Class 2 Transferases I: EC 2.1.1: Springer Handbook of Enzymes, cartea 28
Antje Chang Editat de Dietmar Schomburg, Ida Schomburgen Limba Engleză Paperback – 23 sep 2014
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
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Specificații
ISBN-13: 9783642421617
ISBN-10: 364242161X
Pagini: 680
Ilustrații: XXIV, 656 p.
Dimensiuni: 155 x 235 x 36 mm
Greutate: 0.94 kg
Ediția:2nd ed. 2006
Editura: Springer Berlin, Heidelberg
Colecția Springer
Seria Springer Handbook of Enzymes
Locul publicării:Berlin, Heidelberg, Germany
ISBN-10: 364242161X
Pagini: 680
Ilustrații: XXIV, 656 p.
Dimensiuni: 155 x 235 x 36 mm
Greutate: 0.94 kg
Ediția:2nd ed. 2006
Editura: Springer Berlin, Heidelberg
Colecția Springer
Seria Springer Handbook of Enzymes
Locul publicării:Berlin, Heidelberg, Germany
Public țintă
ResearchCuprins
Nicotinamide N-methyltransferase.- Guanidinoacetate N-methyltransferase.- Thetin-homocysteine S-methyltransferase.- Acetylserotonin O-methyltransferase.- Betaine-homocysteine S-methyltransferase.- Catechol O-methyltransferase.- Nicotinate N-methyltransferase.- Histamine N-methyltransferase.- Thiol S-methyltransferase.- Homocysteine S-methyltransferase.- Magnesium protoporphyrin IX methyltransferase.- Methionine S-methyltransferase.- Methionine synthase.- 5-Methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase.- Fatty-acid O-methyltransferase.- Methylene-fatty-acyl-phospholipid synthase.- Phosphatidylethanolamine N-methyltransferase.- Polysaccharide O-methyltransferase.- Trimethylsulfonium-tetrahydrofolate N-methyltransferase.- Glycine N-methyltransferase.- Methylamine-glutamate N-methyltransferase.- Carnosine N-methyltransferase.- Protein-arginine N-methyltransferase.- Protein-?-glutamate O-methyltransferase.- Phenol O-methyltransferase.- Iodophenol O-methyltransferase.- Tyramine N-methyltransferase.- Phenylethanolamine N-methyltransferase.- tRNA (cytosine-5-)-methyltransferase.- tRNA (purine-2- or -6-)-methyltransferase.- tRNA (guanine-N1-)-methyltransferase.- tRNA (guanine-N2-)-methyltransferase.- tRNA (guanine-N7-)-methyltransferase.- tRNA guanosine-2?-O-methyltransferase.- tRNA (uracil-5-)-methyltransferase.- tRNA (adenine-N1-)-methyltransferase.- DNA (cytosine-5-)-methyltransferase.- O-Demethylpuromycin O-methyltransferase.- Inositol 3-O-methyltransferase.- Inositol 1-methyltransferase.- Sterol 24-C-methyltransferase.- Luteolin O-methyltransferase.- Histone-lysine N-methyltransferase.- Dimethylhistidine N-methyltransferase.- Thymidylate synthase.- Isoflavone 4?-O-methyltransferase.- Indolepyruvate C-methyltransferase.- rRNA(adenine-N6-)-methyltransferase.- Amine N-methyltransferase.- Loganate O-methyltransferase.- rRNA (guanine-N1-)-methyltransferase.- rRNA (guanine-N2-)-methyltransferase.- Putrescine N-methyltransferase.- Deoxycytidylate C-methyltransferase.- tRNA (adenine-N6-)-methyltransferase.- mRNA (guanine-N7-)-methyltransferase.- mRNA (nucleoside-2?-O-)-methyltransferase.- mRNA (adenosine-2?-O-)-methyltransferase.- [Cytochrome c]-lysine N-methyltransferase.- Calmodulin-lysine N-methyltransferase.- tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase.- mRNA (2?-O-methyladenosine-N6-)- methyltransferase.- Methylated-DNA-[protein]-cysteine S-methyltransferase.- 3-Demethylubiquinone-9 3-O-methyltransferase.- Licodione 2?-O-methyltransferase.- rRNA (adenosine-2?-O-)-methyltransferase.- Thiopurine S-methyltransferase.- Caffeate O-methyltransferase.- 5-Hydroxyfuranocoumarin 5-O-methyltransferase.- 8-Hydroxyfuranocoumarin 8-O-methyltransferase.- Phosphatidyl-N-methylethanolamine N-methyltransferase.- Site-specific DNA-methyltransferase (adenine-specific).- Site-specific DNA-methyltransferase (cytosine-specific).- Methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing).- Apigenin 4?-O-methyltransferase.- Quercetin 3-O-methyltransferase.- Protein-L-isoaspartate (D-aspartate) O-methyltransferase.- Isoorientin 3?-O-methyltransferase.- Cyclopropane-fatty-acyl-phospholipid synthase.- Protein-glutamate O-methyltransferase.- Nicotine N-methyltransferase.- 3-Methylquercitin 7-O-methyltransferase.- 3,7-Dimethylquercitin 4?-O-methyltransferase.- Methylquercetagetin 6-O-methyltransferase.- Protein-histidine N-methyltransferase.- Tetrahydromethanopterin S-methyltransferase.- Pyridine N-methyltransferase.- 8-Hydroxyquercitin 8-O-methyltransferase.-Tetrahydrocolumbamine 2-O-methyltransferase.- Methanol-5-hydroxybenzimidazolylcobamide Co-methyltransferase.- Isobutyraldoxime O-methyltransferase.- Bergaptol O-methyltransferase.- Xanthotoxol O-methyltransferase.- 11-O-Demethyl-17-O-deacetylvindoline O-methyltransferase.- Tocopherol O-methyltransferase.- Thioether S-methyltransferase.- 3-Hydroxyanthranilate 4-C-methyltransferase.- Diphthine synthase.- 16-Methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase.- Protein-S-isoprenylcysteine O-methyltransferase.- Macrocin O-methyltransferase.- Demethylmacrocin O-methyltransferase.- Phosphoethanolamine N-methyltransferase.- Caffeoyl-CoA O-methyltransferase.- N-Benzoyl-4-hydroxyanthranilate 4-O-methyltransferase.- Tryptophan 2-C-methyltransferase.- Uroporphyrin-III C-methyltransferase.- 6-Hydroxymellein O-methyltransferase.- Demethylsterigmatocystin 6-O-methyltransferase.- Sterigmatocystin 7-O-methyltransferase.- Anthranilate N-methyltransferase.- Glucuronoxylan 4-O-methyltransferase.- Site-specific DNA-methyltransferase (cytosine-N4-specific).- Hexaprenyldihydroxybenzoate methyltransferase.- (RS)-1-Benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase.- 3?-Hydroxy-N-methyl-(S)-coclaurine 4?-O-methyltransferase.- (S)-Scoulerine 9-O-methyltransferase.- Columbamine O-methyltransferase.- 10-Hydroxydihydrosanguinarine 10-O-methyltransferase.- 12-Hydroxydihydrochelirubine 12-O-methyltransferase.- 6-O-Methylnorlaudanosoline 5?-O-methyltransferase.- (S)-Tetrahydroprotoberberine N-methyltransferase.- [Cytochrome c]-methionine S-methyltransferase.- [Cytochrome c]-arginine N-methyltransferase.- Histone-arginine N-methyltransferase.- [Myelin basic protein]-arginine N-methyltransferase.- [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase.- (RS)-Norcoclaurine6-O-methyltransferase.- Inositol 4-methyltransferase.- Precorrin-2 C20-methyltransferase.- Precorrin-3B C17-methyltransferase.- Precorrin-6Y C5,15-methyltransferase (decarboxylating).- Precorrin-4 C11-methyltransferase.- myo-Inositol 6-O-methyltransferase.- [Methionine synthase]-cobalamin methyltransferase (cob(II)alamin reducing).- Chlorophenol O-methyltransferase.- Arsenite methyltransferase.- Methylarsonite methyltransferase.- 3?-Demethylstaurosporine O-methyltransferase.- (S)-Coclaurine-N-methyltransferase.- Jasmonate O-methyltransferase.- Cycloartenol 24-C-methyltransferase.- 24-Methylenesterol C-methyltransferase.- Trans-aconitate 2-methyltransferase.- Trans-aconitate 3-methyltransferase.- (Iso)eugenol O-methyltransferase.- Corydaline synthase.- Thymidylate synthase (FAD).- Myricetin O-methyltransferase.- Isoflavone 7-O-methyltransferase.- Cobalt-factor II C20-methyltransferase.- Precorrin-6A synthase (deacetylating).
Textul de pe ultima copertă
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
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
Caracteristici
Offers concise and complete description of about 5,000 enzymes sufficiently well characterized as well as their application in analytical, synthetic and biotechnology processes, in food industry, and for medicinal treatments This new, second edition reflects considerable progress in enzymology: many of the enzymes have either been newly classified, or re-classified Content in this new edition has doubled: now consists of 39 volumes as well as a synonym index Starting in 2009 all newly classified enzymes are treated in the Supplement Volumes Available in print as well as online