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140122 ||| eng |
| 020 |
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|a 9783642589485
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| 100 |
1 |
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|a Schomburg, Dietmar
|e [editor]
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| 245 |
0 |
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|a Enzyme Handbook
|h Elektronische Ressource
|b Volume 15: First Supplement Part 1 Class 3: Hydrolases
|c edited by Dietmar Schomburg, Dörte Stephan
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| 250 |
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|a 1st ed. 1998
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| 260 |
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|a Berlin, Heidelberg
|b Springer Berlin Heidelberg
|c 1998, 1998
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| 300 |
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|a XIII, 775 p
|b online resource
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| 505 |
0 |
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|a 1,3-alpha-L-Fucosidase -- 2-Deoxyglucosidase -- Mannosyl-oligosaccharide 1,2-alpha-mannosidase -- Mannosyl-oligosaccharide 1,3–1,6-alpha-mannosidase -- Branched-dextran exo-1,2-alpha-glucosidase -- Glucan 1,4-alpha-maltotriohydrolase -- Amygdalin beta-glucosidase -- Prunasin beta-glucosidase -- Vicianin beta-glucosidase -- Oligoxyloglucan beta-glycosidase -- Polymannuronate hydrolase -- Maltose-6’-phosphate glucosidase -- Endoglycosylceramidase -- 3-Deoxy-2-octulosonidase -- Raucaffricine beta-glucosidase -- Coniferin beta-glucosidase -- 1,6-alpha-L-Fucosidase -- Glycyrrhizinate beta-glucuronidase -- Endo-alpha-sialidase -- Glycoprotein endo-alpha-1,2-mannosidase -- Xylan alpha-1,2-glucuronosidase -- Chitosanase -- Glucan 1,4-alpha-maltohydrolase -- Difructose-anhydride synthase -- Neopullulanase -- Glucuronoarabinoxylan endo-1,4-beta-xylanase -- Mannan exo-1,2–1,6-alpha-mannosidase -- Anhydrosialidase -- DNA-3-methyladenine glycosidase I -- DNA-3-methyladenine glycosidase II --
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| 505 |
0 |
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|a Acetoxybutynylbithiophene deacetylase -- Acetylsalicylate deacetylase -- Methylumbelliferyl-acetate deacetylase -- 2-Pyrone-4,6-dicarboxylate lactonase -- N-Acetylgalactosaminoglycan deacetylase -- Juvenile-hormone esterase -- Bis(2-ethylhexyl)phthalate esterase -- Protein-glutamate methylesterase -- 11-cis-Retinyl-palmitate hydrolase -- all-trans-Retinyl-palmitate hydrolase -- L-Rhamnono-1,4-lactonase -- 5-(3,4-Diacetoxybut-1-ynyl)-2,2’-bithiophene deacetylase -- Fatty-acyl-ethyl-ester synthase -- Xylono-1,4-lactonase -- N-Acetylglucosaminylphosphatidylinositol deacetylase -- Cetraxate benzylesterase -- Ubiquitin thiolesterase -- [Citrate-(pro-3S)-lyase] thiolesterase -- (S)-Methylmalonyl-CoA hydrolase -- ADP-dependent short-chain-acyl-CoA hydrolase -- ADP-dependent medium-chain-acyl-CoA hydrolase -- Acyl-CoA hydrolase -- [3-Methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphatase -- Myosin-light-chain-phosphatase -- Fructose-2,6-bisphosphate 6-phosphatase --
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| 505 |
0 |
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|a Caldesmon-phosphatase -- Inositol-1,4,5-trisphosphate 5-phosphatase -- Inositol-1,4-bisphosphate 1-phosphatase -- Sugar-terminal-phosphatase -- Alkylacetylglycerophosphatase -- Phosphoenolpyruvate phosphatase -- Inositol-1,4,5-trisphosphate 1-phosphatase -- Inositol-1,3,4,5-tetrakisphosphate 3-phosphatase -- 2-Carboxy-D-arabinitol-1-phosphatase -- Phosphatidylinositol 3-phosphatase -- Inositol-1,3-bisphosphate 3-phosphatase -- Inositol-3,4-bisphosphate 4-phosphatase -- Glycerophosphodiester phosphodiesterase -- Variant-surface-glycoprotein phospholipase C -- Dolichyl-phosphate-glucose phosphodiesterase -- Dolichyl-phosphate-mannose phosphodiesterase -- Glycoprotein phospholipase D -- Glucose-1-phospho-D-mannosylglycoprotein phosphodiesterase -- Monomethyl-sulfatase -- D-Lactate-2-sulfatase -- Glucuronate-2-sulfatase -- Aryldialkylphosphatase -- Diisopropyl-fluorophosphatase -- Deoxyribonuclease X -- Ribonuclease IX -- tRNA-intron endonuclease -- rRNA endonuclease --
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| 505 |
0 |
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|a rRNA N-glycosidase -- Formamidopyrimidine-DNA glycosidase -- ADP-ribosyl-[dinitrogen reductase] hydrolase -- Leukotriene-A4 hydrolase -- Hepoxilin-epoxide hydrolase -- Methionyl aminopeptidase -- D-Stereospecific aminopeptidase -- Aminopeptidase Ey -- Non-stereospecific dipeptidase -- Cytosol nonspecific dipeptidase -- Membrane dipeptidase -- beta-Ala-His dipeptidase -- Tripeptidyl-peptidase l -- Tripeptidyl-peptidase ll -- X-Pro dipeptidyl-peptidase -- Peptidyl-dipeptidase B -- Peptidyl-dipeptidase Dcp -- Carboxypeptidase C -- Carboxypeptidase D -- Glutamate carboxypeptidase -- Carboxypeptidase M -- Muramoyltetrapeptide carboxypeptidase -- Zinc D-Ala-D-Ala carboxypeptidase -- Carboxypeptidase A2 -- Membrane Pro-X carboxypeptidase -- Tubulinyl-Tyr carboxypeptidase -- Carboxypeptidase T -- Carboxypeptidase Taq -- beta-Aspartyl-peptidase -- Pyroglutamyl-peptidase II -- N-Formylmethionyl-peptidase -- Pteroylpoly-gamma-glutamate carboxypeptidase -- gamma-Glu-X carboxypeptidase --
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| 505 |
0 |
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|a Acylmuramoyl-Ala peptidase -- gamma-D-Glutamyl-meso-diaminopimelate peptidase I -- Endopeptidase La -- gamma-Renin -- Venombin AB -- Leucyl endopeptidase -- Tryptase -- Scutelarin -- Kexin -- Subtilisin -- Oryzin -- Endopeptidase K -- Thermomycolin -- Thermitase -- Endopeptidase So -- t-Plasminogen activator -- Protein C (activated) -- Pancreatic endopeptidase E -- Pancreatic elastase II -- IgA-specific serine endopeptidase -- u-Plasminogen activator -- Venombin A -- Furin -- Myeloblastin -- Semenogelase -- Granzyme A -- Granzyme B -- Streptogrisin A -- Streptogrisin B -- Glutamyl endopeptidase II -- Oligopeptidase B -- Limulus clotting factor C -- Limulus clotting factor B -- Limulus clotting enzyme -- Omptin -- Repressor LexA -- Signal peptidase I -- Togavirin -- Flavivirin -- Endopeptidase Clp -- Proprotein convertase 1 -- Proprotein convertase 2
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| 653 |
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|a Biochemistry, general
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| 653 |
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|a Biotechnology
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| 653 |
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|a Biotechnology
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| 653 |
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|a Biochemistry
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| 700 |
1 |
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|a Stephan, Dörte
|e [editor]
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| 041 |
0 |
7 |
|a eng
|2 ISO 639-2
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| 989 |
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|b SBA
|a Springer Book Archives -2004
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| 856 |
4 |
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|u https://doi.org/10.1007/978-3-642-58948-5?nosfx=y
|x Verlag
|3 Volltext
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| 082 |
0 |
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|a 572
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| 520 |
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|a Today, as the large international genome sequence projects are gaining a great amount of public atte_ntion and huge sequence data bases are created it be comes more and more obvious that we are very limited in our ability to access functional data for the gene products - the proteins, in particular for enzymes. Those data are inherently very difficult to collect, interpret and standardize as they are highly distributed among journals from different fields and are often sub ject to experimental conditions. Nevertheless a systematic collection is essential for our interpretation of the genome information and more so for possible appli cations of this knowledge in the fields of medicine, agriculture, etc .. Recent pro gress on enzyme immobilization, enzyme production, enzyme inhibition, coen zyme regeneration and enzyme engineering has opened up fascinating new fields for the potential application of enzymes in a large range of different areas. It is the functional profile of an enzyme that enables a biologist or physician to analyse a metabolic pathway and its disturbance; it is the substrate specificity of an enzyme which tells an analytical biochemist how to design an assay; it is the stability, specificity and efficiency of an enzyme which determines its usefulness in the biotechnical transformation of a molecule. And the sum of all these data will have to be considered when the deSigner of artificial biocatalysts has to choose the optimum prototype to start with
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