase -- 1.1.1.296℗ dihydrocarveol dehydrogenase -- 1.1.1.297℗ limonene-1,2-diol dehydrogenase -- 1.1.1.298℗ 3-hydroxypropionate dehydrogenase (NADP+) -- 1.1.1.299℗ malate dehydrogenase [NAD(P)+] -- 1.1.1.300℗ NADP-retinol dehydrogenase -- 1.1.1.301℗ D-arabitol-phosphate dehydrogenase -- 1.1.1.302℗ 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5́€™-phosphate reductase -- 1.1.1.303℗ diacetyl reductase [(R)-acetoin forming] -- 1.1.1.304℗ diacetyl reductase [(S)-acetoin forming] -- 1.1.1.305℗ UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating) -- 1.1.1.306℗ S-(hydroxymethyl)mycothiol dehydrogenase -- 1.1.1.307℗ D-xylose reductase -- 1.1.1.308℗ sulfopropanediol 3-dehydrogenase -- 1.1.1.309℗ phosphonoacetaldehyde reductase (NADH) -- 1.1.2.6℗ ℗ polyvinyl alcohol dehydrogenase (cytochrome) -- 1.1.2.7℗ ℗ methanol dehydrogenase (cytochrome c) -- 1.1.2.8℗ ℗ alcohol dehydrogenase (cytochrome c) -- 1.1.5.3℗ ℗ glycerol-3-phosphate dehydrogenase -- 1.1.5.4℗ ℗ malate dehydrogenase (quinone) -- 1.1.5.5℗ ℗ alcohol dehydrogenase (quinone) -- 1.1.5.6℗ ℗ formate dehydrogenase-N -- 1.1.5.7℗ ℗ cyclic alcohol dehydrogenase (quinone) -- 1.1.5.8℗ ℗ quinate dehydrogenase (quinone) -- 1.1.99.1℗ alcohol dehydrogenase (azurin) -- 1.1.99.33℗ formate dehydrogenase (acceptor) -- 1.1.99.34℗ glucose-6-phosphate dehydrogenase (coenzyme-F420) -- 1.1.99.35℗ soluble quinoprotein glucose dehydrogenase -- 1.1.99.36℗ NDMA-dependent alcohol dehydrogenase -- 1.1.99.37℗ NDMA-dependent methanol dehydrogenase -- 1.2.1.73℗ sulfoacetaldehyde dehydrogenase -- 1.2.1.74℗ abietadienal dehydrogenase -- 1.2.1.75℗ malonyl CoA reductase (malonate semialdehyde-forming) -- 1.2.1.76℗ succinate-semialdehyde dehydrogenase (acylating) -- 1.2.1.77℗ 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) -- 1.2.1.78℗ 2-formylbenzoate dehydrogenase -- 1.2.1.80℗ long-chain acyl-[acyl-carrier-protein] reductase -- 1.2.5.1℗ ℗ pyruvate dehydrogenase (quinone) -- 1.3.1.81℗ (+)-pulegone reductase -- 1.3.1.82℗ (-)-isopiperitenone reductase -- 1.3.1.83℗ geranylgeranyl diphosphate reductase -- 1.3.1.84℗ acrylyl-CoA reductase (NADPH) -- 1.3.1.85℗ crotonyl-CoA carboxylase/reductase -- 1.3.1.86℗ crotonyl-CoA reductase -- 1.3.5.2℗ ℗ dihydroorotate dehydrogenase (quinone) -- 1.3.5.3℗ ℗ protoporphyrinogen IX dehydrogenase (menaquinone) -- 1.3.5.4℗ ℗ fumarate reductase (menaquinone) -- 1.3.7.6℗ ℗ phycoerythrobilin synthase -- 1.3.99.24℗ 2-amino-4-deoxychorismate dehydrogenase -- 1.3.99.25℗ carvone reductase -- 1.4.3.21℗ primary-amine oxidase -- 1.4.3.22℗ diamine oxidase -- 1.4.3.23℗ 7-chloro-L-tryptophan oxidase -- 1.4.5.1℗ ℗ D-amino acid dehydrogenase (quinone) -- 1.5.3.13℗ N1-acetylpolyamine oxidase -- 1.5.3.14℗ polyamine oxidase (propane-1,3-diamineforming) -- 1.5.3.15℗ N8-acetylspermidine oxidase (propane-1,3-diamine-forming) -- 1.5.3.16℗ spermine oxidase -- 1.5.3.17℗ non-specific polyamine oxidase -- 1.5.99.13℗ D-proline dehydrogenase -- 1.7.5.1℗ ℗ nitrate reductase (quinone) -- 1.8.1.16℗ glutathione amide reductase -- 1.8.7.2℗ ℗ ferredoxin:thioredoxin reductase -- 1.11.1.17℗ glutathione amide-dependent peroxidase -- 1.11.1.19℗ dye decolorizing peroxidase -- 1.11.2.1℗ unspecific peroxygenase -- 1.13.11.56℗ 1,2-dihydroxynaphthalene dioxygenase monooxygenase -- 1.14.13.112℗ 3-epi-6-deoxocathasterone 23-monooxygenase -- 1.14.13.113℗ FAD-dependent urate hydroxylase -- 1.14.13.114℗ 6-hydroxynicotinate 3-monooxygenase -- 1.14.13.115℗ angelicin synthase -- 1.14.13.116℗ geranylhydroquinone 3́€™́€™-hydroxylase -- 1.14.13.117℗ isoleucine N-monooxygenase -- 1.14.13.118℗ valine N-monooxygenase -- 1.14.14.7℗ tryptophan 7-halogenase -- 1.14.14.8℗ anthranilate 3-monooxygenase (FAD) -- 1.14.15.8℗ steroid 15b-monooxygenase -- 1.14.19.4℗ D8-fatty-acid desaturase -- 1.14.19.5℗ D11-fatty-acid desaturase -- 1.14.19.6℗ D12-fatty-acid desaturase -- 1.14.21.7℗ biflaviolin synthase -- 1.14.99.39℗ ammonia monooxygenase -- 1.14.99.40℗ 5,6-dimethylbenzimidazole synthase -- 1.17.2.1℗ nicotinate dehydrogenase (cytochrome) -- 1.17.5.2℗ caffeine dehydrogenase -- 1.17.7.1℗ (E)-4-hydroxy-3-methylbut-2-enyldiphosphate synthase -- 1.20.4.3℗ Mycoredoxin -- 1.22.1.1℗ iodotyrosine deiodinase
    Abstract: Springer Handbook of Enzymes provides data on enzymes sufficiently well characterized. It offers concise and complete descriptions of some 5,000 enzymes and their application areas. Data sheets are arranged in their EC-Number sequence and the volumes themselves are arranged according to enzyme classes. This new, second edition reflects considerable progress in enzymology: many enzymes are newly classified or reclassified. Each entry is correlated with references and one or more source organisms. New datafields are created: application and engineering (for the properties of enzymes where the sequence has been changed). The total amount of material contained in the Handbook has more than doubled so that the complete second edition consists of 39 volumes as well as a Synonym Index. In addition, starting in 2009, all newly classified enzymes are treated in Supplement Volumes. Springer Handbook of Enzymes is an ideal source of information for researchers in biochemistry, biotechnology, organic and analytical chemistry, and food sciences, as well as for medicinal applications
    Pages: : digital.
    Edition: Second Edition.
    ISBN: 9783642362651
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  • 3
    Keywords: Life sciences ; Medicine ; Toxicology ; Biotechnology ; Food science ; Veterinary Medicine ; Biochemistry ; Life sciences ; Biochemistry, general ; Molecular Medicine ; Pharmacology/Toxicology ; Food science ; Biotechnology ; Veterinary Medicine ; Springer eBooks
    Pages: : digital
    Edition: Second Edition.
    ISBN: 9783540857075
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  • 4
    Keywords: Life sciences ; Medicine ; Toxicology ; Biotechnology ; Food science ; Veterinary Medicine ; Biochemistry ; Life sciences ; Biochemistry, general ; Molecular Medicine ; Pharmacology/Toxicology ; Food science ; Biotechnology ; Veterinary Medicine ; Springer eBooks
    Description / Table of Contents: 2.1.1.163 demethylmenaquinone methyltransferase -- 2.1.1.164 demethylrebeccamycin-D-glucose Omethyltransferase -- 2.1.1.165 methyl halide transferase -- 2.1.1.166 23S rRNA (uridine2552-2’-O-)-methyltransferase -- 2.1.1.167 27S pre-rRNA (guanosine2922-2’-O)-methyltransferase -- 2.1.1.168 21S rRNA (uridine2791-2’-O)-methyltransferase -- 2.1.1.169 tricetin 3’,4’,5’-O-trimethyltransferase -- 2.1.1.170 16S rRNA (guanine527-N7)-methyltransferase -- 2.1.1.171 16S rRNA (guanine966-N2)-methyltransferase -- 2.1.1.172 16S rRNA (guanine1207-N2)-methyltransferase -- 2.1.1.173 23S rRNA (guanine2445-N2)-methyltransferase -- 2.1.1.174 23S rRNA (guanine1835-N2)-methyltransferase -- 2.1.1.175 tricin synthase -- 2.1.1.176 16S rRNA (cytosine967-C5)-methyltransferase -- 2.1.1.177 23S rRNA (pseudouridine1915-N3)-methyltransferase -- 2.1.1.178 16S rRNA (cytosine1407-C5)-methyltransferase -- 2.1.1.179 16S rRNA (guanine1405-N7)-methyltransferase -- 2.1.1.180 16S rRNA (adenine1408-N1)-methyltransferase -- 2.1.1.181 23S rRNA (adenine1618-N6)-methyltransferase -- 2.1.1.182 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase -- 2.1.1.183 18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase -- 2.1.1.184 23S rRNA (adenine2085-N6)- dimethyltransferase -- 2.1.1.185 23S rRNA (guanosine2251-2’-O-)- methyltransferase -- 2.1.1.186 23S rRNA (cytidine2498-2’-O)-methyltransferase -- 2.1.1.195 cobalt-precorrin-5B (C1)-methyltransferase -- 2.1.1.196 cobalt-precorrin-7 (C15)-methyltransferase[decarboxylating] -- 2.1.1.197 malonyl-CoA O-methyltransferase -- 2.1.1.198 16S rRNA (cytidine1402-2’-O)-methyltransferase -- 2.1.1.199 16S rRNA (cytosine1402-N4)-methyltransferase -- 2.1.2.13 UDP-4-amino-4-deoxy-L-arabinose formyltransferase -- 2.1.3.10 malonyl-S-ACP:biotin-protein carboxyltransferase:- 2.1.3.11 N-succinylornithine carbamoyltransferase -- 2.2.1.9 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase -- 2.3.1.185 tropine acyltransferase -- 2.3.1.186 pseudotropine acyltransferase -- 2.3.1.187 acetyl-S-ACP:malonate ACP transferase -- 2.3.1.188 w-hydroxypalmitate O-feruloyl transferase -- 2.3.1.189 mycothiol synthase -- 2.3.1.190 acetoin dehydrogenase -- 2.3.1.191 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase -- 2.3.1.192 glycine N-phenylacetyltransferase -- 2.3.2.16 lipid II:glycine glycyltransferase -- 2.3.2.17 N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl- (N6-glycyl)-D-alanyl-D-alaninediphosphoundecaprenyl-Nacetylglucosamine: glycine glycyltransferase -- 2.3.2.18 N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl- (N6-triglycine)-D-alanyl-D-alaninediphosphoundecaprenyl-Nacetylglucosamine: glycine lycyltransferase -- 2.4.1.245 a,a-trehalose synthase -- 2.4.1.247 b-D-galactosyl-(1!4)-L-rhamnose phosphorylase -- 2.4.1.248 cycloisomaltooligosaccharide glucanotransferase -- 2.4.1.249 delphinidin 3’,5’-O-glucosyltransferase -- 2.4.1.250 D-inositol-3-phosphate glycosyltransferase -- 2.4.1.251 GlcA-b-(1!2)-D-Man-a-(1!3)-D-Glc-b- (1!4)-D-Glc-a-1-diphospho-ditrans,octacisundecaprenol 4-b-mannosyltransferase -- 2.4.1.252 GDP-mannose:cellobiosyldiphosphopolyprenol a-mannosyltransferase -- 2.4.1.253 baicalein 7-O-glucuronosyltransferase -- 2.4.2.41 xylogalacturonan b-1,3-xylosyltransferase -- 2.4.2.42 UDP-D-xylose:b-D-glucoside a-1,3-Dxylosyltransferase -- 2.4.2.43 lipid IVA 4-amino-4-deoxy-Larabinosyltransferase -- 2.4.99.12 lipid IVA 3-deoxy-D-manno-octulosonic acid transferase -- 2.4.99.13 (KDO)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase -- 2.4.99.14 (KDO)2-lipid IVA (2-8) 3-deoxy-D-mannooctulosonic acid transferase -- 2.4.99.15 (KDO)3-lipid IVA (2-4) 3-deoxy-D-mannooctulosonic acid transferase -- 2.5.1.72 quinolinate synthase -- 2.5.1.73 O-phospho-L-seryl-tRNA:Cys-tRNA synthase -- 2.5.1.74 1,4-dihydroxy-2-naphthoate polyprenyltransferase -- 2.5.1.75 tRNA dimethylallyltransferase -- 2.5.1.76 cysteate synthase -- 2.5.1.77 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase -- 2.5.1.78 6,7-dimethyl-8-ribityllumazine synthase -- 2.5.1.79 thermospermine synthase -- 2.5.1.80 7-dimethylallyltryptophan synthase -- 2.5.1.81 geranylfarnesyl diphosphate synthase -- 2.5.1.82 hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] -- 2.5.1.83 hexaprenyl-diphosphate synthase [(2E,6E)- farnesyl-diphosphate specific] -- 2.5.1.84 all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific] -- 2.5.1.85 all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] -- 2.5.1.86 trans,polycis-decaprenyl diphosphate Synthase -- 2.5.1.87 ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] -- 2.5.1.88 trans,polycis-polyprenyl diphosphate synthase [(2Z,6E)-farnesyl diphosphate specific] -- 2.5.1.89 tritrans,polycis-undecaprenyl-diphosphate synthase [geranylgeranyl-diphosphate specific] -- 2.5.1.93 4-hydroxybenzoate geranyltransferase -- 2.5.1.94 adenosyl-chloride synthase -- 2.6.1.86 2-amino-4-deoxychorismate synthase -- 2.6.1.87 UDP-4-amino-4-deoxy-L-arabinose aminotransferase -- 2.7.1.161 CTP-dependent riboflavin kinase -- 2.7.1.162 N-acetylhexosamine 1-kinase -- 2.7.1.163 hygromycin B 4-O-kinase -- 2.7.1.164 O-phosphoseryl-tRNASec kinase -- 2.7.1.165 glycerate 2-kinase -- 2.7.1.166 3-deoxy-D-manno-octulosonic acid kinase -- 2.7.1.167 D-glycero-b-D-manno-heptose-7-phosphate kinase -- 2.7.1.168 D-glycero-a-D-manno-heptose-7-phosphate kinase -- 2.7.1.169 pantoate kinase -- 2.7.4.25 (d)CMP kinase -- 2.7.7.66 malonate decarboxylase holo-[acyl-carrier protein] synthase -- 2.7.7.67 CDP-archaeol synthase -- 2.7.7.68 2-phospho-L-lactate guanylyltransferase -- 2.7.7.70 D-glycero-b-D-manno-heptose 1-phosphate adenylyltransferase -- 2.7.7.71 D-glycero-a-D-manno-heptose 1-phosphate guanylyltransferase -- 2.7.7.72 CCA tRNA nucleotidyltransferase -- 2.7.8.28 2-phospho-L-lactate transferase -- 2.7.8.29 L-serine-phosphatidylethanolamine phosphatidyltransferase -- 2.7.8.30 undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase -- 2.7.8.31 undecaprenyl-phosphate glucose phosphotransferase -- 2.8.2.35 dermatan 4-sulfotransferase -- 2.8.4.2 arsenate-mycothiol transferase -- 2.9.1.2 O-phospho-L-seryl-tRNASec:L-selenocysteinyltRNA synthase -- 3.1.1.83 monoterpene e-lactone hydrolase -- 3.1.1.84 cocaine esterase -- 3.1.2.28 1,4-dihydroxy-2-naphthoyl-CoA hydrolase -- 3.1.3.78 phosphatidylinositol-4,5-bisphosphate 4-phosphatase -- 3.1.3.80 2,3-bisphosphoglycerate 3-phosphatase -- 3.1.3.81 diacylglycerol diphosphate phosphatase -- 3.1.3.82 -glycero-b-D-manno-heptose 1,7-bisphosphate 7-phosphatase -- 3.1.3.83 D-glycero-a-D-manno-heptose 1,7-bisphosphate 7-phosphatase -- 3.1.4.53 3’,5’-cyclic-AMP phosphodiesterase -- 3.1.7.4 sclareol cyclase -- 3.1.7.5 geranylgeranyl diphosphate diphosphatase -- 3.1.7.6 farnesyl diphosphatase -- 3.1.26.12 ribonuclease E -- 3.1.26.13 retroviral ribonuclease H -- 3.2.1.165 exo-1,4-b-D-glucosaminidase -- 3.2.1.167 baicalin-b-D-glucuronidase -- 3.2.1.168 hesperidin 6-O-a-L-rhamnosyl-b-Dglucosidase -- 3.2.2.27 uracil-DNA glycosylase -- 3.2.2.28 double-stranded uracil-DNA glycosylase -- 3.2.2.29 thymine-DNA glycosylase
    Abstract: Springer Handbook of Enzymes provides data on enzymes sufficiently well characterized. It offers concise and complete descriptions of some 5,000 enzymes and their application areas. Data sheets are arranged in their EC-Number sequence and the volumes themselves are arranged according to enzyme classes. This new, second edition reflects considerable progress in enzymology: many enzymes are newly classified or reclassified. Each entry is correlated with references and one or more source organisms. New datafields are created: application and engineering (for the properties of enzymes where the sequence has been changed). The total amount of material contained in the Handbook has more than doubled so that the complete second edition consists of 39 volumes as well as a Synonym Index. In addition, starting in 2009, all newly classified enzymes are treated in Supplement Volumes. Springer Handbook of Enzymes is an ideal source of information for researchers in biochemistry, biotechnology, organic and analytical chemistry, and food sciences, as well as for medicinal applications
    Pages: : digital.
    Edition: Second Edition.
    ISBN: 9783642362408
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  • 5
    Call number: ATV-BCH:146(2)/2
    Keywords: Enzymes
    Notes: Rev. ed. of: Enzyme handbook. 〈1990-1998 〉
    Pages: xxiv, 796 p.
    Edition: 2nd ed.
    ISBN: 3540413995
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    ATV-BCH:146(2)/2 departmental collection or stack – please contact the library
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  • 6
    Call number: ATV-BCH:146(2)/1
    Keywords: Enzymes
    Notes: Rev. ed. of: Enzyme handbook. 〈1990-1998 〉
    Pages: xxiv, 752 p.
    Edition: 2nd ed.
    ISBN: 3540410082
    Signatur Availability
    ATV-BCH:146(2)/1 departmental collection or stack – please contact the library
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  • 7
    Keywords: Germany ; TOOL ; PROTEIN ; COMPLEX ; COMPLEXES ; DNA ; INTERVENTION ; PREDICTION ; WEB ; QUESTIONNAIRE ; ANNOTATION ; GENOME DATABASE ; PROTEIN DATA ; RESOURCE ; SEQUENCE DATABASE
    Abstract: The Helmholtz Network for Bioinformatics (HNB) is a joint venture of eleven German bioinformatics research groups that offers convenient access to numerous bioinformatics resources through a single web portal. The 'Guided Solution Finder' which is available through the HNB portal helps users to locate the appropriate resources to answer their queries by employing a detailed, tree-like questionnaire. Furthermore, automated complex tool cascades ('tasks'), involving resources located on different servers, have been implemented, allowing users to perform comprehensive data analyses without the requirement of further manual intervention for data transfer and re-formatting. Currently, automated cascades for the analysis of regulatory DNA segments as well as for the prediction of protein functional properties are provided
    Type of Publication: Journal article published
    PubMed ID: 14734319
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  • 8
    Keywords: CANCER ; IN-VIVO ; POPULATION ; RISK ; GENE ; ASSOCIATION ; polymorphism ; POLYMORPHISMS ; BREAST-CANCER ; TRIAL ; HEALTH ; PROSPECTIVE COHORT ; SUPPLEMENTATION ; GLUTATHIONE-PEROXIDASE ; SUBSEQUENT RISK ; SERUM SELENIUM ; ERYTHROCYTE GPX ACTIVITY ; GLUTATHIONE-PEROXIDASE-1 ; NUTRITIONAL PREVENTION
    Abstract: Background: Evidence for an association between selenium status and prostate cancer risk is still inconclusive. Anticarcinogenic effects of selenium are supposedly mediated through cellular protective and redox properties of selenoenzymes in vivo. We evaluated the association between serum selenium status and prostate cancer risk in a population with relative low selenium concentrations considering effect modification by genetic variants in selenoprotein genes. Materials and Methods: A case-control study of 248 incident prostate cancer cases and 492 matched controls was nested within the EPIC-Heidelberg cohort. Baseline blood samples were analyzed for serum selenium and selenoprotein P concentrations and glutathione peroxidase activity. Genotyping was carried out for SEP15 (rs5859, rs540049), SEPP1 (rs3877899, rs7579), GPX1 (rs1050450), and GPX4 (rs713041). Conditional logistic regression was used to calculate adjusted odds ratios (OR) and 95% confidence intervals (95% CI). Results: The OR for prostate cancer was 0.89 (95% CI, 0.79-1.01) per 10 mu g/L increase of serum selenium concentration. This association was modified by rs1050450 (C〉T) in GPX1 (P-interaction = 0.03), with carriers of one or two T alleles having a significantly reduced OR of 0.87 (95% CI, 0.76-0.99). Furthermore, there was an association between rs7579 genotype in SEPP1 and prostate cancer risk (OR, 1.72; 95% CI, 0.99-2.98). Conclusions: Our results support a role of selenium and polymorphisms in selenoenzymes in prostate cancer etiology, which warrants confirmation in future studies. Impact: These findings might help to explain biological effects of selenium in prostate cancer development in order to overcome inconsistencies arising from former studies.
    Type of Publication: Journal article published
    PubMed ID: 20852007
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  • 9
    Keywords: MORTALITY ; BREAST-CANCER ; prevention ; HEALTH ; WOMEN ; COLORECTAL-CANCER ; METAANALYSIS ; COMMUNITY ; VITAMIN-D SUPPLEMENTATION ; CALCIUM SUPPLEMENTATION
    Abstract: BACKGROUND: Several observational studies assessed the relationship between serum 25-hydroxyvitamin D [25(OH)D] concentrations and the risk of cancer but results were inconclusive. METHODS: We measured 25(OH)D concentrations in a population-based cohort study of 9,949 men and women ages 50 to 74 years in Saarland, Germany. Comprehensively adjusted Cox regression models were applied to estimate HRs and 95% confidence intervals (CI) for the association between season-standardized 25(OH)D concentrations and total and site-specific cancer incidence. RESULTS: Overall, during a median of 8 years of follow-up, 873 subjects developed cancer; the most common being prostate (171), breast (137), lung (136), and colorectal (136) cancer. Low season-standardized 25(OH)D (〈30, 35, 40, or 36 nmol/L in winter, spring, summer, and autumn, respectively) was neither significantly associated with total cancer incidence (HR, 1.10; 95% CI, 0.93-1.30) nor with site-specific cancer incidence. However, a significantly increased overall cancer risk was observed for low 25(OH)D among men, nonobese subjects and subjects reporting low fish consumption and for high 25(OH)D in nonsmokers and nonobese subjects. Accordingly, restricted cubic splines to investigate dose-response relationships curves showed an inverse association of 25(OH)D levels and total cancer risk in men but not in women. CONCLUSIONS: 25(OH)D concentrations were significantly associated with overall cancer incidence in subgroups of this large cohort from Germany. No significant association was observed with site-specific cancers but this could be due to a limited statistical power for these endpoints. Impact: Further research should clarify whether and to what extent specific risk groups might profit from vitamin D supplementation. Cancer Epidemiol Biomarkers Prev; 22(5); 905-16. (c)2013 AACR.
    Type of Publication: Journal article published
    PubMed ID: 23462913
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  • 10
    Keywords: GENE ; TRIAL ; prevention ; PROSTATE-CANCER ; SUPPLEMENTATION ; SELENOPROTEIN-P ; adenoma ; SERUM SELENIUM ; VITAMIN ; HUMAN HEALTH
    Abstract: Suboptimal intakes of the micronutrient selenium (Se) are found in many parts of Europe. Low Se status may contribute to colorectal cancer (CRC) development. We assessed Se status by measuring serum levels of Se and Selenoprotein P (SePP) and examined the association with CRC risk in a nested case-control design (966 CRC cases; 966 matched controls) within the European Prospective Investigation into Cancer and Nutrition. Se was measured by total reflection X-ray fluorescence and SePP by immunoluminometric sandwich assay. Multivariable incidence rate ratios (IRRs) and 95% confidence intervals (CIs) were calculated using conditional logistic regression. Respective mean Se and SePP levels were 84.0 mug/L and 4.3 mg/L in cases and 85.6 mug/L and 4.4 mg/L in controls. Higher Se concentrations were associated with a non-significant lower CRC risk (IRR = 0.92, 95% CI: 0.82-1.03 per 25 mug/L increase). However, sub-group analyses by sex showed a statistically significant association for women (p(trend) = 0.032; per 25 mug/L Se increase, IRR = 0.83, 95% CI: 0.70-0.97) but not for men. Higher SePP concentrations were inversely associated with CRC risk (p(trend) = 0.009; per 0.806 mg/L increase, IRR = 0.89, 95% CI: 0.82-0.98) with the association more apparent in women (p(trend) = 0.004; IRR = 0.82, 95% CI: 0.72-0.94 per 0.806 mg/L increase) than men (p(trend) = 0.485; IRR = 0.98, 95% CI: 0.86-1.12 per 0.806 mg/L increase). The findings indicate that Se status is suboptimal in many Europeans and suggest an inverse association between CRC risk and higher serum Se status, which is more evident in women.
    Type of Publication: Journal article published
    PubMed ID: 25042282
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