Novel Cofactors: Volume 58
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Novel Cofactors: Volume 58

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Description

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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Product details

  • Hardback | 474 pages
  • 161.3 x 237 x 27.4mm | 793.8g
  • Academic Press Inc
  • San Diego, United States
  • English
  • 58th edition
  • 0120342588
  • 9780120342587

Table of contents

Preface.
Radical Mechanisms of S-Adenosylmethionine-Dependent Enzymes,
P.A. Frey and S.J. Booker.
Molybdopterin from Molybdenum and Tungsten Enzymes,
H. Schindelin, C. Kisker, and K.V. Rajagopalan.
Pyrroloquinoline Quinone (PQQ) from Methanol Dehydrogenase and Tryptophan Tryptophylquinone (TTQ) from Methylamine Dehydrogenase,
V.L. Davidson.
Trihydroxyphenylalanine Quinone (TPQ) from Copper Amine Oxidases and Lysyl Tyrosylquinone (LTQ) from Lysyl Oxidase,
J.E. Dove and J.P. Klinman.
Methylidene-Imidazolone (MIO) from Histidine and Phenylalanine Ammonia-Lyase,
B. Langer, M. Langer, and J. Retey.
Structural, Redox, and Mechanistic Parameters for Cysteine-Sulfenic Acid Function in Catalysis and Regulation,
A. Claiborne, T.C. Mallett, J.I. Yeh, J. Luba, and D. Parsonage.
Stable Glycyl Radical from Pyruvate Formate-Lyase and Ribonucleotide Reductase (III),
J. Knappe and A.F. Volker Wagner.
Tyrosyl Radical Cofactors,
R.P. Pesavento and W.A. van der Donk.
Posttranslationally Modified Tyrosines from Galactose Oxidase and Cytochrome c Oxidase,
M.S. Rogers and D.M. Dooley.
Author Index.
Subject Index.
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Review quote

Praise for the Series:
"The authority, originality, and editing of the reviews are first class."
--NATURE
"The Advances in Protein Chemistry series has been a major factor in the education of protein chemists."
--JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
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