By Professor Dietmar Schomburg, Dr. Ida Schomburg, Dr. Antje Chang (eds.)
Springer guide of Enzymes presents info on enzymes sufficiently good characterised. It deals concise and whole descriptions of a few 5,000 enzymes and their program parts. info sheets are prepared of their EC-Number series and the volumes themselves are prepared based on enzyme classes.
This new, moment variation displays substantial growth in enzymology: many enzymes are newly categorized or reclassified. each one access is correlated with references and a number of resource organisms. New datafields are created: software and engineering (for the houses of enzymes the place the series has been changed). the full volume of fabric inside the guide has greater than doubled in order that the full moment variation contains 39 volumes in addition to a Synonym Index. moreover, beginning in 2009, all newly labeled 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 nutrients sciences, in addition to for medicinal applications.
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Additional resources for Class 2 Transferases VIII: EC 184.108.40.206–220.127.116.11
Glutamine transaminase from brain tissue. Further studies on kinetic properties and specificity of the enzyme. Eur. J. : Identity of rat kidney histidine-pyruvate aminotransferase with glutamine-oxo acid aminotransferase. Biochem. : Purification of soluble and mitochondrial glutamine transaminase K from rat kidney. Use of a sensitive assay involving transamination between l-phenylalanine and a-keto-g-methiolbutyrate. Anal. : Glutamine transaminase K from rat kidney. : The transamination of lcystathionine, l-cystine and related compounds by a bovine kidney transaminase.
7,8-Diaminopelargonic acid aminotransferase. : The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation. : Purification and preliminary x-ray crystallographic studies of recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli. Acta Crystallogr. Sect. : Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes. J. Mol. 63 Systematic name l-kynurenine:glyoxylate aminotransferase (cyclizing) Recommended name kynurenine-glyoxylate transaminase Synonyms aminotransferase, kynurenine-glyoxylate Additional information (<1,2> cf.
1> )  P 3-indole-2-oxopropanoate + l-phenylalanine S l-tryptophan + oxaloacetate <1> (<1> reverse reaction, 77% activity with respect to l-phenylalanine ) (Reversibility: r <1> )  P 3-indole-2-oxopropanoate + l-aspartate S b-methyl-dl-aspartate + l-phenylpyruvate <1> (<1> 2% activity with respect to l-aspartate ) (Reversibility: ? <1> )  P 3-methyl-2-oxobutanedioate + l-phenylalanine S indolepyruvate + l-aspartate <1> (<1> 10% activity with respect to lphenylpyruvate ) (Reversibility: ?
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