Advances in protein chemisrty and structural biology . Volume ninety seven : metal-containing enzymes / / edited by Christo Z. Christov |
Pubbl/distr/stampa | Waltham, Massachusetts ; ; San Diego, California : , : Academic Press, , 2014 |
Descrizione fisica | 1 online resource (174 p.) |
Disciplina | 572.7 |
Soggetto topico | Proteins |
Soggetto genere / forma | Electronic books. |
ISBN |
0-12-800012-0
0-12-800788-5 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Front Cover; Metal-Containing Enzymes; Copyright; Contents; Contributors; Preface; Chapter 1: Type-3 Copper Proteins: Recent Advances on Polyphenol Oxidases; 1. Introduction; 2. Primary Structure and Molecular Weights of PPOs; 2.1. General sequence structure; 2.2. Core domain, C-terminal domain, and its proteolytic cleavage site; 2.3. Conserved amino acid motifs in the core domain; 2.4. Conserved amino acid motifs in the C-terminal domain; 2.5. Transit peptide and location of PPOs; 2.6. Sequence homologies within PPOs; 2.7. In vitro activation of PPOs; 2.8. In vivo activation of PPOs
2.9. Mutants of PPOs2.9.1. Mutants of plant PPOs; 2.9.2. Mutants of fungal PPOs; 2.9.3. Mutants of bacterial PPOs; 3. Oxo Complex; 3.1. Oxo complex investigated by UV/vis absorption spectroscopy; 3.2. Oxo complex investigated by CD spectroscopy; 3.3. Oxo complex investigated by resonance Raman spectroscopy; 3.4. Oxo complex of catechol oxidase; 3.5. Oxo complex of tyrosinase; 3.6. Oxo complex of aureusidin synthase; 3.7. Oxo complex of hemocyanin; 4. X-ray Crystallographic Structural Data of PPOs and Hemocyanins; 4.1. Published structures in the protein data bank 4.1.1. Published structures in the PDB of hemocyanins4.1.2. Published structures in the PDB of catechol oxidases; 4.1.3. Published structures in the PDB of tyrosinases; 4.2. Structural differences of tyrosinases and catechol oxidases; 5. Conclusions and Outlook; Acknowledgments; References; Chapter 2: Biophysical Studies of Matrix Metalloproteinase/Triple-Helix Complexes; 1. MMPs and Collagen Hydrolysis; 2. Structures of Full-Length, Collagenolytic MMPs in Solution and in the Solid State; 3. Structural Evaluation of MMP Interactions with Collagen; 4. Mechanism of Collagenolysis 5. Heterogeneity in MMP StructuresAcknowledgment; References; Chapter 3: Catalytic Mechanisms of Metallohydrolases Containing Two Metal Ions; 1. Introduction; 2. Metallo-β-Lactamases, Major Culprits in the Emergence of Antibiotic Resistance; 3. Methionine Aminopeptidase, a Target for Novel Anticancer Drugs; 4. Glycerophosphodiesterase, a Very Promiscuous Potential Bioremediator; 5. PAP, an Alternative Target to Treat Osteoporosis; 6. Conclusions and Outlook: Agmatinase, an Emerging Target for Biotechnological Applications; Acknowledgments; References Chapter 4: Applications of Quantum Mechanical/Molecular Mechanical Methods to the Chemical Insertion Step of DNA and RNA ...1. Introduction; 2. Methods for Describing Reactive Pathways; 3. DNA Polymerase β; 3.1. Abashkin, Erickson, and Burt (2001): A cluster QM calculation at steps along a proposed reaction path; 3.2. Rittenhouse, Apostoluk, Miller, and Straatsma (2003): A cluster QM calculation on the prechemistry complex of Pol β; 3.3. Sawaya et al., 1997); 3.4. Batra et al., 2006); 3.5. Batra et al., 2008) 3.6. Batra et al. (2013): A QM/MM study based on the X-ray crystal structure of the Pol β variant D256E |
Record Nr. | UNINA-9910465130003321 |
Waltham, Massachusetts ; ; San Diego, California : , : Academic Press, , 2014 | ||
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Lo trovi qui: Univ. Federico II | ||
|
Advances in protein chemistry and structural biology . Volume ninety seven : metal-containing enzymes / / edited by Christo Z. Christov |
Pubbl/distr/stampa | Waltham, Massachusetts ; ; San Diego, California : , : Academic Press, , 2014 |
Descrizione fisica | 1 online resource (174 p.) |
Disciplina | 572.7 |
Soggetto topico | Proteins |
ISBN |
0-12-800012-0
0-12-800788-5 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Front Cover; Metal-Containing Enzymes; Copyright; Contents; Contributors; Preface; Chapter 1: Type-3 Copper Proteins: Recent Advances on Polyphenol Oxidases; 1. Introduction; 2. Primary Structure and Molecular Weights of PPOs; 2.1. General sequence structure; 2.2. Core domain, C-terminal domain, and its proteolytic cleavage site; 2.3. Conserved amino acid motifs in the core domain; 2.4. Conserved amino acid motifs in the C-terminal domain; 2.5. Transit peptide and location of PPOs; 2.6. Sequence homologies within PPOs; 2.7. In vitro activation of PPOs; 2.8. In vivo activation of PPOs
2.9. Mutants of PPOs2.9.1. Mutants of plant PPOs; 2.9.2. Mutants of fungal PPOs; 2.9.3. Mutants of bacterial PPOs; 3. Oxo Complex; 3.1. Oxo complex investigated by UV/vis absorption spectroscopy; 3.2. Oxo complex investigated by CD spectroscopy; 3.3. Oxo complex investigated by resonance Raman spectroscopy; 3.4. Oxo complex of catechol oxidase; 3.5. Oxo complex of tyrosinase; 3.6. Oxo complex of aureusidin synthase; 3.7. Oxo complex of hemocyanin; 4. X-ray Crystallographic Structural Data of PPOs and Hemocyanins; 4.1. Published structures in the protein data bank 4.1.1. Published structures in the PDB of hemocyanins4.1.2. Published structures in the PDB of catechol oxidases; 4.1.3. Published structures in the PDB of tyrosinases; 4.2. Structural differences of tyrosinases and catechol oxidases; 5. Conclusions and Outlook; Acknowledgments; References; Chapter 2: Biophysical Studies of Matrix Metalloproteinase/Triple-Helix Complexes; 1. MMPs and Collagen Hydrolysis; 2. Structures of Full-Length, Collagenolytic MMPs in Solution and in the Solid State; 3. Structural Evaluation of MMP Interactions with Collagen; 4. Mechanism of Collagenolysis 5. Heterogeneity in MMP StructuresAcknowledgment; References; Chapter 3: Catalytic Mechanisms of Metallohydrolases Containing Two Metal Ions; 1. Introduction; 2. Metallo-β-Lactamases, Major Culprits in the Emergence of Antibiotic Resistance; 3. Methionine Aminopeptidase, a Target for Novel Anticancer Drugs; 4. Glycerophosphodiesterase, a Very Promiscuous Potential Bioremediator; 5. PAP, an Alternative Target to Treat Osteoporosis; 6. Conclusions and Outlook: Agmatinase, an Emerging Target for Biotechnological Applications; Acknowledgments; References Chapter 4: Applications of Quantum Mechanical/Molecular Mechanical Methods to the Chemical Insertion Step of DNA and RNA ...1. Introduction; 2. Methods for Describing Reactive Pathways; 3. DNA Polymerase β; 3.1. Abashkin, Erickson, and Burt (2001): A cluster QM calculation at steps along a proposed reaction path; 3.2. Rittenhouse, Apostoluk, Miller, and Straatsma (2003): A cluster QM calculation on the prechemistry complex of Pol β; 3.3. Sawaya et al., 1997); 3.4. Batra et al., 2006); 3.5. Batra et al., 2008) 3.6. Batra et al. (2013): A QM/MM study based on the X-ray crystal structure of the Pol β variant D256E |
Record Nr. | UNINA-9910792224403321 |
Waltham, Massachusetts ; ; San Diego, California : , : Academic Press, , 2014 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Advances in protein chemistry and structural biology . Volume ninety seven : metal-containing enzymes / / edited by Christo Z. Christov |
Pubbl/distr/stampa | Waltham, Massachusetts ; ; San Diego, California : , : Academic Press, , 2014 |
Descrizione fisica | 1 online resource (174 p.) |
Disciplina | 572.7 |
Soggetto topico | Proteins |
ISBN |
0-12-800012-0
0-12-800788-5 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Front Cover; Metal-Containing Enzymes; Copyright; Contents; Contributors; Preface; Chapter 1: Type-3 Copper Proteins: Recent Advances on Polyphenol Oxidases; 1. Introduction; 2. Primary Structure and Molecular Weights of PPOs; 2.1. General sequence structure; 2.2. Core domain, C-terminal domain, and its proteolytic cleavage site; 2.3. Conserved amino acid motifs in the core domain; 2.4. Conserved amino acid motifs in the C-terminal domain; 2.5. Transit peptide and location of PPOs; 2.6. Sequence homologies within PPOs; 2.7. In vitro activation of PPOs; 2.8. In vivo activation of PPOs
2.9. Mutants of PPOs2.9.1. Mutants of plant PPOs; 2.9.2. Mutants of fungal PPOs; 2.9.3. Mutants of bacterial PPOs; 3. Oxo Complex; 3.1. Oxo complex investigated by UV/vis absorption spectroscopy; 3.2. Oxo complex investigated by CD spectroscopy; 3.3. Oxo complex investigated by resonance Raman spectroscopy; 3.4. Oxo complex of catechol oxidase; 3.5. Oxo complex of tyrosinase; 3.6. Oxo complex of aureusidin synthase; 3.7. Oxo complex of hemocyanin; 4. X-ray Crystallographic Structural Data of PPOs and Hemocyanins; 4.1. Published structures in the protein data bank 4.1.1. Published structures in the PDB of hemocyanins4.1.2. Published structures in the PDB of catechol oxidases; 4.1.3. Published structures in the PDB of tyrosinases; 4.2. Structural differences of tyrosinases and catechol oxidases; 5. Conclusions and Outlook; Acknowledgments; References; Chapter 2: Biophysical Studies of Matrix Metalloproteinase/Triple-Helix Complexes; 1. MMPs and Collagen Hydrolysis; 2. Structures of Full-Length, Collagenolytic MMPs in Solution and in the Solid State; 3. Structural Evaluation of MMP Interactions with Collagen; 4. Mechanism of Collagenolysis 5. Heterogeneity in MMP StructuresAcknowledgment; References; Chapter 3: Catalytic Mechanisms of Metallohydrolases Containing Two Metal Ions; 1. Introduction; 2. Metallo-β-Lactamases, Major Culprits in the Emergence of Antibiotic Resistance; 3. Methionine Aminopeptidase, a Target for Novel Anticancer Drugs; 4. Glycerophosphodiesterase, a Very Promiscuous Potential Bioremediator; 5. PAP, an Alternative Target to Treat Osteoporosis; 6. Conclusions and Outlook: Agmatinase, an Emerging Target for Biotechnological Applications; Acknowledgments; References Chapter 4: Applications of Quantum Mechanical/Molecular Mechanical Methods to the Chemical Insertion Step of DNA and RNA ...1. Introduction; 2. Methods for Describing Reactive Pathways; 3. DNA Polymerase β; 3.1. Abashkin, Erickson, and Burt (2001): A cluster QM calculation at steps along a proposed reaction path; 3.2. Rittenhouse, Apostoluk, Miller, and Straatsma (2003): A cluster QM calculation on the prechemistry complex of Pol β; 3.3. Sawaya et al., 1997); 3.4. Batra et al., 2006); 3.5. Batra et al., 2008) 3.6. Batra et al. (2013): A QM/MM study based on the X-ray crystal structure of the Pol β variant D256E |
Record Nr. | UNINA-9910826143903321 |
Waltham, Massachusetts ; ; San Diego, California : , : Academic Press, , 2014 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
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