Evidence for the existence of independent chloromethane- and S-adenosylmethionine-utilizing systems for methylation in Phanerochaete chrysosporium

Article Abstract:

The utilization of C2H3Cl and S-adenosyl-L-(methyl-2H3)methionine as methyl donors in methylation of acetovanillone in whole cells and in cell extracts of Phanerochaete chrysosporium at different stages of growth was reported. Methylation of acetovanillone by the labelled methyl donors was examined in the presence and absence of S-adenosylhomocysteine. The results show the existence of two biochemically distinct systems for O methylation of acetovanillone utilizing SAM and CH3Cl, respectively, as the methyl donor.

User Contributions:

Comment about this article or add new information about this topic:

Comment:  (50-4000 characters)

Name:

E-mail:

Security Code:

Purification and properties of an S-adenosylmethionine: 2,4-disubstituted phenol O-methyltransferase from Phanerochate chrysosporium

Article Abstract:

The purification and characterization of S-adenosylmethionine from Phanerochaete chrysosporium are discussed. Ultrafiltration, anion-exchange chromatography and gel filtration were used in the purification of the enzyme. Its monomeric feature and molecular weight were determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Results show that catabolism or detoxification are involved in the process.

User Contributions:

Comment about this article or add new information about this topic:

Comment:  (50-4000 characters)

Name:

E-mail:

Security Code:

Halomethane:bisulfide/halide ion methyltransferase, an unusual corrinoid enzyme of environmental significance isolated from an aerobic methylotroph using chloromethane as the sole carbon source

Article Abstract:

Halomethane:bisulfide/halide ion methyltransferase is discussed. This unusual corrinoid enzyme of environmental significance has been isolated from an aerobic methylotroph that uses chloromethane as its only carbon source. The unusual methyl-transferase enzyme was purified and characterized.

User Contributions:

Comment about this article or add new information about this topic:

Comment:  (50-4000 characters)

Name:

E-mail:

Security Code: