Article
Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli.
European journal of biochemistry - 1 Jun 1994
Palmer T, Vasishta A, Whitty P W, Boxer D H
Abstract excerpt
The mob mutants in Escherichia coli are pleiotropically defective in all molybdoenzyme activities. They synthesise molybdopterin, the unique core of the molybdenum cofactor, but are unable to attach the GMP moiety to molybdopterin to form molybdopterin guanine dinucleotide, the functional molybde...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Chromatography, Gel
- Cloning, Molecular
- Coenzymes
- DNA, Bacterial
- Electrophoresis, Polyacrylamide Gel
- Enzyme Activation
- Enzyme Precursors
- Escherichia coli
- Genes, Bacterial
- Genomic Library
- Genotype
- Kinetics
- Metalloproteins
- Molecular Sequence Data
- Molecular Weight
- Molybdenum Cofactors