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Purification and characterization of molybdenum-containing aldehyde dehydrogenase that oxidizes benzyl maltol derivative from Pseudomonas nitroreducens SB32154.
- Source :
-
Bioscience, Biotechnology & Biochemistry . Nov2020, Vol. 84 Issue 11, p2390-2400. 11p. - Publication Year :
- 2020
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Abstract
- Maltol derivatives are used in a variety of fields due to their metal-chelating abilities. In the previous study, it was found that cytochrome P450 monooxygenase, P450nov, which has the ability to effectively convert the 2-methyl group in a maltol derivative, transformed 3-benzyloxy-2-methyl-4-pyrone (BMAL) to 2-(hydroxymethyl)-3-(phenylmethoxy)-4H-pyran-4-one (BMAL-OH) and slightly to 3-benzyloxy-4-oxo-4 H-pyran-2-carboxaldehyde (BMAL-CHO). We isolated Pseudomonas nitroreducens SB32154 with the ability to convert BMAL-CHO to BMAL-COOH from soil. The enzyme responsible for aldehyde oxidation, a BMAL-CHO dehydrogenase, was purified from P. nitroreducens SB32154 and characterized. The purified BMAL-CHO dehydrogenase was found to be a xanthine oxidase family enzyme with unique structure of heterodimer composed of 75 and 15 kDa subunits containing a molybdenum cofactor and [Fe-S] clusters, respectively. The enzyme showed broad substrate specificity toward benzaldehyde derivatives. Furthermore, one-pot conversion of BMAL to BMAL-COOH via BMAL-CHO by the combination of the BMAL-CHO dehydrogenase with P450nov was achieved. Enzymatic conversion of BMAL to BMAL-COOH by P450nov from Novosphingobium sp. SB32149 and BMAL-CHO dehydrogenase from Pseudomonas nitroreducens SB32154 [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09168451
- Volume :
- 84
- Issue :
- 11
- Database :
- Academic Search Index
- Journal :
- Bioscience, Biotechnology & Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 146515222
- Full Text :
- https://doi.org/10.1080/09168451.2020.1799749