Pyridine nucleotide-dependent dehydrogenases.

Proceedings of an Advanced Study Institute held at the University of Konstanz, Germany, September 15-20, 1969.
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Springer-Verlag , Berlin, New York
Dehydrogenases -- Congresses., Pyridine nucleotides -- Congre
StatementEdited by Horst Sund.
ContributionsSund, Horst, 1926- ed., Universität Konstanz., International Union of Biochemistry.
Classifications
LC ClassificationsQP601 .P96
The Physical Object
Paginationxv, 472 p.
ID Numbers
Open LibraryOL5699145M
LC Control Number70112313

Pyridine Nucleotide-Dependent Dehydrogenases: Proceedings of an Advanced Study Institute held at the University of Konstanz, Germany, SeptemberMedicine & Pyridine nucleotide-dependent dehydrogenases. book Science Books @ Pyridine Nucleotide-Dependent Dehydrogenases. Proceedings of an Advanced Study Institute Held at the University of Konstanz, Germany, September Hardcover – January 1, Author: horst sund.

Pyridine Nucleotide-Dependent Dehydrogenases Proceedings of an Advanced Study Institute held at the University of Konstanz, Germany, September 15–20, Editors: Sund, Horst (Ed.).

Book Review: Pyridine Nucleotide-Dependent Dehydrogenases. Crawford. Annals of Clinical Biochemistry 8:Download Citation. Book Review: Pyridine Nucleotide-Dependent Dehydrogenases Show all authors. Crawford. Crawford. See all articles by this : N. Crawford. The aim of the symposium was to provide a forum for discussion among the experts interested in the various aspects of pyridine nucleotide-dependent de­ hydrogenases and the pyridine coenzymes, so as to evaluate the state of the present knowledge and to stimulate further progress in this field.

Details Pyridine nucleotide-dependent dehydrogenases. PDF

The present volume represents the proceedings of the symposium on npyridine Nucleotide-Dependent Dehydrogenases" which was held on the campus of the re cently established University of Konstanz, Germany, from September 15 to 20, The aim of the symposium was to provide a forum for discussion among the experts interested in the various aspects of pyridine nucleotide-dependent de.

Conformational Adaptations Among Dehydrogenases was published in Pyridine Nucleotide-Dependent Dehydrogenases on page 3. BOOK REVIEWS Pyridine Nucleotide-Dependent Dehydrogenases. SUND (ed.). Springer-Verlag, Berlin, Pp, $ This volume records the proceedings of the International Union ofBiochemistry Symposium of the same title held in Konstanz in The success of this symposium was in no small part due to the.

Pyridine nucleotide-dependent dehydrogenases. Proceedings of an Advanced Study Institute held at the University of Konstanz, Germany, SeptemberAuthor. The aim of the symposium was to provide a forum for discussion among the experts interested in the various aspects of pyridine nucleotide-dependent de hydrogenases and the pyridine coenzymes, so as to evaluate the state of the present knowledge and to stimulate further progress in this field.

Pyridine nucleotide-dependent dehydrogenases: proceedings of the 2nd international symposium held at the University Pyridine nucleotide-dependent dehydrogenases. book Konstanz, West Germany, March April 1, Author: Horst Sund ; Deutsche Forschungsgemeinschaft.

The symposium was sponsored by the * The complete proceedings have been published in book form, Pyridine Nucleotide-Dependent Dehydrogenases, ed. Springer-Verlag, Berlin-Heidelberg-New York, North-Holland Publishing Company - Amsterdam International Union of' by: 6.

Pyridine-Nucleotide-Dependent Dehydrogenases Most dehydrogenases, which utilize DPN (1, 2) or TPNas hydrogen accep-tors, canbe classified as either alcohol or aldehyde dehydrogenases. A large body of evidence, accumulated in recent years, indicate that fundamental differences exist between these two classes of en-zymes.

Theenzymeswhich can be. * The complete proceedings have been published in book form, Pyridine Nucleotide-Dependent Dehydrogenases, ed.Springer-Verlag, Berlin-Heidelberg-New York, North-Holland Publishing Company - Amsterdam International Union of’Biochemist[v.

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A great deal of financial support was given by the NATO Science. A Mechanism for Pyridine-Nucleotide-Dependent Dehydrogenases. By JAN VAN EYS, ANTHONY SAN PIETRO, NATHAN O. KAPLAN. See all Hide authors and affiliations.

Science 20 Jun Vol.Issuepp. DOI: /science Article; Info & Metrics; eLetters; PDF; This is a PDF-only article. – in Pyridine Nucleotide-dependent Dehydrogenases(ed. Sund) Springer–Verlag, Berlin. mM mM 20 too. 20 too.

experimental data for binding Of NAD to yeast glyceraldehydephosphate dehydrogenase at Curve calculated assuming Kl x Pyridine nucleotide-dependent glucose dehydrogenase activity (GPND) is described for the first time in cell-free extracts of certain blue-green algae.

When glucose is added to these crude cell extracts, nicotinamide adenine dinucleotide phosphate is reduced at twice the rate as nicotinamide adenine dinucleotide; but evidence suggests that this Cited by: The reaction between a number of dehydrogenases, DPN or DPN analogues, and nucleophilic substances, known to form addition complexes with DPN has Cited by: CHEM Biochemistry Practice Problem.

Perspectives on Pyridine-Nucleotide-Dependent Dehydrogenases. NAD (Nicotinamide-Adenine Dinucleotide) and its phosphorylated derivative, NADP, serve as coenzymes for pyridine nucleotide-dependent imately one sixth of all enzymes involved in intermediary metabolism require a pyridine nucleotide coenzyme.

Pyridine Nucleotide-dependent Dehydrogenases () vásárlás 63 Ft. Olcsó Pyridine Nucleotide dependent Dehydrogenases Könyvek árak, akciók. Pyridine Nucleotide-dependent Dehydrogenases () vélemények.

Description Pyridine nucleotide-dependent dehydrogenases. FB2

Paperback. Book. pyridine nucleotide-dependent dehydrogenases that will oxidize n-mannitol to n-fructose at the nonphosphorylated level (). On the other hand, Wolff and Kaplan (6, 7) have reported the presence of a diphosphopyridine nucleotide-dependent n-man- nitol l Cited by:   NAD(P) + (nicotinamide–adenine dinucleotide (phosphate)) serves as a coenzyme for pyridine nucleotide‐dependent dehydrogenase catalysed redox reactions.

When the coenzyme behaves as a nondissociable prosthetic group it can function to promote aldehyde dismutation with nicotinoproteins as well as regular alcohol by: 3. Pyridine-Nucleotide-Dependent Dehydrogenases Most dehydrogenases, which utilize DPN (1, 2) or TPN as hydrogen accep-tors, can be classified as either alcohol or aldehyde dehydrogenases.

A large body of evidence, accumulated in recent years, indicate that fundamental differences exist between these two classes of en-zymes.

The enzymes which can. pyridine nucleotide-dependent dehydrogenases and the characterization of the coenzyme binding sites. Structure-Function Relationship. Problems of structure-function relationships including allo- steric problems and X-ray structure analysis.

Kinetics and Regulation. This non-pyridine dependent activity was related to the L-glutamate dehydrogenases proper, owing to the following: a) the localization of activity noticed corresponds to that obtained with the NAD- or NADP-containing media, b) the incubation time needed for initial formation of red and blue formazans is similar to that with coenzyme-containing Cited by:   The pyridine nucleotide coenzymes, NAD and NADP, appear to be among the most versatile of molecules with respect to their biological functions.

In addition to their well-documented roles in a large number of oxidation-reduction reactions, these coenzymes are involved in many aspects of metabolic Edition: 1. Aldehyde dehydrogenases catalyze the pyridine nucleotide‐dependent oxidation of aldehydes to acids.

Seventeen enzymes are currently viewed as belonging Cited by: 1 A method for the isolation and purification of a reversible NADH‐NADP+ transhydrogenase from Azotobacter vinelandii is described.

The purification consists of 7 steps: preparation of cell‐free e Cited by: The Reduced Pyridine Nucleotide of Human Erythrocytes Dehydrogenases EDWARD M.

SCOTT, IRMA W. DUNCAN, AND VIRGINIA EKSTRAXD From the Arctic Health Research Center, United States Public Health Service, Anchorage, Alaska (Received for publication, J ) Kiese (1) reported the presence of an enzyme in erythrocytes.

Molecular oxygen is reduced by the enzyme complex with S of about 30 micromolar and production of H2O and H2O2, without superoxide involvement.

The ratio NAD(P)H:O2 averages in the presence of KCN and in its absence. The pyridine nucleotide specificity of the dehydrogenases has been investigated by kinetic competition by:. Pyridine Nucleotide-Dependent Dehydrogenases Proceedingsofthe2ndInternational Symposiumheld at the Universityof Konstanz,WestGermany, MarchApril 1.NAD(P)H is the major carrier of reducing equivalents in cells.

NAD(P)-dependent dehydrogenases and reductases catalyze the reversible transfer of hydrogen equivalents between substrates and NAD(P). Author: Sund H, Journal: FEBS letters[/07] Pyridine nucleotide-dependent dehydrogenases a report of an advanced study Institute held at the University of Konstanz, Germany, SeptemberCited by: 6.