L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase.
@article{Nasu1982LAspartateOA, title={L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase.}, author={S Nasu and Floyd Wicks and R. K. Gholson}, journal={The Journal of biological chemistry}, year={1982}, volume={257 2}, pages={ 626-32 } }
80 Citations
The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase.
- Biology, ChemistryBiochimica et biophysica acta
- 1982
L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition.
- BiologyEuropean journal of biochemistry
- 1996
Modification of a previously published procedure allowed overexpression of the holoenzyme in an unproteolysed form and biochemical characterization of the flavoprotein L-aspartate oxidase from Escherichia coli is reported.
Mechanistic Characterization of Escherichia coli l-Aspartate Oxidase from Kinetic Isotope Effects.
- Biology, ChemistryBiochemistry
- 2017
NadB has structurally evolved from succinate dehydrogenase/fumarate reductase-type enzymes to gain the new functionality of oxidizing amino acids while retaining the ability to reduce fumarate, according to previous kinetic and structural data.
L-aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate: fumarate oxidoreductase activity.
- Biology, ChemistryEuropean journal of biochemistry
- 1996
Evidence is presented which suggests that in vitro fumarate can be a valuable alternative to oxygen as a substrate for L-aspartate oxidase, and Steady-state kinetics for the oxidase and thefumarate reductase activity of L- aspartate oxidation were obtained.
Protein A of quinolinate synthetase is the site of oxygen poisoning of pyridine nucleotide coenzyme synthesis in Escherichia coli.
- Biology, ChemistryFree radical biology & medicine
- 1992
Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family.
- Biology, ChemistryStructure
- 1999
Quinolinate synthetase, an iron–sulfur enzyme in NAD biosynthesis
- Biology, ChemistryFEBS letters
- 2005
Purification and characterization of an L-amino acid oxidase from Pseudomonas sp. AIU 813.
- Biology, ChemistryJournal of bioscience and bioengineering
- 2012
Distribution in Different Organisms of Amino Acid Oxidases with FAD or a Quinone As Cofactor and Their Role as Antimicrobial Proteins in Marine Bacteria
- BiologyMarine drugs
- 2015
It is shown that it is possible to recognize different groups of these enzymes and those containing the quinone cofactor are clearly differentiated, and most of the proteins described as antimicrobial because of their capacity to generate hydrogen peroxide belong to the group of LodA-like proteins.
Higher plants contain L-asparate oxidase, the first enzyme of the Escherichia coli quinolinate synthetase system.
- BiologyBiochemical and biophysical research communications
- 1983
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The facile separation of the wild-type quinolinate synthetase A and B proteins out of a nadC mutant suggests that quinolinic acid does not exists as a tightly bound complex.
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A crude enzyme preparation from a nadA mutant of Escherichia coli was used to catalyze the conversion of [14C]aspartic acid into a precursor of quinolinic acid, a key intermediate in the biosynthesis…