Text in English.

Made available through: Science Direct.

Includes bibliographical references and index.

Radical mechanisms of S-adenosylmethionine-dependent enzymes / Perry A. Frey and Squire J. Booker -- Molybdopterin from molybdenum and tungsten enzymes / Hermann Schindelin, Caroline Kisker, and K.V. Rajagopalan -- Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase / Victor L. Davidson -- Trihydroxyphenylalanine quinone (TPQ) from copper amine oxidases and lysyl tyrosylquinone (LTQ) from lysyl oxidase / Joanne E. Dove and Judith P. Klinman -- Methylidene-imidazolone (MIO) from histidine and phenylalanine ammonia-lyase / Birgid Langer, Martin Langer, and János Rétey -- Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation / Al Claiborne [and others] -- Stable glycyl radical from pyruvate formate-lyase and ribonucleotide reductase (III) / Joachim Knappe and A.F. Volker Wagner -- Tyrosyl radical cofactors / Russell P. Pesavento and Wilfred A. van der Donk -- Posttranslationally modified tyrosines from galactose oxidase and cytochrome c oxidase Melanie S. Rogers and David M. Dooley.

A cofactor is a component part of many enzymes and functions by uniting with another molecule in order to become active. The use of cofactors to supplement the native amino acids of a protein is essential to maintain the chemical capabilities necessary for organisms to survive. This volume focuses on the significant advances of the past decade in identifying and describing new cofactors--either small molecules or those derived posttranslationally.

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