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Enzymatic Properties of an Extracellular Quinoprotein, Enacyloxin Oxidase
- Source :
- Bioscience, Biotechnology, and Biochemistry. 59:123-125
- Publication Year :
- 1995
- Publisher :
- Informa UK Limited, 1995.
-
Abstract
- Some properties of enacyloxin (ENX) oxidase from Frateuria sp. [Oyama et al., Biosci. Biotech. Biochem., 58, 1914-1917 (1994)] were studied. The enzyme catalyzed the oxidation of ENX IVa, ENX IIIa, and decarbamoyl ENX IVa, specifically. The optimum pH and temperature for the enzyme activity were pH 9.0 and 60°C, respectively. It is suggested that the enzyme is a quinoprotein but its redox cofactor is different from pyrroloquinoline quinone.
- Subjects :
- chemistry.chemical_classification
Oxidase test
biology
Organic Chemistry
General Medicine
Applied Microbiology and Biotechnology
Biochemistry
Redox
Enzyme assay
Cofactor
Analytical Chemistry
chemistry.chemical_compound
Enzyme
chemistry
Pyrroloquinoline quinone
Enacyloxin oxidase
Extracellular
biology.protein
sense organs
Molecular Biology
Biotechnology
Subjects
Details
- ISSN :
- 13476947 and 09168451
- Volume :
- 59
- Database :
- OpenAIRE
- Journal :
- Bioscience, Biotechnology, and Biochemistry
- Accession number :
- edsair.doi...........73f6432cd2b9b7ca076aa1a2e9220131