D-Amino Acids in Chemistry, Life Sciences, and Biotechnology
(Sprache: Englisch)
D-Amino Acids in Chemistry, Life Sciences and Biotechnology presents a collection of state of the art contributions from leading scientists in D-amino acid research, a field that has significant implications in relation to health care, research in...
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D-Amino Acids in Chemistry, Life Sciences and Biotechnology presents a collection of state of the art contributions from leading scientists in D-amino acid research, a field that has significant implications in relation to health care, research in age-related and neuronal diseases, pharmaceutical chemistry and food science.
Klappentext zu „D-Amino Acids in Chemistry, Life Sciences, and Biotechnology “
'D-Amino Acids in Chemistry, Life Sciences and Biotechnology' presents a collection of state of the art contributions from leading scientists in D-amino acid research, a field that has significant implications in relation to health care, research in age-related and neuronal diseases, pharmaceutical chemistry and food science.The increasing importance of D-amino acids and the need for a forum to exchange ideas and hypothesis led to the foundation of the 'D-Amino Acid Research Society' in Japan, followed by the First International Conference on D-Amino Acid Research in 2009. The majority of the contributions published in D-Amino Acids in Chemistry, Life Sciences and Biotechnology result from this event and reflect the long-standing interest of the Guest Editors and their co-workers and collaborators in the field of D-amino acid research.
Inhaltsverzeichnis zu „D-Amino Acids in Chemistry, Life Sciences, and Biotechnology “
PART 1: TRANSPEPTIDATION AND ISOMERIZATIONThe Role of Protein L-Isoaspartyl/D-Aspartyl O-Methyltransferase (PIMT) in Intracellular Signal Transduction (T. Furuchi, K. Sakurako, M. Katane, M. Sekine, H. Homma*)Modeling the Enolization of Succinimide Derivatives, a Key Step of Racemization of Aspartic Acid Residues: Importance of a Two-Water Mechanism (O. Takahashi*, K. Kobayashi, A. Oda)Molecular-Dynamics Simulations for Amyloid beta 1-42 Monomer with D-Aspartic Acid Residues Using Continuous Solvent (A. Oda*, K. Kobayashi, O. Takahashi)Accumulation of D-beta-Aspartic Acid-Containing Proteins in Age-Related Ocular Diseases (Y. Kaji*, T. Oshika, Y. Takazawa, M. Fukayama, N. Fujii)Quantification of Structural Alterations of L-Asp and L-Asn Residues in Peptides Related to Neuronal Diseases by Reversed-Phase High-Performance Liquid Chromatography (Y. Sadakane*, K. Konoha, M. Kawahara, K. Nakagomi)SAXS and SANS Observations of Abnormal Aggregation of Human alpha-Crystallin (M. Sugiyama*, N. Fujii, Y. Morimoto, K. Itoh, K. Mori, T. Fukunaga, N. Fujii)Collapse of Homochirality of Amino Acids in Proteins from Various Tissues during Aging (N. Fujii*, Y. Kaji, N. Fujii, T. Nakamura, R. Motoie, Y. Mori, T. Kinouchi)Influence of Oxidative Stress on D-Aspartyl Endopeptidase Activity (T. Kinouchi*, A. Matsuda, S. Kawakami, T. Shimizu, T. Shirasawa, N. Fujii)Structural Consideration of Mammalian D-Aspartyl Endopeptidase (T. Kinouchi*, N. Fujii)Oxidative Stress Induces the Formation of D-Aspartyl Residues in the Elastin Mimic Peptides (K. Kuge, K. Kitamura, K. Nakaoji, K. Hamada, N. Fujii, T. Saito, N. Fujii*)PART 2: D-AMINO ACID (D-ASPARTIC ACID) OXIDASEIndispensable but Insufficient Role of Renal D-Amino Acid Oxidase in Chiral Inversion of NG-Nitro-D-arginine (Y.-F. Xin, X. Li, B. Hao, N. Gong, W.-Q. Sun, R. Konno, Y.-X. Wang*)Comparative Characterization of Three D-Aspartate Oxidases and One D-Amino Acid Oxidase from Caenorhabditis elegans (M. Katane, Y. Saitoh, Y. Seida, M.
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Sekine, T. Furuchi, H. Homma*)D-Aspartate Oxidase: The Sole Catabolic Enzyme Acting on Free D-Aspartate in Mammals (M. Katane, H. Homma*)Mutant Mice and Rats Lacking D-Amino Acid Oxidase (R. Konno*, K. Hamase, R. Maruyama, K. Zaitsu)Effects of D-Aspartate Treatment on D-Aspartate Oxidase, Superoxide Dismutase, and Caspase 3 Activities in Frog (Rana esculenta) Tissues (L. Burrone, M. Di Giovanni, M. M. Di Fiore, G. C. Baccari, A. Santillo*)Thyroid Hormones and D-Aspartic Acid, D-Aspartate Oxidase, D-Aspartate Racemase, Hydrogen peroxide, and ROS in Rats and Mice (E. Topo, G. Fisher, A. Sorricelli, F. Errico, A. Usiello, A. D'Aniello*)Aberrant Control of Motoneuronal Excitability in Amyotrophic Lateral Sclerosis: Excitatory Glutamate/D-Serine vs. Inhibitory Glycine/gamma-Aminobutanoic Acid (GABA) (J. Sasabe*, S. Aiso)PART 3: D-AMINO ACIDS RELATED TO NUTRITION AND INDUSTRIAL APPLICATIONSOrigin, Microbiology, Nutrition, and Pharmacology of D-Amino Acids (M. Friedman)Natural Occurrence and Industrial Applications of D-Amino Acids: An Overview (S. Martinez-Rodriguez*, A. I. Martinez-Gomez, F. Rodriguez-Vico, J. M. Clemente-Jimenez, F. J. Las Heras-Vazquez*)Enzymes Responsible for the Conversion of Nalpha-[(Benzyloxy)carbonyl]-D-lysine to Nalpha-[(Benzyloxy)carbonyl]-D-aminoadipic Acid by Rhodococcus sp. AIU Z-35-1 (K. Isobe*, N. Fukuda, S. Nagasawa, K. Saitou)New Biological Functions and Applications of High-Molecular-Mass Poly-¿-glutamic Acid (H. Poo, C. Park, M.-S. Kwak, D.-Y. Choi, S.-P. Hong, I.-H. Lee, Y. T. Lim, Y. K. Choi, S.-R. Bae, H. Uyama, C.-J. Kim, M.-H. Sung*)Identification and Biochemical Characterization of Membranous Short-Chain Polyglutamate from Bacillus subtilis (T. Kamei, D. Yamashiro, T. Horiuchii, Y. Minouchi, M. Ashiuchi*)PART 4: AMINO ACID RACEMASES AND PEPTIDE ISOMERASESSerine Racemase Knockout Mice (H. Mori*, R. Inoue)Site-Directed Mutagenesis of Rice Serine Racemase: Evidence That Glu219 and Asp225 Mediate the Effects of Mg2+ on the Activity (Y. Gogami, A. Kobayashi, T. Ikeuchi, T. Oikawa*)Detection and Function of the Intramolecular Disulfide Bond in Arginine Racemase: An Enzyme with Broad Substrate Specificity (D. Matsui, T. Oikawa*)Mammalian Peptide Isomerase: Platypus-Type Activity Is Present in Mouse Heart (J. M. S. Koh, S. J. P. Chow, B. Crossett, P. W. Kuchel*)PART 5: RACEMIZATION MECHANISMS AND CHEMISTRY OF D-AMINO ACIDSConfigurational Assignment of D- and L-Isovalines in Intact, Natural, and Synthetic Peptides by 2D-NMR Spectroscopy (M. De Zotti, E. Schievano, S. Mammi, B. Kaptein, Q. B. Broxterman, S. B. Singh, H. Brückner, C. Toniolo*)Computational Insight into the Mechanism of Serine Residue Racemization (O. Takahashi*, K. Kobayashi, A. Oda)Computational Modeling of the Enolization in a Direct Mechanism of Racemization of the Aspartic Acid Residue (O. Takahashi*, K. Kobayashi, A. Oda)Protein-Engineering Study of Contribution of Conceivable D-Serine Residues to the Thermostabilization of Ovalbumin under Alkaline Conditions (N. Takahashi*, M. Maeda, M. Yamasaki, B. Mikami)Generation of Enantiomeric Amino Acids during Acid Hydrolysis of Peptides Detected by the Liquid Chromatography/Tandem Mass Spectroscopy (T. Miyamoto, M. Sekine, T. Ogawa, M. Hidaka, H. Homma, H. Masaki*)Photolysis of rac-Leucine with Circularly Polarized Synchrotron Radiation (U. J. Meierhenrich*, J.-J. Filippi, C. Meinert, S. V. Hoffmann, J. H. Bredehöft, L. Nahon)Amino Acid Ligand Chirality for Enantioselective Syntheses (K. Micskei*, T. Patonay, L. Caglioti, G. Pályi*)Hydrophobicity of Peptides Containing D-Amino Acids (T. Munegumi)INDEX
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Autoren-Porträt
Noriko Fujii was born in Tokyo, Japan, in 1951 and graduated from Meiji University, Tokyo in 1974. In 1976, she obtained an M.S. from Tokyo University of Fisheries and then obtained a Ph.D. from Tokyo Medical and Dental University in 1982. She became a lecturer in the Chemistry Department, University of Tsukuba (1980-1991), and then moved to Takeda Chemical Industries as a Research Scientist (1991-1994). In 1994-1997, she was appointed to the position of Research Scientist in the Group of Field and Reaction, Precursory Research for Embryonic Science and Technology (PRESTO), Japan Science and Technology Corporation (JST). In 1997, she became a Research Scientist (COE) at the National Institute for Advanced Interdisciplinary Research (NAIR) and moved to the Research Reactor Institute, Kyoto University as an associate professor in 1998, and became a full professor (2002-present). Her research interests span the homochirality and life, the appearance of D-amino acids in protein from aged tissues, the effects on higher order structure of protein of the formation of D-amino acid in living tissue. She is president of the 'D-Amino Acid Research Society', Japan.Hans Brückner was born in 1944 near Stuttgart, Germany. After several years employment as chemical engineer in synthetic peptide chemistry at Ciba in Basel/Switzerland, he graduated and received his equivalents of MSc and PhD in chemistry at Tübingen University in 1979. After two years as research assistant at the Institute of Chemistry and Institute of Microbiology at Tübingen, he changed to the Institute of Food Technology at the University of Hohenheim at Stuttgart. In 1985, he became docent of general food chemistry and technology, and in 1991 assistant professor and deputy of the professorship of dairy technology and head of the dairy plant. He is recipient of the Ajinomoto Prize for Amino Acid Research. In 1995, he accepted a call as full professor for food sciences at the Institute of Nutritional Science,
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located at the Interdisciplinary Research Centre (IFZ) at Giessen University and held the professorship until his retirement in 2008. He is still active in writing research articles and reviews and as a member of the honorary editorial board of the journal Chromatographia. His research topics cover isolation and sequence determination of peptide antibiotics, alterations of amino acids and proteins in the course of food processing, development of new methods for the chiral and non-chiral separation of amino acids, and relevance of D-amino acids in foodstuffs and life sciences in general. Together with Prof. C. Toniolo, Padova, Italy, he was guest editor of a topical issue of Chemistry & Biodiversity and a VHCA-Wiley book on peptide antibiotics ('Peptaibiotics'). In collaboration with Prof. N. Fujii and an international board, he co-edited the 4 volumes anthology 'D-Amino Acids. Practical Methods and Protocols' and, together with Prof. N. Fujii, he was guest-editor of a topical issue of Chemistry & Biodiversity on D-amino acid research. He is currently also appointed visiting professor at King Saud University, Riyadh, Saudi Arabia.
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Bibliographische Angaben
- 2010, 392 Seiten, 26 farbige Abbildungen, 121 Schwarz-Weiß-Abbildungen, Maße: 21,8 x 23,5 cm, Gebunden, Englisch
- Herausgegeben: Hans Brückner, Noriko Fujii
- Verlag: Wiley-VCH
- ISBN-10: 3906390659
- ISBN-13: 9783906390659
- Erscheinungsdatum: 15.12.2010
Sprache:
Englisch
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