Mechanisms of biosynthesis of protein-derived redox cofactors

Prior to 1990, redox cofactors were widely believed to be small molecule, dissociable compounds. In the past 10 years, however, four novel redox cofactors have been discovered, each of which is derived from posttranslational modification of specific amino acids within their cognate enzymes. These in...

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Published inCofactor Biosynthesis: a Mechanistic Perspective Vol. 61; pp. 219 - 239
Main Authors Schwartz, Benjamin, Klinman, Judith P
Format Book Chapter Journal Article
LanguageEnglish
Published United States Elsevier Science & Technology 2001
Academic Press
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ISBN9780127098616
0127098615
ISSN0083-6729
2162-2620
DOI10.1016/S0083-6729(01)61007-0

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Summary:Prior to 1990, redox cofactors were widely believed to be small molecule, dissociable compounds. In the past 10 years, however, four novel redox cofactors have been discovered, each of which is derived from posttranslational modification of specific amino acids within their cognate enzymes. These include topa quinone, found in copper amine oxidases, lysine tyrosyl quinone, found in lysyl oxidase, tryptophan tryptophylquinone, found in methylamine dehydrogenase, and the cysteine-cross-linked tyrosine found in galactose oxidase. The processes by which these cofactors are formed, called biogenesis, is currently a major focus of mechanistic work in this field. In this review, the latest progress toward elucidating the various biogenesis mechanisms is discussed, along with possible linkages between the chemistries involved in catalysis and biogenesis.
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ISBN:9780127098616
0127098615
ISSN:0083-6729
2162-2620
DOI:10.1016/S0083-6729(01)61007-0