Biosynthesis of tetrapyrroles
著者
書誌事項
Biosynthesis of tetrapyrroles
（New comprehensive biochemistry / general editors, A. Neuberger, L.L.M. van Deenen, v. 19）
Elsevier, 1991
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注記
Includes bibliographical references and index
内容説明・目次
内容説明
The study of the structure and function of tetrapyrrolic compounds has excited the interests of organic chemists, biochemists, botanists and biologists for more than a hundred years. Scientific analysis began with the first descriptions of naturally occurring porphyrins, and progress was made towards understanding the structure of chlorophyll. This was followed by the use of newly available isotopes of carbon and nitrogen to investigate the formation of porphyrins in biological systems. Further discoveries led to the elucidation of the atoms in protoporphyrin IX, made possible by the application of physical methods, such as NMR spectroscopy and recombinant DNA technology. The present volume discusses many more exciting and unexpected developments which have been made in the field over the last ten to fifteen years. While not all questions have yet been answered, the forum is set for a great scope of further research in the study of tetrapyrroles. # Of interest to biochemists, organic chemists and plant scientists # The book focusses on the exciting and unexpected developments in the field of tetrapyrolles over the last ten years # It paves the way for future research in this area
目次
The biosynthesis of 5-aminolaevulinic acid and its transformation into uroporphyrinogen III (P.M. Jordan). Early isotopic studies on the origin of the tetrapyrrole ring. The biosynthesis of 5-aminolaevulinic acid from glycine. The biosynthesis of 5-aminolaevulinic acid from glutamate. The biosynthesis of porphobilinogen. The biosynthesis of uroporphyrinogen III. Mechanism and stereochemistry of the enzymes involved in the conversion of uroporphyrinogen III into haem (M. Akhtar). Uroporphyrinogen decarboxylase [uroporphyrinogen carboxylase]. Coproporphyrinogen oxidase. Protoporphyrinogen IX oxidase. Ferrochelatase. The biosynthesis of vitamin B12 (A.I. Scott and P.J. Santander). The carbon balance. Stereochemistry of methyl group insertion in corrinoid biosynthesis. Concerning the fate of the methyl group protons. Uro'gen III is a precursor of vitamin B12. Characterization and intermediacy of the isobacteriochlorins of P.shermanii. The methylation sequence: pulse experiments. Timing of the decarboxylation step. The protein balance of vitamin B12 biosynthesis. Factors S1-S4, isomeric, tetramethylated corphinoids derived from uro'gen I. The methyl transferases. Biosynthesis of the neucleotide loop and coenzyme B12. Evolutionary aspects of B12 biosynthesis. Biochemistry of coenzyme F430, a nickel porphinoid involved in methanogenesis (H.C. Friedman, A. Klein and R.K. Thauer). Structural relations to other tetrapyrroles. Biosynthesis from glutamate via uroporphyrinogen III and dihydrosirohydrochlorin. Properties of free coenzyme F430 including its redox behaviour. Function of coenzyme F430 as prosthetic group of methyl coenzyme M reductase in methanogenesis. Comparative analysis of genes encoding methyl coenzyme M reductase. Biochemistry and regulation of photosynthetic pigment formation in plants and algae (S.I. Beale and J.D. Weinstein). The variety and functions of plant and algal tetrapyrroles. The biosynthetic route. Regulation. The structure and biosynthesis of bacteriochlorophylls (K.M. Smith). Nomenclature. Occurrence and structures. Biosynthesis. The genes of tetrapyrrole biosynthesis (P.M. Jordan and I.A. Mgbeje). Genes of haem biosynthesis. Genes of cobalamin (B12) biosynthesis. Genes of bacteriochlorophyll and chlorophyll biosynthesis.
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