By Professor Dietmar Schomburg, Dr. Ida Schomburg (eds.)
Springer guide of Enzymes presents facts on enzymes sufficiently good characterised. It bargains concise and whole descriptions of a few 5,000 enzymes and their software parts. info sheets are prepared of their EC-Number series and the volumes themselves are prepared in response to enzyme classes.
This new, moment version displays substantial development in enzymology: many enzymes are newly categorised or reclassified. every 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 complete quantity of fabric inside the guide has greater than doubled in order that the total moment variation contains 39 volumes in addition to a Synonym Index. furthermore, beginning in 2009, all newly categorized enzymes are taken care of 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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Extra info for Springer Handbook of Enzymes: Class 1 · Oxidoreductases IX EC 1.6–1.8
Studies on the mitochondrial energy-linked pyridine nucleotide transhydrogenase. : Oxidative phosphorylation in Micrococcus dentrificans. II. The properties of pyridine nucleotide transhydrogenase. Biochim. Biophys. : Membrane-bound pyridine dinucleotide transhydrogenases. : Transhydrogenases linked to pyridine nucleotides. Pyridine Nucleotide Coenzymes, Chem. Biochem. Med. : Mitochondrial nicotinamide nucleotide transhydrogenase. , Dallner, G. : Pyridine nucleotide transhydrogenase. VIII. Properties of the transhydrogenase reactions of an enzyme complex isolated from beef heart mitochondria.
Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties. Biochim. Biophys. : The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase. : Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum. Biochim. Biophys. : The presence of an aqueous cavity in the protonpumping pathway of the pyridine nucleotide transhydrogenase of Escherichia coli is suggested by the reaction of the enzyme with sulfhydryl inhibitors.
Biochim. Biophys. : Mitochondrial energy-linked nicotinamide nucleotide transhydrogenase. Membrane topography of the bovine enzyme. J. Biol. ; Cotton, N. : Purification and properties of the H(+)-nicotinamide nucleotide transhydrogenase from Rhodobacter capsulatus. Eur. J. : The coupling between protonmotive force and the NAD(P)+ transhydrogenase in chromatophores from photosynthetic bacteria [published erratum appears in Eur J Biochem 1989 Oct 1;184(3):729]. Eur. J. : Mitochondrial nicotinamide nucleotide transhydrogenase: NADPH binding increases and NADP binding decreases the acidity and susceptibility to modification of cysteine-893.