Schomburg / Stephan | Enzyme Handbook 16 | Buch | 978-3-540-64384-5 | www.sack.de

Buch, Englisch, 719 Seiten, Book, Format (B × H): 155 mm x 235 mm, Gewicht: 1620 g

Schomburg / Stephan

Enzyme Handbook 16

First Supplement Part 2 Class 3: Hydrolases
1. Auflage 1998
ISBN: 978-3-540-64384-5
Verlag: Springer-Verlag GmbH

First Supplement Part 2 Class 3: Hydrolases

Buch, Englisch, 719 Seiten, Book, Format (B × H): 155 mm x 235 mm, Gewicht: 1620 g

ISBN: 978-3-540-64384-5
Verlag: Springer-Verlag GmbH


Today, as the large international genome sequence projects are gaining a great amount of public attention 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 differentfields 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 ofan enzyme that enables a biologist or physician to analyse a metabolicpathwayand its disturbance; it is the substrate specificityof an enzyme which tells an analytical biochemisthow to design an assay; it is the stability, specificityand efficiencyofan enzyme which determines its usefulness in the biotechnicaltransformation ofa molecule. Andthe sumofallthese data will have to be considered when the designerofartificial biocatalysts has to choose the optimum prototype to start with.

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Cathepsin T.- Glycyl endopeptidase.- Cancer procoagulant.- Cathepsin S.- Picornain 3C.- Picornain 2A.- Caricain.- Ananain.- Stem bromelain.- Fruit bromelain.- Legumain.- Histolysain.- Interleukin 1beta converting enzyme.- Gingipain R.- Retropepsin.- Pro-opiomelanocortin converting enzyme.- Aspergillopepsin I.- Aspergillopepsin II.- Penicillopepsin.- Rhizopuspepsin.- Endothiapepsin.- Mucorpepsin.- Candidapepsin.- Saccharopepsin.- Rhodotorulapepsin.- Physaropepsin.- Acrocylindropepsin.- Polyporopepsin.- Pycnoporopepsin.- Scytalidopepsin A.- Scytalidopepsin B.- Xanthomonapepsin.- Cathepsin E.- Barrierpepsin.- Signal peptidase II.- Pseudomonapepsin.- Plasmepsin I.- Plasmepsin II.- Stromelysin 1.- Meprin A.- Procollagen C-endopeptidase.- Peptidyl-Lys metalloendopeptidase.- Astacin.- Stromelysin 2.- Matrilysin.- Gelatinase A.- Aeromonolysin.- Pseudolysin.- Thermolysin.- Bacillolysin.- Aureolysin.- Coccolysin.- Mycolysin.- beta-Lytic metalloendopeptidase.- Peptidyl-Asp metalloendopeptidase.- Neutrophil collagenase.- Gelatinase B.- Leishmanolysin.- Saccharolysin.- Autolysin.- Deuterolysin.- Serralysin.- Atrolysin B.- Atrolysin C.- Atroxase.- Atrolysin E.- Atrolysin F.- Adamalysin.- Horrilysin.- Ruberlysin.- Bothropasin.- Bothrolysin.- Ophiolysin.- Trimerelysin I.- Trimerelysin II.- Mucrolysin.- Pitrilysin.- Insulysin.- O-Sialoglycoprotein endopeptidase.- Russellysin.- Mitochondrial intermediate peptidase.- Dactylysin.- Nardilysin.- Magnolysin.- Meprin B.- Mitochondrial processing peptidase.- Macrophage elastase.- Choriolysin L.- Choriolysin H.- Tentoxilysin.- Bontoxilysin.- Oligopeptidase A.- Endothelin-converting enzyme 1.- Fibrolase.- Jararhagin.- Thermopsin.- Multicatalytic endopeptidase complex.- N-Carbamoylputrescine amidase.- Allophanate hydrolase.- Long-chain-fatty-acyl-glutamate deacylase.- N,N-Dimethylformamidase.- Tryptophanamidase.- N-Benzyloxycarbonylglycine hydrolase.- N-Carbamoylsarcosine amidase.- N-(Long-chain-acyl)ethanolamine deacylase.- Mimosinase.- Acetylputrescine deacetylase.- 4-Acetamidobutyrate deacetylase.- Nalpha-Benzyloxycarbonylleucine hydrolase.- Theanine hydrolase.- 2-(Hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase.- 4-Methyleneglutaminase.- N-Formylglutamate deformylase.- Glycosphingolipid deacylase.- Aculeacin-A deacylase.- N-Feruloylglycine deacylase.- D-Benzoylarginine-4-nitroanilide amidase.- Carnitinamidase.- Chenodeoxycholoyltaurine hydrolase.- Urethanase.- 2,5-Dioxopiperazine hydrolase.- N-Methylhydantoinase (ATP-hydrolysing).- Guanidinopropionase.- Dimethylargininase.- Ureidoglycolate hydrolase.- Diguanidinobutanase.- Methenyltetrahydromethanopterin cyclohydrolase.- S-Adenosylhomocysteine deaminase.- Cyanoalanine nitrilase.- Arylacetonitrilase.- Bromoxynil nitrilase.- Guanosine-5’-triphosphate,3’-diphosphate pyrophosphatase.- Bis(5’-nucleosyl)-tetraphosphatase (symmetrical).- Guanosine-diphosphatase.- Dolichyldiphosphatase.- Oligosaccharide-diphosphodolichol pyrophosphatase.- beta-Diketone hydrolase.- 2,6-Dioxo-6-phenylhexa-3-enoate hydrolase.- 2-Hydroxymuconate-semialdehyde hydrolase.- Cyclohexane-1,3-dione hydrolase.- Haloalkane dehalogenase.- 4-Chlorobenzoate dehalogenase.- Trithionate hydrolase.



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