Sarcosine/dimethylglycine N-methyltransferase

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Sarcosine/dimethylglycine N-methyltransferase
Identifiers
EC no. 2.1.1.157
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Sarcosine/dimethylglycine N-methyltransferase (EC 2.1.1.157, ApDMT, sarcosine-dimethylglycine methyltransferase, SDMT, sarcosine dimethylglycine N-methyltransferase, S-adenosyl-L-methionine:N,N-dimethylglycine N-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:sarcosine(or N,N-dimethylglycine) N-methyltransferase (N,N-dimethylglycine(or betaine)-forming). [1] [2] [3] This enzyme catalyses the following chemical reaction

2 S-adenosyl-L-methionine + sarcosine 2 S-adenosyl-L-homocysteine + betaine (overall reaction)
(1a) S-adenosyl-L-methionine + sarcosine S-adenosyl-L-homocysteine + N,N-dimethylglycine
(1b) S-adenosyl-L-methionine + N,N-dimethylglycine S-adenosyl-L-homocysteine + betaine

This enzyme participates in biosynthesis of betaine from glycine in cyanobacterium Aphanocthece halophytica .

Related Research Articles

<span class="mw-page-title-main">Betaine—homocysteine S-methyltransferase</span> Class of enzymes

In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively:

<span class="mw-page-title-main">Glycine N-methyltransferase</span>

In enzymology, a glycine N-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a theobromine synthase is an enzyme that catalyzes the chemical reaction

In enzymology, a choline dehydrogenase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Choline oxidase</span>

In enzymology, a choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Betaine-aldehyde dehydrogenase</span> Enzyme

In enzymology, a betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction

Glycine/sarcosine N-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:glycine(or sarcosine) N-methyltransferase . This enzyme catalyses the following chemical reaction

Dimethylglycine N-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:N,N-dimethylglycine N-methyltransferase (betaine-forming). This enzyme catalyses the following chemical reaction

Glycine/sarcosine/dimethylglycine N-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:glycine(or sarcosine or N,N-dimethylglycine) N-methyltransferase . This enzyme catalyses the following chemical reaction

Demethylmenaquinone methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:demethylmenaquinone methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (uridine2552-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uridine2552-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (guanine966-N2)-methyltransferase (EC 2.1.1.171, yhhF (gene), rsmD (gene), m2G966 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (guanine966-N2)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (uracil1939-C5)-methyltransferase (EC 2.1.1.190, RumA, RNA uridine methyltransferase A, YgcA) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uracil1939-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

Cobalt-precorrin-5B (C1)-methyltransferase (EC 2.1.1.195), cobalt-precorrin-6A synthase, CbiD (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:cobalt-precorrin-5B (C1)-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (guanine10-N2)-dimethyltransferase (EC 2.1.1.213, PAB1283, N(2),N(2)-dimethylguanosine tRNA methyltransferase, Trm-G10, PabTrm-G10, PabTrm-m2 2G10 enzyme) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (guanine10-N2)-dimethyltransferase. This enzyme catalyses the following chemical reaction

tRNA (guanine37-N1)-methyltransferase (EC 2.1.1.228, TrmD, tRNA (m1G37) methyltransferase, transfer RNA (m1G37) methyltransferase, Trm5p, TRMT5, tRNA-(N1G37) methyltransferase, MJ0883 (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (guanine37-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

[Fructose-bisphosphate aldolase]-lysine N-methyltransferase (EC 2.1.1.259) is an enzyme that catalyses the following chemical reaction

4-dimethylallyltryptophan N-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:4-(3-methylbut-2-enyl)-L-tryptophan N-methyltransferase. This enzyme catalyses the following chemical reaction

Squalene methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:squalene C-methyltransferase. This enzyme catalyses the following chemical reaction

Botryococcene C-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:botryococcene C-methyltransferase.

References

  1. Nyyssola A, Kerovuo J, Kaukinen P, von Weymarn N, Reinikainen T (July 2000). "Extreme halophiles synthesize betaine from glycine by methylation". The Journal of Biological Chemistry. 275 (29): 22196–201. doi: 10.1074/jbc.M910111199 . PMID   10896953.
  2. Nyyssölä A, Reinikainen T, Leisola M (May 2001). "Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase". Applied and Environmental Microbiology. 67 (5): 2044–50. doi:10.1128/AEM.67.5.2044-2050.2001. PMC   92834 . PMID   11319079.
  3. Waditee R, Tanaka Y, Aoki K, Hibino T, Jikuya H, Takano J, Takabe T, Takabe T (February 2003). "Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica". The Journal of Biological Chemistry. 278 (7): 4932–42. doi: 10.1074/jbc.M210970200 . PMID   12466265.