| Entry |
|
|---|
| Name |
sterol 24-C-methyltransferase;
Delta24-methyltransferase;
Delta24-sterol methyltransferase;
zymosterol-24-methyltransferase;
S-adenosyl-4-methionine:sterol Delta24-methyltransferase;
SMT1;
24-sterol C-methyltransferase;
S-adenosyl-L-methionine:Delta24(23)-sterol methyltransferase;
phytosterol methyltransferase |
|---|
| Class |
Transferases;
Transferring one-carbon groups;
Methyltransferases
 |
|---|
| Sysname |
S-adenosyl-L-methionine:zymosterol 24-C-methyltransferase |
|---|
| Reaction(IUBMB) |
S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol =
S-adenosyl-L-homocysteine +
24-methylene-5alpha-cholest-8-en-3beta-ol [RN:R04427] |
|---|
| Reaction(KEGG) |
R04427;
(other) R07481
 |
|---|
| Substrate |
S-adenosyl-L-methionine [CPD:C00019];
5alpha-cholesta-8,24-dien-3beta-ol [CPD:C05437] |
|---|
| Product |
S-adenosyl-L-homocysteine [CPD:C00021];
24-methylene-5alpha-cholest-8-en-3beta-ol [CPD:C04525] |
|---|
| Cofactor |
Glutathione [CPD:C00051] |
|---|
| Comment |
Requires glutathione. Acts on a range of sterols with a
24(25)-double bond in the sidechain. While zymosterol is the
preferred substrate it also acts on desmosterol,
5alpha-cholesta-7,24-dien-3beta-ol,
5alpha-cholesta-5,7,24-trien-3beta-ol, 4alpha-methylzymosterol and
others. S-Adenosyl-L-methionine attacks the Si-face of the 24(25)
double bond and the C-24 hydrogen is transferred to C-25 on the Re
face of the double bond. |
|---|
| Pathway |
PATH: ec00100 Steroid biosynthesis
PATH: ec01062 Biosynthesis of terpenoids and steroids
PATH: ec01070 Biosynthesis of plant hormones
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K00559 sterol 24-C-methyltransferase |
|---|
| Genes |
ATH: AT5G13710(SMT1)
OSA: 4342690(Os07g0206700)
OLU: OSTLU_30710
CME: CMP275C
SCE: YML008C(ERG6)
AGO: AGOS_ADR196W
KLA: KLLA0A01738g
PIC: PICST_80971
CAL: CaO19.1631(ERG6)
CGR: CAGL0H04653g
YLI: YALI0F08701g
SPO: SPBC16E9.05(erg6)
NCR: NCU02502 NCU03006
MGR: MGG_10568
ANI: AN7146.2
AFM: AFUA_4G03630 AFUA_4G09190
AOR: AO090011000289
ANG: An14g01590
CNE: CNB03100
UMA: UM03182.1
DDI: DDB_0237965
TBR: Tb10.6k15.3820
TCR: 504191.10 505683.10 510185.10
LMA: LmjF36.2380 LmjF36.2390
NOC: Noc_0994
HMA: pNG6036(mitN)
 |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:5354959]
Moore JT, Gaylor JL.
Isolation and purification of an S-adenosylmethionine: delta
24-sterol methyltransferase from yeast.
J. Biol. Chem. 244 (1969) 6334-40.
Saccharomyces cerevisiae [GN:sce] |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:8597586]
Venkatramesh M, Guo DA, Jia Z, Nes WD.
Mechanism and structural requirements for transformation of
substrates by the (S)-adenosyl-L-methionine:delta 24(25)-sterol
methyl transferase from Saccharomyces cerevisiae.
Biochim. Biophys. Acta. 1299 (1996) 313-24.
Saccharomyces cerevisiae [GN:sce] |
|---|
Reference
Authors
Title
Journal
|
3
Tong, Y., McCourt, B.S., Guo, D., Mangla, A.T., Zhou, W.X., Jenkins,
M.D., Zhou, W., Lopez, M. and Nes, W.D.
, Stereochemical features of C-methylation on the path to
Delta24(28)-methylene and Delta24(28)-ethylidene sterols: studies on
the recombinant phytosterol methyl transferase from Arabidopsis
thaliana.
Tetrahedron Lett. 38 (1997) 6115-6118. |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:9746350]
Bouvier-Nave P, Husselstein T, Benveniste P.
Two families of sterol methyltransferases are involved in the first
and the second methylation steps of plant sterol biosynthesis.
Eur. J. Biochem. 256 (1998) 88-96.
Nicotiana tabacum |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:9606964]
Nes WD, McCourt BS, Zhou WX, Ma J, Marshall JA, Peek LA, Brennan M.
Overexpression, purification, and stereochemical studies of the
recombinant (S)-adenosyl-L-methionine: delta 24(25)- to delta
24(28)-sterol methyl transferase enzyme from Saccharomyces
cerevisiae.
Arch. Biochem. Biophys. 353 (1998) 297-311.
Saccharomyces cerevisiae [GN:sce] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 2.1.1.41
IUBMB Enzyme Nomenclature: 2.1.1.41
ExPASy - ENZYME nomenclature database: 2.1.1.41
BRENDA, the Enzyme Database: 2.1.1.41
CAS: 37257-07-1 |
|---|
