Identification and properties of 8α-[N(1)-histidyl]-riboflavin: The flavin component of thiamine dehydrogenase and β-cyclopiazonate oxidocyclase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference8 articles.
1. A novel form of covalently bound flavin from thiamine dehydrogenase
2. The covalently bound flavin prosthetic group of β-cyclopiazonate oxidocyclase
3. Studies on Succinate Dehydrogenase. 8alpha-Histidyl-FAD as the Active Center of Succinate Dehydrogenase
4. 8α-Substituted flavins of biological importance
5. Flavins and Flavo-proteins;Singer,1975
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1. Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs;Protein Science;1998-01
2. Mutagenesis at a Highly Conserved Tyrosine in Monoamine Oxidase B Affects FAD Incorporation and Catalytic Activity;Biochemistry;1995-07-25
3. BIOSYNTHESIS AND FUNCTION OF ENZYMES WITH COVALENTLY BOUND FLAVIN;ANNU REV NUTR;1993
4. beta-Cyclopiazonate dehydrogenase;Enzyme Handbook;1993
5. Evidence for a competing condensation reaction in the alloxan synthesis of flavins: synthesis and crystal and molecular structures of 7-chloro-8-methylalloxazine and 7,10-dimethyl-8-[(2-hydroxyethyl)thio]isoalloxazine;Journal of the American Chemical Society;1986-02
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