A mechanism for substrate-Induced formation of 6-hydroxyflavin mononucleotide catalyzed by C30A trimethylamine dehydrogenase

Xingliang Lu; Dejan Nikolic; Deanna J Mitchell; Richard B van Breemen; John A Mersfelder; Russ Hille; Richard B Silverman

doi:10.1016/j.bmcl.2003.07.032

A mechanism for substrate-Induced formation of 6-hydroxyflavin mononucleotide catalyzed by C30A trimethylamine dehydrogenase

Bioorg Med Chem Lett. 2003 Nov 17;13(22):4129-32. doi: 10.1016/j.bmcl.2003.07.032.

Authors

Xingliang Lu¹, Dejan Nikolic, Deanna J Mitchell, Richard B van Breemen, John A Mersfelder, Russ Hille, Richard B Silverman

Affiliation

¹ Department of Chemistry, Northwestern University, Evanston, IL 60208-3113, USA.

PMID: 14592522
DOI: 10.1016/j.bmcl.2003.07.032

Abstract

Experiments are described to determine the origin of the 6-hydroxyl group of 6-hydroxyFMN produced by the substrate-induced transformation of FMN in the C30A mutant of trimethylamine dehydrogenase. The conversion of FMN to 6-hydroxyFMN is carried out in the presence of H(2)(18)O and 18O(2), and the results clearly show that the 6-hydroxyl group is derived from molecular oxygen and not from water.

Publication types

Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amino Acid Substitution
Cloning, Molecular
Escherichia coli / enzymology
Escherichia coli / genetics
Flavin Mononucleotide / analogs & derivatives*
Flavin Mononucleotide / biosynthesis*
Flavin Mononucleotide / metabolism*
Methylophilus methylotrophus / enzymology
Mutagenesis, Site-Directed
Oxidoreductases, N-Demethylating / metabolism*
Recombinant Proteins / metabolism
Substrate Specificity

Substances

6-hydroxyflavin mononucleotide
Recombinant Proteins
Flavin Mononucleotide
Oxidoreductases, N-Demethylating
trimethylamine dehydrogenase

Abstract

Publication types

MeSH terms

Substances

Grants and funding