Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs-Reference-Cited by-同舟云学术

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Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs

Published:1998-01 Issue:1 Volume:7 Page:7-20
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Mewies Martin,McIntire William S.,Scrutton Nigel S.

Funder

Leverhulme Trust

Biotechnology and Biological Sciences Research Council

Royal Society

Department of Veterans Affairs

National Heart, Lung and Blood Institute

National Institutes of Health

Academic Senate and Research Evaluation and Allocation Committee

University of California San Francisco

McIntire's group

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560070102/fullpdf

Reference142 articles.

1. D-Fructose dehydrogenase from Gluconobacter industrius, membrane bound;Ameyama;Methods Enzymol,1982

2. Cloning and analysis of a locus (mcr) involved in mitomycin C resistance in Streptomyces lavendulae;August;J Bacteriol,1994

3. cDNA cloning of human liver monoamine oxidase A and B: Molecular basis of differences in enzymatic properties;Bach;Proc Natl Acad Sci USA,1988

4. An enzyme-substrate complex involved in cell wall biosynthesis;Bensen;Nature Struct Biol,1995

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