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Purification and characterization of a novel O-methyltransferase from Flammulina velutipes.
- Source :
-
Bioscience, biotechnology, and biochemistry [Biosci Biotechnol Biochem] 2014; Vol. 78 (5), pp. 806-11. Date of Electronic Publication: 2014 May 28. - Publication Year :
- 2014
-
Abstract
- An enzyme catalyzing the methylation of phenolic hydroxyl groups in polyphenols was identified from mycelial cultures of edible mushrooms to synthesize O-methylated polyphenols. Enzyme activity was measured to assess whether methyl groups were introduced into (-)-epigallocatechin-3-O-gallate (EGCG) using SAM as a methyl donor, and (-)-epigallocatechin-3-O-(3-O-methyl)-gallate (EGCG3″Me), (-)-epigallocatechin-3-O-(4-O-methyl)-gallate (EGCG4″Me), and (-)-epigallocatechin-3-O-(3,5-O-dimethyl)-gallate (EGCG3″,5″diMe) peaks were detected using crude enzyme preparations from mycelial cultures of Flammulina velutipes. The enzyme was purified using chromatographic and two-dimensional electrophoresis. The purified enzyme was subsequently analyzed on the basis of the partial amino acid sequence using LC-MS/MS. Partial amino acid sequencing identified the 17 and 12 amino acid sequences, VLEVGTLGGYSTTWLAR and TGGIIIVDNVVR. In database searches, these sequences showed high identity with O-methyltransferases from other mushroom species and completely matched 11 of 17 and 9 of 12 amino acids from five other mushroom O-methyltransferases.
Details
- Language :
- English
- ISSN :
- 1347-6947
- Volume :
- 78
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Bioscience, biotechnology, and biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 25035983
- Full Text :
- https://doi.org/10.1080/09168451.2014.912117