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Ferredoxins from two sulfonylurea herbicide monooxygenase systems in Streptomyces griseolus.
Two ferredoxins are purified and characterized from the soluble protein fraction of sulfonylurea herbicide induced Streptomyces griseolus, resulting in cells capable of herbicide metabolism and transformants encoding only cytochrome P-450SU1 do not metabolize herbicide.
Escherichia coli biotin synthase: an investigation into the factors required for its activity and its sulfur donor.
- I. Sanyal, K. Gibson, D. Flint
- Chemistry, MedicineArchives of biochemistry and biophysics
- 1 February 1996
It is found that a labile low-molecular-weight product of the 7,8-diaminopelargonic acid aminotransferase reaction stimulates the rate of biotin formation in the defined biotin synthase reaction mixture and can increase the final amount ofBiotin formed by threefold.
Snapshot of a phosphorylated substrate intermediate by kinetic crystallography.
- H. Käck, K. Gibson, Y. Lindqvist, G. Schneider
- Chemistry, MedicineProceedings of the National Academy of Sciences…
- 12 May 1998
A key feature in the structure of the complex of the enzyme with the reaction intermediate is two magnesium ions, bridging the phosphates at the cleavage site, which compensate the negative charges at both phosphate groups after phosphoryl transfer and contribute to the stabilization of the Reaction intermediate.
Phosphoribosylpyrophosphate synthetase (ribose-5-phosphate pyrophosphokinase) from Salmonella typhimurium.
This chapter describes the assay methodology of phosphoribosylpyrophosphate synthetase (PRPP) (ribose-5-phosphate pyrophosphokinase) from Salmonella typhimurium as well as an alternative form of this assay in which release of 14 CO 2 from [7- 14 C] orotate is measured.
Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes.
- H. Käck, J. Sandmark, K. Gibson, G. Schneider, Y. Lindqvist
- Chemistry, MedicineJournal of molecular biology
- 27 August 1999
Structures analysis reveals that diaminopelargonic acid synthase belongs to the family of vitamin B6-dependent aminotransferases with the same fold as originally observed in aspartate aminOTransferase, and that they form at least six different subclasses.
Chemotaxis toward amino acids by Bacillus subtilis
In it, chemotaxis measured by capillary assays was insensitive to pH between 5.5 and 9, and to temperature between 28 degrees C and 42 degrees C, and Chemotaxis was observed toward all 20 common amino acids, with thresholds varying from 3nM for alanine to 0.1 mM for glutamate.
Cloning and Characterization of a Gene Cluster for Cyclododecanone Oxidation in Rhodococcus ruber SC1
- K. Kostichka, Stuart M. Thomas, K. Gibson, V. Nagarajan, Q. Cheng
- Medicine, BiologyJournal of bacteriology
- 1 November 2001
The biochemical function of the enzymes encoded on the 10-kb gene cluster, the flavin monooxygen enzyme, the lactone hydrolase, the alcohol dehydrogenase, and the aldehyde dehydrogenases, was determined in Escherichia coli based on the ability to convert cyclododecanone.
Binding of the substrates and the allosteric inhibitor adenosine 5'-diphosphate to phosphoribosylpyrophosphate synthetase from Salmonella typhimurium.
- K. Gibson, K. Schubert, R. Switzer
- Medicine, ChemistryThe Journal of biological chemistry
- 10 March 1982
The binding of the substrates and the most effective inhibitor, ADP, to phosphoribosylpyrophosphate synthetase from Salmonella typhimurium was characterized using equilibrium dialysis of these compounds labeled with 32P and confirmed the existence of an allosteric ADP site.
Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based on crystallographic studies of complexes with substrates and a reaction intermediate.
Crystal structures of six complexes of homodimeric Escherichia coli dethiobiotin synthetase with a variety of substrates, substrate analogs, and products have been determined to high resolution, indicating that, even in the absence of added bicarbonate in the crystallization mixture, the carbamylated intermediate is formed in the crystal.
Crystal structure of an ATP-dependent carboxylase, dethiobiotin synthetase, at 1.65 A resolution.
- W. Huang, Y. Lindqvist, G. Schneider, K. Gibson, D. Flint, G. Lorimer
- Biology, MedicineStructure
- 1 May 1994
The three-dimensional structure of dethiobiotin synthetase has revealed that ATP-dependent carboxylases contain the classical monon nucleotide-binding fold, indicating that both proteins might have evolved from a common ancestral mononucleotide- binding fold.