By Professor Dietmar Schomburg, Dr. Ida Schomburg, Dr. Antje Chang (eds.)

Springer instruction manual of Enzymes offers information on enzymes sufficiently good characterised. It deals concise and entire descriptions of a few 5,000 enzymes and their program parts. information sheets are prepared of their EC-Number series and the volumes themselves are prepared in line with enzyme classes.

This new, moment version displays huge growth in enzymology: many enzymes are newly labeled or reclassified. every one access is correlated with references and a number of resource organisms. New datafields are created: program and engineering (for the homes of enzymes the place the series has been changed). the entire quantity of fabric inside the guide has greater than doubled in order that the total moment variation involves 39 volumes in addition to a Synonym Index. furthermore, beginning in 2009, all newly categorized enzymes are handled in complement Volumes.

Springer guide of Enzymes is a perfect resource of knowledge for researchers in biochemistry, biotechnology, natural and analytical chemistry, and nutrition sciences, in addition to for medicinal applications.

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2, 3, 6, 7, 11, 14] P ? e. e. e. e. e. e. e. e. e. ) [2, 3, 5, 6, 7, 11, 13, 14] ? e. : A new caffeine biosynthetic pathway in tea leaves: utilisation of adenosine released from the S-adenosyl-l-methionine cycle. : Cloning, expression, crystallization and preliminary x-ray analysis of the XMT and DXMT N-methyltransferases from Coffea canephora (robusta). Acta Crystallogr. Sect. ). : 7-Methylxanthine methyltransferase of coffee plants. Gene isolation and enzymatic properties. J. Biol. : Substrate specificity of N-methyltransferase involved in purine alkaloids synthesis is dependent upon one amino acid residue of the enzyme.

G. : Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase. Appl. Environ. : Extreme halophiles synthesize betaine from glycine by methylation. J. Biol. : Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. : Identification of glycine betaine as compatible solute in Synechococcus sp. WH8102 and characterization of its N-methyltransferase genes involved in betaine synthesis.

J. Biol. : Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. : Effects of substrate and potassium on the betaine-synthesizing enzyme glycine sarcosine dimethylglycine N-methyltransferase from a halophilic methanoarchaeon Methanohalophilus portucalensis. Res. ) [12] P ? ) [5, 12] P ? 3 <1> (<1> assay at [1]) [1] Temperature optimum ( C) 20 <2> (<2> assay at [4]) [4] 27 <1, 4> (<1,4> assay at [1,10]) [1, 10] 30 <2> (<2> assay at [7]) [7] 37 <3> (<3> assay at [11]) [11] 4 Enzyme Structure Molecular weight 67000 <2> (<2> about, gel filtration [7]) [7] 69000 <4> (<4> recombinant isozyme XMT1, gel filtration [10]) [10] 80000 <5> (<5> about, recombinant enzyme, gel filtration [2]) [2] Subunits ?

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