Entry Name squalene methyltransferase;
Class Transferases;BRITE hierarchy
Sysname S-adenosyl-L-methionine:squalene C-methyltransferase
Reaction(IUBMB) 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) [RN:
R10169 ];
(1a) S-adenosyl-L-methionine + squalene = S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrosqualene [RN:
R10167 ];
(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 [RN:
R10168 ]
Reaction(KEGG) Substrate S-adenosyl-L-methionine [CPD:
C00019 ];
squalene [CPD:
C00751 ];
3-methyl-1,2-didehydro-2,3-dihydrosqualene [CPD:
C20411 ]
Product S-adenosyl-L-homocysteine [CPD:
C00021 ];
3,22-dimethyl-1,2,23,24-tetradehydro-2,3,22,23-tetrahydrosqualene [CPD:
C20412 ];
3-methyl-1,2-didehydro-2,3-dihydrosqualene [CPD:
C20411 ]
Comment 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.
History EC 2.1.1.262 created 2012
Orthology K21541 squalene methyltransferase
Reference Authors Niehaus TD, Kinison S, Okada S, Yeo YS, Bell SA, Cui P, Devarenne TP, Chappell J
Title Functional identification of triterpene methyltransferases from Botryococcus braunii race B.
Journal Sequence Other DBs ExPASy - ENZYME nomenclature database: 2.1.1.262
