Purification and characterization of a monohalomethane-producing enzyme S-adenosyl-L-methionine: Halide ion methyltransferase from a marine microalga, Pavlova pinguis

Article abstract of DOI:10.1271/bbb.65.2397

A monohalomethane-producing enzyme, S-adenosyl-L-methionine-dependent halide ion methyltransferase (EC 2.1.1.-) was purified from the marine microalga Pavlova pinguis by two anion exchange, hydroxyapatite and gel filtration chromatographies. The methyltransferase was a monomeric molecule having a molecular weight of 29,000. The enzyme had an isoelectric point at 5.3, and was optimally active at pH 8.0. The K_m, for iodide and SAM were 12 mM and 12 μM, respectively, which were measured using a partially purified enzyme. Various metal ions had no significant effect on methyl iodide production, suggesting that the enzyme does not require metal ions. The enzyme reaction strictly depended on SAM as a methyl donor, and the enzyme catalyzed methylation of the I , Br , and Cl^- to corresponding monohalomethanes and of bisulfide to methyl mercaptan.

Full text of DOI:10.1271/bbb.65.2397

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Purification and Characterization of a
Monohalomethane-producing Enzyme S-adenosyl-
L-methionine: Halide Ion Methyltransferase from a
Marine Microalga, Pavlova pinguis
Noboru OHSAWAa, Mika TSUJITAb, Satoru MORIKAWAb & Nobuya ITOHa
a Biotechnology Research Center, Toyama Prefectural University
b Department of Applied Chemistry and Biotechnology, Faculty of Engineering, Fukui
University
Published online: 22 May 2014.
To cite this article: Noboru OHSAWA, Mika TSUJITA, Satoru MORIKAWA & Nobuya ITOH (2001) Purification and
Characterization of a Monohalomethane-producing Enzyme S-adenosyl-L-methionine: Halide Ion Methyltransferase from
a Marine Microalga, Pavlova pinguis, Bioscience, Biotechnology, and Biochemistry, 65:11, 2397-2404, DOI: 10.1271/
bbb.65.2397
To link to this article: http://dx.doi.org/10.1271/bbb.65.2397
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