Metalloenzymes
From Bench to Bedside
- 1st Edition - September 1, 2023
- Latest edition
- Editors: Claudiu T. Supuran, William Alexander Donald
- Language: English
Metalloenzymes: From Bench to Bedside offers a thorough overview of metalloenzymes, spanning biochemical and structural features, pharmacology, and biotechnological applicati… Read more
Metalloenzymes: From Bench to Bedside offers a thorough overview of metalloenzymes, spanning biochemical and structural features, pharmacology, and biotechnological applications. After a brief overview, international experts in the field discuss a wide range of magnesium, calcium, zinc, manganese, nickel, iron, copper, cadmium, molybdenum, and tungsten enzymes, along with catalytic roles within their active sites. With a uniform approach throughout, each chapter includes the structure and function of the enzyme, physiologic and pathologic roles, inhibitors and activators of the enzyme (and their design), and clinical agents or compounds applied in medicine and drug discovery. This book enables scientists across academia and industry to adopt ongoing metalloenzyme research, and continuous discovery of novel metalloenzymes, in new life science studies and clinical applications.
- Examines a range of metalloenzymes, from biochemistry to pharmacology and drug design
- Each chapter examines enzyme structure and function, physiologic and pathologic roles, inhibitors and activators, and clinical application
- Features chapter contributions from international experts in the field
Active researchers in biochemistry, molecular biology, pharmaceutical science, cellular biology, applied microbiology, and biotechnology, medical chemists, clinician scientists, Clinicians and students
1. Introduction to metalloenzymes
Section II
2. Magnesium and calcium-containing enzymes
2.1. DNA and RNA polymerase
2.2. Reverse transcriptase
2.3. Integrase
2.4. Nucleases
2.5. Terminases
2.6. Cyclin-dependent kinase 2 (CDK2)
2.7. Ketol acid reductoisomerase (KARI)
2.8. Catechol-O-methyltransferase (COMT)
2.9. D-Ala-D-Ala ligase
2.10. Sarco/endoplasmic reticulum calcium ATPase
2.11. Paraoxonases
Section III
3. Zinc enzymes
3.1. Carbonic anhydrases
3.2. Metallo-beta-lactamases
3.3. Bacterial zinc proteases
(clostridium collagenases, anthrax LF, botulinum and tetanus toxins, elastase B.)
3.4. Matrix metalloproteases
3.5. A Disintegrin and Metalloenzymes (ADAMs) and tumor necrosis factor-alpha-converting enzyme (TACE)
3.6. Angiotensin converting enzyme
3.7. Histidinol dehydrogenases
3.8. Histone deacetylases and other epigenetic targets
3.9. Protein prenyl transferases
3.10. CD73
3.11. Adenosine deaminase
3.12. Glyoxalase II
3.13. Aminopeptidase N
3.14 Glutamate carboxypeptidase II
3.15. AMP deaminase (AMPD)
3.16. Phosphodiesterase IV
3.17. Neutral endopeptidase (neprilysin)
3.18. VanX
3.19. Lpx
3.20. 19S proteasome regulatory subunit Rpn11
3.21. Class II fructose-1,6-biphosphate aldolase
Section IV. Other metalloenzymes
4. Manganese enzymes
4.1. Bacterial iota-carbonic anhydrases
4.2. Human arginases
4.3. Parasite (protozoan) arginases, Igor Almeida
4.4. 1-Deoxyxylulose-5-phosphate reductase isomerase
4.5. Methionine aminopeptidase
4.6. Imidazole glycerol phosphate dehydratase
5. Nickel enzymes
5.1. Glyoxalase I,
5.2. Bacterial ureases,
5.3. Acetyl-coenzyme A synthase/decarbonylase
5.4. Methyl-coenzyme M reductase
5.5. Lactate racemase
6. Iron enzymes (heme-containing)
6.1. COX
6.2. Cytochrome P450 (inhibitors for the metabolism of drugs, e.g., colbicistat)
6.3. Lanosterol 14α-demethylase
7. Iron enzymes (non-heme containing, Fe(II) or Fe(III) proteins)
7.1. Mono – and dioxygenases (including 4-hydroxyphenylpyruvate dioxygenase)
7.2. Indoleamine 2,3-dioxygenase
7.3. Non-heme di-iron catalases
7.4. Lysyl hydroxylases
7.5. 5-Lypoxygenase
7.6. Peptide deformylase (previously considered zinc enzyme)
7.7. Jumonji domain lysine demethylase (JmJc KDM)
8. Copper enzymes
8.1. Superoxide dismutase
8.2. Formylglycine-generating enzyme (FGE)
8.3. Tyrosinase
9. Cadmium enzymes
9.1. Cadmium CAs, G De Simone
10. Molybdenum enzymes
10.1. Nitrate reductase (NR), sulfite oxidase (SO), xanthine oxidoreductase (XOR), and aldehyde oxidase (AO)
10.2. Molybdenum cofactor of mARC (mitochondrial Amidoxime Reducing Component)
11. Tungsten-containing enzymes
- Edition: 1
- Latest edition
- Published: September 1, 2023
- Language: English
CS
Claudiu T. Supuran
Dr. Claudiu T. Supuran received his BSc in chemistry from the Polytechnic University of Bucharest, Romania (1987) and PhD in chemistry at the same university in 1991. In 1990, he became Assistant and then Associate Professor of Chemistry at the University of Bucharest. He was Visiting Scholar at the University of Florida, Gainesville, United States, at Griffith University, Brisbane, Australia, and Visiting Professor at University of La Plata, Argentina. In 1995 he moved to the University of Florence, Italy, where he is currently Full Professor in the Department of Neuroscience, Psychology, Medicine and Child Health. His main research interests include design of enzyme inhibitors and activators, heterocyclic chemistry, chemistry of sulfonamides, sulfamates, and sulfamides, biologically active organo-element derivatives, QSAR studies, X-ray crystallography of metallo-enzymes, metal complexes with biologically active ligands (metal-based drugs), carbonic anhydrases, cyclooxygenases, serine proteases, matrix metalloproteinases, bacterial proteases, and amino acid derivatives among others. He has published more than 1900 papers in these fields.
Affiliations and expertise
Full Professor, University of Florence, Neuroscience, Psychology, Medicine and Child Health, Florence, ItalyWD
William Alexander Donald
Dr. William Alexander Donald is an academic and research group leader in the School of Chemistry at the University of New South Wales, Australia. His research interests include carbonic anhydrases, coordination chemistry, and the development of bioanalytical methodologies for improving drug discovery and development. He has published more than 120 papers in these fields.
Affiliations and expertise
Associate Professor, School of Chemistry, University of New South Wales, Sydney, AustraliaRead Metalloenzymes on ScienceDirect