Cofactor Biosynthesis
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Author | : |
Publisher | : Academic Press |
Total Pages | : 375 |
Release | : 2001-01-02 |
Genre | : Science |
ISBN | : 0080544533 |
The longest running serial published by Academic Press continues its well-respected run with Volume 61, a special volume in which a guest editor has come on board and has assembled some well-known contributors who are international authorities in the field. Together they tackle some of the latest topics in the field such as riboflavin and folate biosynthesis, biotin and lipoic acid biosynthesis, nicotinamide adenine dinucleotide biosynthesis, biosynthesis of vitamin B6 and structurally related derivatives, pantothenic acid and coenzyme A biosynthesis, mechanistic biosynthesis of protein-derived redox cofactors, ascorbic acid biosynthesis, biosynthesis of menaquinone and ubiquinone - Vitamin B12 biosynthesis, biosynthesis of the methanogenic cofactors, and thiamin biosynthesis.
Author | : Tadhg P. Begley |
Publisher | : |
Total Pages | : |
Release | : 2001 |
Genre | : Electronic book |
ISBN | : |
Author | : Thomas G. Spiro |
Publisher | : Wiley-Interscience |
Total Pages | : 632 |
Release | : 1985-11-14 |
Genre | : Science |
ISBN | : |
Volume 7 in the Metal Ions in Biology Series, divided into two parts, covers the nitrogenase enzyme complex and the molybdenum redox enzymes. Part one covers the chemistry of Mo-Fe-S clusters and their relationship to nitrogenase, cofactor chemistry and biochemistry of nitrogenase, spectroscopic and electrochemical studies of the Fe-Mo cofactor and Fe-S clusters, and more. Part Two surveys oxo-molybdenum chemistry, discusses the nature of the molybdo-pterin complex, and describes the characteristics of several of the Mo redox enzymes.
Author | : F.J. Leeper |
Publisher | : Springer Science & Business Media |
Total Pages | : 214 |
Release | : 2003-09-05 |
Genre | : Science |
ISBN | : 3540695427 |
Concerned with discovering the chemical pathways of biosynthesis, this book devotes four chapters to the use of isotopes in biosynthetic research and the biosynthesis of enzyme cofactors and vitamin B12 and of reduced polyketides such as erythromycin. The topics covered demonstrate the revolution that has occurred in biosynthetic studies with the advent of gene cloning and overexpression. Yet the book also shows that the more classical approach to biosynthetic studies must go hand in hand with these new techniques.
Author | : Priya Rangaraj |
Publisher | : |
Total Pages | : 250 |
Release | : 1999 |
Genre | : |
ISBN | : |
Author | : F.J. Leeper |
Publisher | : Springer Science & Business Media |
Total Pages | : 212 |
Release | : 2000-02-14 |
Genre | : Science |
ISBN | : 9783540669692 |
Concerned with discovering the chemical pathways of biosynthesis, this book devotes four chapters to the use of isotopes in biosynthetic research and the biosynthesis of enzyme cofactors and vitamin B12 and of reduced polyketides such as erythromycin. The topics covered demonstrate the revolution that has occurred in biosynthetic studies with the advent of gene cloning and overexpression. Yet the book also shows that the more classical approach to biosynthetic studies must go hand in hand with these new techniques.
Author | : Luana Presta |
Publisher | : Springer |
Total Pages | : 79 |
Release | : 2015-05-07 |
Genre | : Science |
ISBN | : 9401799725 |
In this brief, the authors explore and review the current knowledge regarding the role of molybdenum in the evolution of biological systems and their interaction with biogeochemical cycles. Special emphasis is placed on biological nitrogen fixation and the nitrogen element cycle. The origin and evolution of molybdenum cofactor biosynthetic pathways as well as the evolutionary significance of molybdenum containing enzymes appearance is analyzed. Original data regarding nitrogen fixation pathways and related enzymes molecular evolution processes is presented. The trace element molybdenum is essential for nearly all organisms and forms the catalytic center of a large variety of enzymes such as nitrogenase, nitrate reductases, sulphite oxidase and xanthine oxidoreductases.
Author | : K. Tada |
Publisher | : Springer Science & Business Media |
Total Pages | : 421 |
Release | : 2013-03-14 |
Genre | : Medical |
ISBN | : 3662031477 |
Each disease-related chapter begins with a detailed description of the patient and the delineating symptoms used for establishing the diagnosis and differential diagnosis. The highly detailed figures illustrate the metabolic derangement in a uniform way, together with essential aspects of the genetics involved, thus affording clarification and better understanding of the treatment. Topics covered range from general aspects such as the clinical approach, emergency treatment, diagnostic procedures, and psychosocial care for the child and the family, to specific discussions of new modes of treatment, including liver, bone marrow transplantation and somatic gene therapy.
Author | : Chia-Hung Wu (Ph. D.) |
Publisher | : |
Total Pages | : 362 |
Release | : 2009 |
Genre | : |
ISBN | : |
The small subunit ([beta]2) of Escherichia coli class Ia ribonucleotide reductases (RNRs) contains a diferric tyrosyl radical (Y*) cofactor essential for the conversion of nucleotides to deoxynucleotides that are needed for DNA synthesis and repair. The mechanism and factors involved in the biosynthesis, maintenance and regulation of this cluster remains unclear. To understand these pathways, the genes contiguous to nrdB (gene encoding [beta]) in 181 bacterial genomes were analyzed which revealed a highly conserved [2Fe2S]-ferredoxin, YfaE in E. coli. YfaE has been cloned, expressed, reconstituted, and characterized by UV-visible, EPR and Mössbauer spectroscopies. Titration of met-[beta]2 (an inactive diferric-[beta]2 with Y* reduced) with [2Fe2S]1+-YfaE results in formation of diferrous-[beta]2 with one Fe reduced/YfaE oxidized. At the end point of titration, exposure of the reduced cluster to O2 in the absence of an additional reducing equivalent yields the diferric-Y* with 2 Fe/Y* generated, suggesting that the reducing equivalent required for cluster assembly is supplied by [beta]2, likely by W48. The kobs for the reaction between met-[beta]2 and [2Fe2S]1+-YfaE determined by anaerobic stopped flow spectroscopy is ~1-5 s-1. Studies of conserved Lys to Ala mutations of [beta]2 indicate electrostatic interactions may play an important role for interaction with YfaE. Quantitative Western blots of the whole cells suggest that YfaE acts catalytically in reactivating met-[beta]2 in vivo. Titration experiments establish that met-[beta]2 can be reduced by catalytic amounts of YfaE, Fre (a flavin reductase) and flavin with consumption of NADPH. In the presence of a Y* scavenger, hydroxyurea, [delta]yfaE shows slower growth rates than the isogenic wt strain and Western blots analysis shows up-regulation of YfaE expression, supporting YfaE's role in the reactivation of diferric-[beta]2 in vivo. To investigate the iron sources for diferric-Y* assembly, changes in Fe pools inside the cell subsequent to expression of [beta]2 was monitored by whole cell Mössbauer spectroscopy. The results show that both Fe2+ and Fe3+ pools can provide the iron for cluster assembly, suggesting a reduction mechanism(s) for Fe3+ to allow it function in this capacity. A potential role of YfaE as an iron chaperone for iron delivery to [beta]2 has also been investigated.
Author | : Astrid Sigel |
Publisher | : Royal Society of Chemistry |
Total Pages | : 539 |
Release | : 2009-03-09 |
Genre | : Medical |
ISBN | : 1847559158 |
Chapter 10 focuses on the interaction of CN- with enzymes containing vanadium, manganese, non-heme iron, and zinc, and the inhibiting properties of this ligand, allowing its use as a probe. The reaction mechanism of the molybdenum hydroxylase xanthine oxidoreductase is revisited in Chapter 11; previously a molybdenum-carbon bond was postulated but now proof is presented against its formation. The terminating Chapter 12 reviews briefly the most popular computational approaches employed in theoretical studies of bioorganometallic species by providing detailed examples.