By Paul D. Boyer (Eds.)
Content material: entrance conceal; The Enzymes: Hydrolysis; Copyright web page; Contents; record of participants; Preface; Contents of different Volumes; bankruptcy 1. The Hydrolysis of Sulfate Esters; bankruptcy 2. Arylsulfatases; bankruptcy three. Carboxylic Ester Hydrolases; bankruptcy four. Phospholipases; bankruptcy five. Acetylcholinesterase; bankruptcy 6. Plant and Animal Amylases; bankruptcy 7. Glycogen and Starch Debranching Enzymes; bankruptcy eight. Bacterial and mildew Amylases; bankruptcy nine. Cellulases; bankruptcy 10. Yeast and Neurospora lnvertases; bankruptcy eleven. Hyaluronidases; bankruptcy 12. Neuraminidases; bankruptcy thirteen. Phage Lysozyme and different Lytic Enzymes. bankruptcy 14. AconitaseChapter 15. ß-Hydroxydecanoyl Thioester Dehydrase; bankruptcy sixteen. Dehydration in Nucleotide-Linked Deoxysugar Synthesis; bankruptcy 17. Dehydrations Requiring nutrition B12 Coenzyme; bankruptcy 18. Enolase; bankruptcy 19. Fumarase and Crotonase; bankruptcy 20. 6-Phosphogluconic and comparable Dehydrases; bankruptcy 21. Carbonic Anhydrase; writer Index; topic Index
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Additional resources for The Enzymes, Vol V: Hydrolysis (Sulfate Esters, Carboxyl Esters, Glycosides), Hydration, 3rd Edition
Ungar, Steroids 14, 161 (1969). 6 A. B. ROY tures of the substrates it is difficult not to conclude that each of them (111)-(VI) must be hydrolyzed by a different enzyme. Whatever the number of enzymes involved, of the commonly occurring steroid sulfates only androsterone sulfate (VII) and testosterone sulfate (VIII) are resistant to hydrolysis by presently known enzymes. The function of the steroid sulfatases in mammals needs no discussion. It, can be presumed that they play a part in the general pathways of steroid metabolism, and in one case a disordered estrogen metabolism has been shown to be associated with a deficiency of placental androstenolone sulfatase (19).
Dodgson, and F. A. Rose, BBA 220, 284 (1970). 72a. D. Armstrong, J. Austin, T. Luttenegger, B. Bachhawat, and D. Stumpf, BBA 198, 523 (1970). 73. T. Koiaumi, T. Suematsu, A. Kawasaki, K. Hiramatsu, and N. Iwabori, BBA 184, 106 (1969). 74. J. Austin, D. Armstrong, D. Stumpf, T. Luttenegger, and M. Dragoo, BBA 192, 29 (1969). 75. A. S. Balasubramanian and B. K. Bachhawat, BBA 59, 389 (1902). 18 A. B. 01 M (75). Although these enzymes are regarded as sulfohydrolases this has not been proven. Certainly their action leads to the production of sulfate from a sulfatophosphate, but this could occur by fission of either the 0 4 or the P-0 bond.
I 3, 149 (1936); I. Yamashina and F. Egnmi, J . Japan. Bwchem. Soc. 25, 281 (1963); P. F. Lloyd and C. H. Stuart, BJ 99, 37P (1966). 36. S. Dodgson, BJ 78, 324 (1961). 37. J. Fielder and P. F. Lloyd, BJ 109, 14P (1968). 38. A. G. Lloyd, P. J. Large, M. Davies, A. H. Olnvesen, and K. S. Dodgson, BJ 108, 393 (1968). 39. J. Weigl and W. Ynphe, Can. J . Microbud. 12,874 (1966). 40. F. Egnmi and N. Takahashi, in “Bioclwmistry and Medicine of Mucopolysaccharides” (F. Egami and Y. ), p. 53. , Tokyo, 1962.