Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking-Reference-Cited by-同舟云学术

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Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking

Published:2001-11-20 Issue:25 Volume:98 Page:14268-14273
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Datta S.,Mori Y.,Takagi K.,Kawaguchi K.,Chen Z.-W.,Okajima T.,Kuroda S.,Ikeda T.,Kano K.,Tanizawa K.,Mathews F. S.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference38 articles.

1. Quinoprotein-catalysed reactions

2. A New Redox Cofactor in Eukaryotic Enzymes: 6-Hydroxydopa at the Active Site of Bovine Serum Amine Oxidase

3. A Crosslinked Cofactor in Lysyl Oxidase: Redox Function for Amino Acid Side Chains

4. A New Cofactor in a Prokaryotic Enzyme: Tryptophan Tryptophylquinone as the Redox Prosthetic Group in Methylamine Dehydrogenase

5. QUINOENZYMES IN BIOLOGY

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