Rational homotopy theory: Difference between revisions

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Formal spaces: Deleted a statement I beleive to be false and misleading. See Talk page for details. -- Ilya.
 
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{{enzyme
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| Name = 24-methylenesterol C-methyltransferase
| EC_number = 2.1.1.143
| CAS_number =
| IUBMB_EC_number = 2/1/1/143
| GO_code = 0030797
| image =
| width =
| caption =
}}
In [[enzymology]], a '''24-methylenesterol C-methyltransferase''' ({{EC number|2.1.1.143}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
 
:S-adenosyl-L-methionine + 24-methylenelophenol <math>\rightleftharpoons</math> S-adenosyl-L-homocysteine + (Z)-24-ethylidenelophenol
 
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[S-Adenosyl methionine|S-adenosyl methionine]] and [[24-methylenelophenol]], whereas its two [[product (chemistry)|products]] are [[S-adenosylhomocysteine]] and [[(Z)-24-ethylidenelophenol]].
 
This enzyme belongs to the family of [[transferase]]s, specifically those transferring one-carbon group methyltransferases.  The systematic name of this enzyme class is '''S-adenosyl-L-methionine:24-methylenelophenol C-methyltransferase'''. Other names in common use include '''SMT2''', and '''24-methylenelophenol C-241-methyltransferase'''. This enzyme participates in the biosynthesis of [[steroid]]s. 
 
==References==
{{reflist|1}}
* {{cite journal | author = Bouvier-Nave P, Husselstein T, Benveniste P | date = 1998 | title = Two families of sterol methyltransferases are involved in the first and the second methylation steps of plant sterol biosynthesis | journal = Eur. J. Biochem.  | volume = 256 | pages = 88–96  | pmid = 9746350 | doi = 10.1046/j.1432-1327.1998.2560088.x | issue = 1 }}
 
{{transferase-stub}}
 
[[Category:EC 2.1.1]]
[[Category:Enzymes of unknown structure]]

Latest revision as of 22:30, 22 November 2014

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