Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase

Antti Nyyssölä (Corresponding Author), Tapani Reinikainen, Matti Leisola

Research output: Contribution to journalArticleScientificpeer-review

25 Citations (Scopus)

Abstract

Glycine betaine is accumulated in cells living in high salt concentrations to balance the osmotic pressure. Glycine sarcosine N-methyltransferase (GSMT) and sarcosine dimethylglycine N-methyltransferase (SDMT) of Ectothiorhodospira halochloris catalyze the threefold methylation of glycine to betaine, with S-adenosylmethionine acting as the methyl group donor. These methyltransferases were expressed in Escherichia coli and purified, and some of their enzymatic properties were characterized. Both enzymes had high substrate specificities and pH optima near the physiological pH. No evidence of cofactors was found. The enzymes showed Michaelis-Menten kinetics for their substrates. The apparent Km and Vmax values were determined for all substrates when the other substrate was present in saturating concentrations. Both enzymes were strongly inhibited by the reaction product S-adenosylhomocysteine. Betaine inhibited the methylation reactions only at high concentrations.
Original languageEnglish
Pages (from-to)2044-2050
Number of pages7
JournalApplied and Environmental Microbiology
Volume67
Issue number5
DOIs
Publication statusPublished - 2001
MoE publication typeA1 Journal article-refereed

Fingerprint

glycine N-methyltransferase
Glycine N-Methyltransferase
Sarcosine
Betaine
betaine
methyltransferases
Methyltransferases
substrate
methylation
Methylation
Ectothiorhodospira
Enzymes
enzyme
enzymes
adenosylhomocysteine
S-Adenosylhomocysteine
S-Adenosylmethionine
enzyme kinetics
S-adenosylmethionine
Osmotic Pressure

Cite this

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title = "Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase",
abstract = "Glycine betaine is accumulated in cells living in high salt concentrations to balance the osmotic pressure. Glycine sarcosine N-methyltransferase (GSMT) and sarcosine dimethylglycine N-methyltransferase (SDMT) of Ectothiorhodospira halochloris catalyze the threefold methylation of glycine to betaine, with S-adenosylmethionine acting as the methyl group donor. These methyltransferases were expressed in Escherichia coli and purified, and some of their enzymatic properties were characterized. Both enzymes had high substrate specificities and pH optima near the physiological pH. No evidence of cofactors was found. The enzymes showed Michaelis-Menten kinetics for their substrates. The apparent Km and Vmax values were determined for all substrates when the other substrate was present in saturating concentrations. Both enzymes were strongly inhibited by the reaction product S-adenosylhomocysteine. Betaine inhibited the methylation reactions only at high concentrations.",
author = "Antti Nyyss{\"o}l{\"a} and Tapani Reinikainen and Matti Leisola",
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language = "English",
volume = "67",
pages = "2044--2050",
journal = "Applied and Environmental Microbiology",
issn = "0099-2240",
publisher = "American Society for Microbiology",
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Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase. / Nyyssölä, Antti (Corresponding Author); Reinikainen, Tapani; Leisola, Matti.

In: Applied and Environmental Microbiology, Vol. 67, No. 5, 2001, p. 2044-2050.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase

AU - Nyyssölä, Antti

AU - Reinikainen, Tapani

AU - Leisola, Matti

PY - 2001

Y1 - 2001

N2 - Glycine betaine is accumulated in cells living in high salt concentrations to balance the osmotic pressure. Glycine sarcosine N-methyltransferase (GSMT) and sarcosine dimethylglycine N-methyltransferase (SDMT) of Ectothiorhodospira halochloris catalyze the threefold methylation of glycine to betaine, with S-adenosylmethionine acting as the methyl group donor. These methyltransferases were expressed in Escherichia coli and purified, and some of their enzymatic properties were characterized. Both enzymes had high substrate specificities and pH optima near the physiological pH. No evidence of cofactors was found. The enzymes showed Michaelis-Menten kinetics for their substrates. The apparent Km and Vmax values were determined for all substrates when the other substrate was present in saturating concentrations. Both enzymes were strongly inhibited by the reaction product S-adenosylhomocysteine. Betaine inhibited the methylation reactions only at high concentrations.

AB - Glycine betaine is accumulated in cells living in high salt concentrations to balance the osmotic pressure. Glycine sarcosine N-methyltransferase (GSMT) and sarcosine dimethylglycine N-methyltransferase (SDMT) of Ectothiorhodospira halochloris catalyze the threefold methylation of glycine to betaine, with S-adenosylmethionine acting as the methyl group donor. These methyltransferases were expressed in Escherichia coli and purified, and some of their enzymatic properties were characterized. Both enzymes had high substrate specificities and pH optima near the physiological pH. No evidence of cofactors was found. The enzymes showed Michaelis-Menten kinetics for their substrates. The apparent Km and Vmax values were determined for all substrates when the other substrate was present in saturating concentrations. Both enzymes were strongly inhibited by the reaction product S-adenosylhomocysteine. Betaine inhibited the methylation reactions only at high concentrations.

U2 - 10.1128/AEM.67.5.2044-2050.2001

DO - 10.1128/AEM.67.5.2044-2050.2001

M3 - Article

VL - 67

SP - 2044

EP - 2050

JO - Applied and Environmental Microbiology

JF - Applied and Environmental Microbiology

SN - 0099-2240

IS - 5

ER -