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Redox-active amino acids in biology /
General Description of the Volume: The role of low molecular weight cofactors (often vitamins) in enzyme catalysis has been discussed in many earlier volumes of Methods in Enzymology. Exciting new results indicate that redox-active prosthetic groups can also arise from pre-existing amino acid side c...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
San Diego :
Academic Press,
�1995.
|
| Colección: | Methods in enzymology ;
v. 258. |
| Temas: | |
| Acceso en línea: | Texto completo Texto completo Texto completo |
MARC
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| 245 | 0 | 0 | |a Redox-active amino acids in biology / |c edited by Judith P. Klinman. |
| 260 | |a San Diego : |b Academic Press, |c �1995. | ||
| 300 | |a 1 online resource (xxvii, 415 pages) : |b illustrations | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
| 490 | 1 | |a Methods in enzymology, |x 0076-6879 ; |v v. 258 | |
| 588 | 0 | |a Print version record. | |
| 520 | |a General Description of the Volume: The role of low molecular weight cofactors (often vitamins) in enzyme catalysis has been discussed in many earlier volumes of Methods in Enzymology. Exciting new results indicate that redox-active prosthetic groups can also arise from pre-existing amino acid side chains in proteins. In this volume, methods are described for the detection and characterization of such prosthetic groups in a range of enzyme systems. General Description of the Series: The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences. Key Features * Among the redox-active prosthetic groups covered are: * Topa quinones * Pyrroloquinoline quinones * Quinoproteins * Tryptophan tryptophylquinones. | ||
| 504 | |a Includes bibliographical references and index. | ||
| 505 | 0 | |a Precursors of quinone tanning: Dopa-containing proteins / J. Herbert Waite -- Isolation of 2,4,5-trihydroxyphenylalanine quinone (topa quinone) from copper amine oxidases / Susan M. Janes, Judith P. Klinman -- Spectrophotometric detection of topa quinone / Monica M. Palcic, Susan M. Janes -- Model studies of topa quinone: Synthesis and characterization of topa quinone derivatives / Minae Mure, Judith P. Klinman -- Catalytic aerobic deamination of activated primary amines by a model for the quinone cofactor of mammalian copper amine oxidases / Lawrence M. Sayre, Younghee lee -- Detection of reaction intermediates in topa quinone enzymes / Christa Hartmann, David M. Dooley -- Mass spectrometric studies of the primary sequence and structure of bovine liver and serum amine oxidase / Gregory W. Adams, Petra Mayer, Katalin F. Medzihradszky, Alma L. Burlingame -- Cloning of mammalian topa quinone-containing enzymes / David Mu, Judith P. Klinman -- Isolation of active site peptides of lysyl oxidase / Herbert M. Kagan, Ping Cai -- Resonance Raman spectroscopy of quinoproteins / David M. Dooley, Doreen E. Brown -- Redox-cycling detection of dialyzable pyrroloquinoline quinone and quinoproteins / Rudolf Fl�uckiger, Mercedes A. Paz, Paul M. Gallop -- Tryptophan tryptophylquinone in bacterial amine dehydrogenases / William S. McIntire -- Model studies of cofactor tryptophan tryptophylquinone / Shinobu Itoh, Yoshiki Ohshiro -- Detection of intermediates in tryptophan tryptophylquinone enzymes / Victor L. Davidson, Harold B. Brooks, M. Elizabeth Graichen, Limei H. Jones, Young-Lan Hyun -- X-ray studies of quinoproteins / F. Scott Mathews -- Genetics of bacterial quinoproteins / Mary E. Lidstrom -- Biogenesis of pyrrolquinone quinone from 3C-labeled tyrosine / Clifford J. Unkefer, David R. Houck, B. Mark Britt, Tobin R. Sosnick, John L. Hanners -- X-ray crystallographic studies of cofactors in galactose oxidase / Nobutoshi Ito, Peter F. Knowles, Simon E.V. Phillips -- Spectroscopic studies of galactose oxidase / James W. Whittaker -- Use of rapid kinetics methods to study the assembly of the diferric-tyrosyl radical cofactor of E. coli ribonucleotide reductase / J. Martin Bollinger Jr., Wing Hang Tong, Natarajan Ravi, Boi Hanh Huynh, Dale Edmondson, JoAnne Stubbe -- Tyrosyl radicals in photosystem II / Bridgette A. Barry -- Role of tryptophans in substrate binding and catalysis by DNA photolyase / Sang-Tae Kim, Paul F. Heelis, Aziz Sancar -- Glycyl free radical in pyruvate formate-lyase: Synthesis, structure characteristics, and involvement in catalysis / Joachim Knappe, A.F. Volker Wagner -- Characterization of a radical intermediate in the lysine 2,3-aminomutase reaction / George H. Reed, Marcus D. Ballinger -- Role of oxidized amino acids in protein breakdown and stability / Earl R. Stadtman. | |
| 506 | |3 Use copy |f Restrictions unspecified |2 star |5 MiAaHDL | ||
| 533 | |a Electronic reproduction. |b [Place of publication not identified] : |c HathiTrust Digital Library, |d 2011. |5 MiAaHDL | ||
| 538 | |a Master and use copy. Digital master created according to Benchmark for Faithful Digital Reproductions of Monographs and Serials, Version 1. Digital Library Federation, December 2002. |u http://purl.oclc.org/DLF/benchrepro0212 |5 MiAaHDL | ||
| 583 | 1 | |a digitized |c 2011 |h HathiTrust Digital Library |l committed to preserve |2 pda |5 MiAaHDL | |
| 546 | |a English. | ||
| 650 | 0 | |a Oxidoreductases. | |
| 650 | 0 | |a Quinoproteins. | |
| 650 | 0 | |a Oxidation-reduction reaction. | |
| 650 | 0 | |a Amino acid sequence. | |
| 650 | 0 | |a Dehydrogenases. | |
| 650 | 1 | 2 | |a Amino Acids |x metabolism |0 (DNLM)D000596Q000378 |
| 650 | 1 | 2 | |a Oxidation-Reduction |0 (DNLM)D010084 |
| 650 | 2 | |a Oxidoreductases |0 (DNLM)D010088 | |
| 650 | 2 | 2 | |a Quinones |x chemistry |0 (DNLM)D011809Q000737 |
| 650 | 2 | 2 | |a Amino Acid Sequence |0 (DNLM)D000595 |
| 650 | 6 | |a Oxydor�eductases. |0 (CaQQLa)201-0045923 | |
| 650 | 6 | |a Quinoprot�eines. |0 (CaQQLa)201-0277990 | |
| 650 | 6 | |a Oxydor�eduction. |0 (CaQQLa)201-0081574 | |
| 650 | 6 | |a S�equence des acides amin�es. |0 (CaQQLa)201-0160535 | |
| 650 | 7 | |a Dehydrogenases. |2 fast |0 (OCoLC)fst00889845 | |
| 650 | 7 | |a Amino acid sequence. |2 fast |0 (OCoLC)fst00807613 | |
| 650 | 7 | |a Oxidation-reduction reaction. |2 fast |0 (OCoLC)fst01049564 | |
| 650 | 7 | |a Oxidoreductases. |2 fast |0 (OCoLC)fst01049585 | |
| 650 | 7 | |a Quinoproteins. |2 fast |0 (OCoLC)fst01085883 | |
| 650 | 7 | |a Aminos�auren |2 gnd |0 (DE-588)4142205-3 | |
| 650 | 7 | |a Proteine |2 gnd |0 (DE-588)4076388-2 | |
| 650 | 7 | |a Redoxreaktion |2 gnd |0 (DE-588)4177303-2 | |
| 650 | 7 | |a Redoxsystem |2 gnd |0 (DE-588)4177304-4 | |
| 650 | 7 | |a Seitenkette |2 gnd |0 (DE-588)4330425-4 | |
| 650 | 7 | |a Aufsatzsammlung |2 gnd |0 (DE-588)4143413-4 | |
| 650 | 1 | 7 | |a Enzymen. |2 gtt |
| 650 | 1 | 7 | |a Aminozuren. |2 gtt |
| 650 | 1 | 7 | |a Redoxreacties. |2 gtt |
| 650 | 1 | 7 | |a Co�enzymen. |2 gtt |
| 653 | 0 | |a Amino acids | |
| 700 | 1 | |a Klinman, Judith P., |e editor. | |
| 776 | 0 | 8 | |i Print version: |t Redox-active amino acids in biology. |d San Diego : Academic Press, �1995 |z 0121821595 |w (OCoLC)33096942 |
| 830 | 0 | |a Methods in enzymology ; |v v. 258. |x 0076-6879 | |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/book/9780121821593 |z Texto completo |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/258 |z Texto completo |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879 |z Texto completo |