R. Gholson

Publications70
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Citations1,496
Highly Influential Citations25
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L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase.
Hydrocarbon oxidation by a bacterial enzyme system. I. Products of octane oxidation.
The Pyridine Nucleotide Cycle
TLDR
Enzymes of the NAD glycohydrolase type are highly active, almost ubiquitous in biological materials, and may, therefore, be assumed to take the principal role in the formation of nicotinamide.
The pyridine nucleotide cycle and its role in the biosynthesis of ricinine by Ricinus communis L.
Higher plants contain L-asparate oxidase, the first enzyme of the Escherichia coli quinolinate synthetase system.
Metabolism of 6-aminonicotinic acid in Escherichia coli
TLDR
It is concluded that 6-aminonicotinamide and 6-aminsonicotinic acid probably exert at least a portion of their bacteriostatic effects by being metabolized, by the enzymes of the pyridine nucleotide cycle, to 6-AMino analogs of compounds in the p Pyridine nucleucleotide cycle.
HYDROCARBON OXIDATION BY A BACTERIAL ENZYME SYSTEM. II. COFACTOR REQUIREMENTS FOR OCTANOL FORMATION FROM OCTANE.
An improved column chromatographic method for isolation of tryptophan metabolites.
CHAPTER 6 – Metabolism of Aromatic Amino Acids
The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase.
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