Journal
BIOORGANIC CHEMISTRY
Volume 33, Issue 3, Pages 159-170Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bioorg.2004.10.001
Keywords
amine dehydrogenase; quinoprotein; posttranslational modification; protein-derived cofactor; redox protein; hydrogen tunneling
Funding
- NIGMS NIH HHS [GM-41574] Funding Source: Medline
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Tryptophylquinone cofactors are formed by posttranslational modifications that result in the incorporation of two oxygens into a tryptophan side chain, and the covalent cross-linking of that side chain to another amino acid residue. Tryptophylquinone enzymes catalyze the oxidative deamination of primary amines, and utilize other redox proteins as electron acceptors. Mechanistic and structural studies of these enzymes are providing insight into how these enzymes utilize these highly reactive protein-derived quinones in a controlled manner to facilitate biologically important catalytic and electron transfer reactions. (c) 2004 Elsevier Inc. All rights reserved.
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