3 Oxygenases: Dioxygenases

作者: Osamu Hayaishi , Mitsuhiro Nozaki , Mitchel T. Abbott

DOI: 10.1016/S1874-6047(08)60226-7

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摘要: Publisher Summary Pyrocatechase was isolated from cells of a pseudomonad, which catalyzed oxidative ring cleavage the benzene catechol forming cis, cis-muconic acid as reaction product. This enzyme exhibited properties unlike those an oxidase or dehydrogenase because it not associated with any previously known coenzymes electron carriers, and none dyes artificial acceptors tested could replace oxygen oxidant. Biological oxidation proceeded exclusively by removal electrons hydrogen atoms substrates, directs addition molecular excluded consideration. Oxygen act only ultimate acceptor in biological that all incorporated into substrates are derived water. chapter proposes new term, “oxygenase” to designate enzymes catalyze fixation reactions, terms “di” “mono” oxygenases generally assigned enzymes. Dioxygenases defined catalyzing reactions both substrates. In many instances where one substrate can acceptor. play important roles biosynthesis, transformation, degradation essential metabolites, such amino acids, lipids, sugars, nucleic porphyrins, vitamins, hormones. They also crucial role various aromatic compounds drugs, insecticides, carcinogens.

参考文章(163)
J. P. Comstock, S. Udenfriend, Effect of lactate on collagen proline hydroxylase activity in cultured L-929 fibroblasts. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 66, pp. 552- 557 ,(1970) , 10.1073/PNAS.66.2.552
M.T. Abbott, E.K. Schandl, R.F. Lee, T.S. Parker, R.J. Midgett, Cofactor requirements of thymine 7-hydroxylase Biochimica et Biophysica Acta. ,vol. 132, pp. 525- 528 ,(1967) , 10.1016/0005-2744(67)90177-5
J. A. Olson, O. Hayaishi, The enzymatic cleavage of beta-carotene into vitamin A by soluble enzymes of rat liver and intestine Proceedings of the National Academy of Sciences of the United States of America. ,vol. 54, pp. 1364- 1370 ,(1965) , 10.1073/PNAS.54.5.1364
Kari I. Kivirikko, Harold J. Bright, Darwin J. Prockop, Kinetic patterns of protocollagen hydroxylase and further studies on the polypeptide substrate Biochimica et Biophysica Acta. ,vol. 151, pp. 558- 567 ,(1968) , 10.1016/0005-2744(68)90002-8
F. L. H. Stassen, G. J. Cardinale, S. Udenfriend, Activation of Prolyl Hydroxylase in L-929 Fibroblasts by Ascorbic Acid Proceedings of the National Academy of Sciences of the United States of America. ,vol. 70, pp. 1090- 1093 ,(1973) , 10.1073/PNAS.70.4.1090
Jouko Halme, Kari I. Kivirikko, Kai Simons, Isolation and partial characterization of highly purified protocollagen proline hydroxylase Biochimica et Biophysica Acta. ,vol. 198, pp. 460- 470 ,(1970) , 10.1016/0005-2744(70)90124-5
Henry W.-S. Chan, Soya-bean lipoxygenase: An iron-containing dioxygenase Biochimica et Biophysica Acta (BBA) - Enzymology. ,vol. 327, pp. 32- 35 ,(1973) , 10.1016/0005-2744(73)90100-9
Maija Pänkäläinen, Heikki Aro, Kai Simons, Kari I. Kivirikko, Protocollagen proline hydroxylase: Molecular weight, subunits and isoelectric point Biochimica et Biophysica Acta (BBA) - Protein Structure. ,vol. 221, pp. 559- 565 ,(1970) , 10.1016/0005-2795(70)90227-8