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Class 2 ø Transferases VI [electronic resource] : EC 2.5.1.312.6.1.57 / edited by Dietmar Schomburg, Ida Schomburg, Antje Chang.

Por: Colaborador(es): Tipo de material: TextoTextoSeries Springer Handbook of Enzymes ; 34 | Springer Handbook of Enzymes ; 34Editor: Berlin, Heidelberg : Springer Berlin Heidelberg, 2007Edición: Second EditionDescripción: XXII, 622 p. online resourceTipo de contenido:
  • text
Tipo de medio:
  • computer
Tipo de soporte:
  • online resource
ISBN:
  • 9783540497554
Trabajos contenidos:
  • SpringerLink (Online service)
Tema(s): Formatos físicos adicionales: Sin títuloClasificación CDD:
  • 572 23
Clasificación LoC:
  • QH345
  • QD415-436
Recursos en línea:
Contenidos:
Springer eBooksResumen: 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.
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Di-trans,poly-cis-decaprenylcistransferase -- Phytoene synthase -- trans-Pentaprenyltranstransferase -- Tryptophan dimethylallyltransferase -- Aspulvinone dimethylallyltransferase -- Trihydroxypterocarpan dimethylallyltransferase -- Leukotriene-C4 synthase -- Isonocardicin synthase -- 4-Hydroxybenzoate nonaprenyltransferase -- Aristolochene synthase -- Phosphoglycerol geranylgeranyltransferase -- Geranylgeranylglycerol-phosphate geranylgeranyltransferase -- Nicotianamine synthase -- Homospermidine synthase -- Homospermidine synthase (spermidine-specific) -- Deoxyhypusine synthase -- Cysteine synthase -- Cystathionine ?-synthase -- O-Acetylhomoserine aminocarboxypropyltransferase -- Zeatin 9-aminocarboxyethyltransferase -- ?-Pyrazolylalanine synthase -- l-Mimosine synthase -- Uracilylalanine synthase -- 3-Deoxy-7-phosphoheptulonate synthase -- 3-Deoxy-8-phosphooctulonate synthase -- N-Acetylneuraminate synthase -- N-Acylneuraminate-9-phosphate synthase -- Protein farnesyltransferase -- Protein geranylgeranyltransferase type I -- Protein geranylgeranyltransferase type II -- Hydroxymethylbilane synthase -- Chlorophyll synthase -- Adenosyl-fluoride synthase -- 2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase -- Aspartate transaminase -- Alanine transaminase -- Cysteine transaminase -- Glycine transaminase -- Tyrosine transaminase -- Leucine transaminase -- Kynurenine-oxoglutarate transaminase -- 2,5-Diaminovalerate transaminase -- Histidinol-phosphate transaminase -- D-Aspartate transaminase -- Acetylornithine transaminase -- Alanine-oxo-acid transaminase -- Ornithine-oxo-acid transaminase -- Asparagine-oxo-acid transaminase -- Glutamine-pyruvate transaminase -- Glutamine-fructose-6-phosphate transaminase (isomerizing) -- Succinyldiaminopimelate transaminase -- ?-Alanine-pyruvate transaminase -- 4-Aminobutyrate transaminase -- Tyrosine-pyruvate transaminase -- D-Alanine transaminase -- (S)-3-Amino-2-methylpropionate transaminase -- 4-Hydroxyglutamate transaminase -- Diiodotyrosine transaminase -- Thyroxine transaminase -- Thyroid-hormone transaminase -- Tryptophan transaminase -- Tryptophan-phenylpyruvate transaminase -- Diamine transaminase -- Pyridoxamine-pyruvate transaminase -- Pyridoxamine-oxaloacetate transaminase -- Valine-3-methyl-2-oxovalerate transaminase -- dTDP-4-Amino-4,6-dideoxy-D-glucose transaminase -- UDP-2-Acetamido-4-amino-2,4,6-trideoxyglucose transaminase -- Glycine-oxaloacetate transaminase -- l-Lysine 6-transaminase -- 2-Aminoethylphosphonate-pyruvate transaminase -- Histidine transaminase -- 2-Aminoadipate transaminase -- (R)-3-Amino-2-methylpropionate-pyruvate transaminase -- D-Methionine-pyruvate transaminase -- Branched-chain-amino-acid transaminase -- Aminolevulinate transaminase -- Alanine-glyoxylate transaminase -- Serine-glyoxylate transaminase -- Diaminobutyrate-pyruvate transaminase -- Alanine-oxomalonate transaminase -- 5-Aminovalerate transaminase -- Dihydroxyphenylalanine transaminase -- Glutamine-scyllo-inositol transaminase -- Serine-pyruvate transaminase -- Phosphoserine transaminase -- Glutamate synthase -- Pyridoxamine-phosphate transaminase -- Taurine-2-oxoglutarate transaminase -- 1D-1-Guanidino-3-amino-1,3-dideoxy-scyllo-inositol transaminase -- Aromatic-amino-acid transaminase.

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.

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