ExplorEnz: EC 2.1.1.26*

Your query returned 11 entries. Printable version

2.1.1.26

Accepted name:

iodophenol O-methyltransferase

Reaction:

S-adenosyl-L-methionine + 2-iodophenol = S-adenosyl-L-homocysteine + 2-iodophenol methyl ether

Systematic name:

S-adenosyl-L-methionine:2-iodophenol O-methyltransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-95-4

References:

1.	Tomita, K., Cha, C.-J. and Lardy, H.A. Enzymic O-methylation of iodinated phenols and thyroid hormones. J. Biol. Chem. 239 (1964) 1202–1207. [PMID: 14165927]

[EC 2.1.1.26 created 1972]

2.1.1.260

Accepted name:

rRNA small subunit pseudouridine methyltransferase Nep1

Reaction:

S-adenosyl-L-methionine + pseudouridine¹¹⁹¹ in yeast 18S rRNA = S-adenosyl-L-homocysteine + N¹-methylpseudouridine¹¹⁹¹ in yeast 18S rRNA

Other name(s):

Nep1; nucleolar essential protein 1

Systematic name:

S-adenosyl-L-methionine:18S rRNA (pseudouridine¹¹⁹¹-N¹)-methyltransferase

Comments:

This enzyme, which occurs in both prokaryotes and eukaryotes, recognizes specific pseudouridine residues (Ψ) in small subunits of ribosomal RNA based on the local RNA structure. It recognizes Ψ⁹¹⁴ in 16S rRNA from the archaeon Methanocaldococcus jannaschii, Ψ¹¹⁹¹ in yeast 18S rRNA, and Ψ¹²⁴⁸ in human 18S rRNA.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Taylor, A.B., Meyer, B., Leal, B.Z., Kötter, P., Schirf, V., Demeler, B., Hart, P.J., Entian, K.-D. and Wöhnert, J. The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site. Nucleic Acids Res. 36 (2008) 1542–1554. [DOI] [PMID: 18208838]
2.	Wurm, J.P., Meyer, B., Bahr, U., Held, M., Frolow, O., Kötter, P., Engels, J.W., Heckel, A., Karas, M., Entian, K.-D. and Wöhnert, J. The ribosome assembly factor Nep1 responsible for Bowen-Conradi syndrome is a pseudouridine-N¹-specific methyltransferase. Nucleic Acids Res. 38 (2010) 2387–2398. [DOI] [PMID: 20047967]
3.	Meyer, B., Wurm, J.P., Kötter, P., Leisegang, M.S., Schilling, V., Buchhaupt, M., Held, M., Bahr, U., Karas, M., Heckel, A., Bohnsack, M.T., Wöhnert, J. and Entian, K.-D. The Bowen-Conradi syndrome protein Nep1 (Emg1) has a dual role in eukaryotic ribosome biogenesis, as an essential assembly factor and in the methylation of Ψ¹¹⁹¹ in yeast 18S rRNA. Nucleic Acids Res. 39 (2011) 1526–1537. [DOI] [PMID: 20972225]

[EC 2.1.1.260 created 2012]

2.1.1.261

Accepted name:

4-dimethylallyltryptophan N-methyltransferase

Reaction:

S-adenosyl-L-methionine + 4-prenyl-L-tryptophan = S-adenosyl-L-homocysteine + 4-prenyl-L-abrine

For diagram of ergot alkaloid biosynthesis, click here

Glossary:

4-prenyl-L-tryptophan = 4-(3-methylbut-2-enyl)-L-tryptophan = 4-dimethylallyl-L-tryptophan (ambiguous);
4-prenyl-L-abrine = 4-(3-methylbut-2-enyl)-L-abrine = 4-dimethylallyl-L-abrine (ambiguous)

Other name(s):

fgaMT (gene name); easF (gene name)

Systematic name:

S-adenosyl-L-methionine:4-(3-methylbut-2-enyl)-L-tryptophan N-methyltransferase

Comments:

The enzyme catalyses a step in the pathway leading to biosynthesis of ergot alkaloids in certain fungi.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Rigbers, O. and Li, S.M. Ergot alkaloid biosynthesis in Aspergillus fumigatus. Overproduction and biochemical characterization of a 4-dimethylallyltryptophan N-methyltransferase. J. Biol. Chem. 283 (2008) 26859–26868. [DOI] [PMID: 18678866]

[EC 2.1.1.261 created 2012]

2.1.1.262

Accepted name:

squalene methyltransferase

Reaction:

2 S-adenosyl-L-methionine + squalene = 2 S-adenosyl-L-homocysteine + 3,22-dimethyl-1,2,23,24-tetradehydro-2,3,22,23-tetrahydrosqualene (overall reaction)
(1a) S-adenosyl-L-methionine + squalene = S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrosqualene
(1b) S-adenosyl-L-methionine + 3-methyl-1,2-didehydro-2,3-dihydrosqualene = S-adenosyl-L-homocysteine + 3,22-dimethyl-1,2,23,24-tetradehydro-2,3,22,23-tetrahydrosqualene

For diagram of botryococcus braunii BOT22 squalene and botrycoccene biosynthesis, click here

Other name(s):

TMT-1; TMT-2

Systematic name:

S-adenosyl-L-methionine:squalene C-methyltransferase

Comments:

Two isoforms differing in their specificity were isolated from the green alga Botryococcus braunii BOT22. TMT-1 gave more of the dimethylated form whereas TMT2 gave more of the monomethylated form.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Niehaus, T.D., Kinison, S., Okada, S., Yeo, Y.S., Bell, S.A., Cui, P., Devarenne, T.P. and Chappell, J. Functional identification of triterpene methyltransferases from Botryococcus braunii race B. J. Biol. Chem. 287 (2012) 8163–8173. [DOI] [PMID: 22241476]

[EC 2.1.1.262 created 2012]

2.1.1.263

Accepted name:

botryococcene C-methyltransferase

Reaction:

2 S-adenosyl-L-methionine + C₃₀ botryococcene = 2 S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene (overall reaction)
(1a) S-adenosyl-L-methionine + C₃₀ botryococcene = S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene
(1b) S-adenosyl-L-methionine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene = S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
(2a) S-adenosyl-L-methionine + C₃₀ botryococcene = S-adenosyl-L-homocysteine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene
(2b) S-adenosyl-L-methionine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene = S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene

For diagram of botryococcus braunii BOT22 squalene and botrycoccene biosynthesis, click here

Glossary:

C₃₀ botryococcene = (10S,13R)-10-ethenyl-2,6,10,13,17,21-hexamethyldocosa-2,5,11,16,20-pentaene
3-methyl-1,2-didehydro-2,3-dihydrobotryococcene = showacene
20-methyl-21,22-didehydro-20,21-dihydrobotryococcene = isoshowacene

Other name(s):

TMT-3

Systematic name:

S-adenosyl-L-methionine:botryococcene C-methyltransferase

Comments:

Isolated from the green alga Botryococcus braunii BOT22. Shows a very weak activity with squalene.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc

References:

1.	Niehaus, T.D., Kinison, S., Okada, S., Yeo, Y.S., Bell, S.A., Cui, P., Devarenne, T.P. and Chappell, J. Functional identification of triterpene methyltransferases from Botryococcus braunii race B. J. Biol. Chem. 287 (2012) 8163–8173. [DOI] [PMID: 22241476]

[EC 2.1.1.263 created 2012]

2.1.1.264

Accepted name:

23S rRNA (guanine²⁰⁶⁹-N⁷)-methyltransferase

Reaction:

S-adenosyl-L-methionine + guanine²⁰⁶⁹ in 23S rRNA = S-adenosyl-L-homocysteine + N⁷-methylguanine²⁰⁶⁹ in 23S rRNA

Other name(s):

rlmK (gene name); 23S rRNA m⁷G²⁰⁶⁹ methyltransferase

Systematic name:

S-adenosyl-L-methionine:23S rRNA (guanine²⁰⁶⁹-N⁷)-methyltransferase

Comments:

The enzyme specifically methylates guanine²⁰⁶⁹ at position N7 in 23S rRNA. In γ-proteobacteria the enzyme also catalyses EC 2.1.1.173, 23S rRNA (guanine²⁴⁴⁵-N²)-methyltransferase, while in β-proteobacteria the activities are carried out by separate proteins [1]. The enzyme from the γ-proteobacterium Escherichia coli has RNA unwinding activity as well [1].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Kimura, S., Ikeuchi, Y., Kitahara, K., Sakaguchi, Y., Suzuki, T. and Suzuki, T. Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity. Nucleic Acids Res. 40 (2012) 4071–4085. [DOI] [PMID: 22210896]

[EC 2.1.1.264 created 2012]

2.1.1.265

Accepted name:

tellurite methyltransferase

Reaction:

S-adenosyl-L-methionine + tellurite = S-adenosyl-L-homocysteine + methanetelluronate

Other name(s):

TehB

Systematic name:

S-adenosyl-L-methionine:tellurite methyltransferase

Comments:

The enzyme is involved in the detoxification of tellurite. It can also methylate selenite and selenium dioxide.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Liu, M., Turner, R.J., Winstone, T.L., Saetre, A., Dyllick-Brenzinger, M., Jickling, G., Tari, L.W., Weiner, J.H. and Taylor, D.E. Escherichia coli TehB requires S-adenosylmethionine as a cofactor to mediate tellurite resistance. J. Bacteriol. 182 (2000) 6509–6513. [DOI] [PMID: 11053398]
2.	Choudhury, H.G., Cameron, A.D., Iwata, S. and Beis, K. Structure and mechanism of the chalcogen-detoxifying protein TehB from Escherichia coli. Biochem. J. 435 (2011) 85–91. [DOI] [PMID: 21244361]

[EC 2.1.1.265 created 2012]

2.1.1.266

Accepted name:

23S rRNA (adenine²⁰³⁰-N⁶)-methyltransferase

Reaction:

S-adenosyl-L-methionine + adenine²⁰³⁰ in 23S rRNA = S-adenosyl-L-homocysteine + N⁶-methyladenine²⁰³⁰ in 23S rRNA

Other name(s):

YhiR protein; rlmJ (gene name); m⁶A²⁰³⁰ methyltransferase

Systematic name:

S-adenosyl-L-methionine:23S rRNA (adenine²⁰³⁰-N⁶)-methyltransferase

Comments:

The recombinant RlmJ protein is most active in methylating deproteinized 23S ribosomal subunit, and does not methylate the completely assembled 50S subunits [1].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

Golovina, A.Y., Dzama, M.M., Osterman, I.A., Sergiev, P.V., Serebryakova, M.V., Bogdanov, A.A. and Dontsova, O.A. The last rRNA methyltransferase of E. coli revealed: the yhiR gene encodes adenine-N6 methyltransferase specific for modification of A²⁰³⁰ of 23S ribosomal RNA. RNA 18 (2012) 1725–1734. [DOI] [PMID: 22847818]

[EC 2.1.1.266 created 2013]

2.1.1.267

Accepted name:

flavonoid 3′,5′-methyltransferase

Reaction:

(1) S-adenosyl-L-methionine + a 3′-hydroxyflavonoid = S-adenosyl-L-homocysteine + a 3′-methoxyflavonoid
(2) S-adenosyl-L-methionine + a 5′-hydroxy-3′-methoxyflavonoid = S-adenosyl-L-homocysteine + a 3′,5′-dimethoxyflavonoid

For diagram of anthocyanidin glucoside biosynthesis, click here

Glossary:

delphinidin = 3,3′,4′,5,5′,7-hexahydroxyflavylium
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
myricetin = 3,3′,4′,5,5′,7-hexahydroxyflavone
quercetin = 3,3′,4′,5,7-pentahydroxyflavone

Other name(s):

AOMT; CrOMT2

Systematic name:

S-adenosyl-L-methionine:flavonoid 3′-O-methyltransferase

Comments:

Isolated from Vitis vinifera (grape) [2]. Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. The enzyme from Catharanthus roseus was most active with myricetin [1].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc

References:

1.	Cacace, S., Schröder, G., Wehinger, E., Strack, D., Schmidt, J. and Schröder, J. A flavonol O-methyltransferase from Catharanthus roseus performing two sequential methylations. Phytochemistry 62 (2003) 127–137. [DOI] [PMID: 12482447]
2.	Hugueney, P., Provenzano, S., Verries, C., Ferrandino, A., Meudec, E., Batelli, G., Merdinoglu, D., Cheynier, V., Schubert, A. and Ageorges, A. A novel cation-dependent O-methyltransferase involved in anthocyanin methylation in grapevine. Plant Physiol. 150 (2009) 2057–2070. [DOI] [PMID: 19525322]

[EC 2.1.1.267 created 2013, modified 2014]

2.1.1.268

Accepted name:

tRNA^Thr (cytosine³²-N³)-methyltransferase

Reaction:

(1) S-adenosyl-L-methionine + cytosine³² in tRNA^Thr = S-adenosyl-L-homocysteine + N³-methylcytosine³² in tRNA^Thr
(2) S-adenosyl-L-methionine + cytosine³² in tRNA^Ser = S-adenosyl-L-homocysteine + N³-methylcytosine³² in tRNA^Ser

Other name(s):

ABP140; Trm140p

Systematic name:

S-adenosyl-L-methionine:tRNA^Thr (cytosine³²-N³)-methyltransferase

Comments:

The enzyme from Saccharomyces cerevisiae specifically methylates cytosine³² in tRNA^Thr and in tRNA^Ser.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Noma, A., Yi, S., Katoh, T., Takai, Y., Suzuki, T. and Suzuki, T. Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae. RNA 17 (2011) 1111–1119. [DOI] [PMID: 21518805]
2.	D'Silva, S., Haider, S.J. and Phizicky, E.M. A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop. RNA 17 (2011) 1100–1110. [DOI] [PMID: 21518804]

[EC 2.1.1.268 created 2013]

2.1.1.269

Accepted name:

dimethylsulfoniopropionate demethylase

Reaction:

S,S-dimethyl-β-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate

For diagram of 3-(dimethylsulfonio)propanoate metabolism, click here

Glossary:

S,S-dimethyl-β-propiothetin = 3-(S,S-dimethylsulfonio)propanoate

Other name(s):

dmdA (gene name); dimethylsulfoniopropionate-dependent demethylase A

Systematic name:

S,S-dimethyl-β-propiothetin:tetrahydrofolate S-methyltransferase

Comments:

The enzyme from the marine bacteria Pelagibacter ubique and Ruegeria pomeroyi are specific towards S,S-dimethyl-β-propiothetin. They do not demethylate glycine-betaine [1,2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Jansen, M. and Hansen, T.A. Tetrahydrofolate serves as a methyl acceptor in the demethylation of dimethylsulfoniopropionate in cell extracts of sulfate-reducing bacteria. Arch. Microbiol. 169 (1998) 84–87. [PMID: 9396840]
2.	Reisch, C.R., Moran, M.A. and Whitman, W.B. Dimethylsulfoniopropionate-dependent demethylase (DmdA) from Pelagibacter ubique and Silicibacter pomeroyi. J. Bacteriol. 190 (2008) 8018–8024. [DOI] [PMID: 18849431]
3.	Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B. and Lanzilotta, W.N. Structures of dimethylsulfoniopropionate-dependent demethylase from the marine organism Pelagibacter ubique. Protein Sci. 21 (2012) 289–298. [DOI] [PMID: 22162093]

[EC 2.1.1.269 created 2013]