KEGG   ENZYME: 2.1.1.41Help
Entry
EC 2.1.1.41                 Enzyme                                 
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
BRITE hierarchy
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
Show
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]
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
Steroid biosynthesis
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K00559  
sterol 24-C-methyltransferase
Genes
AQU: 
ATH: 
AT5G13710(SMT1)
ALY: 
GMX: 
MTR: 
CSV: 
RCU: 
POP: 
VVI: 
OSA: 
DOSA: 
Os03t0807600-00(Os03g0807600) Os07t0206700-01(Os07g0206700)
BDI: 
100826864 100834229
SBI: 
SORBI_01g004290(SORBIDRAFT_01g004290) SORBI_09g029600(SORBIDRAFT_09g029600)
ZMA: 
100126899(smt1) 100282501 100286381 541682(SMT)
SMO: 
SELMODRAFT_449609(SMT1-2) SELMODRAFT_449613(SMT1-1)
PPP: 
PHYPADRAFT_228167
OLU: 
OSTLU_30710
OTA: 
Ot03g03760
CME: 
CMP275C
SCE: 
YML008C(ERG6)
AGO: 
AGOS_ADR196W
ERC: 
Ecym_4063
KLA: 
KLLA0A01738g
LTH: 
KLTH0G03806g
PPA: 
PAS_chr3_0371
VPO: 
Kpol_1004p23
ZRO: 
ZYRO0D12606g
CGR: 
CAGL0H04653g
NCS: 
NCAS_0H02570(NCAS0H02570)
NDI: 
NDAI_0C01050(NDAI0C01050)
TPF: 
TPHA_0D02350(TPHA0D02350)
TBL: 
TBLA_0D01630(TBLA0D01630)
TDL: 
TDEL_0A03930(TDEL0A03930)
KAF: 
KAFR_0C05410(KAFR0C05410)
DHA: 
DEHA2D17622g
PIC: 
PICST_80971
PGU: 
PGUG_00661
LEL: 
LELG_02736
CAL: 
CaO19.1631(ERG6) CaO19.9199(ERG6)
CTP: 
CTRG_02396
CDU: 
CD36_82130(ERG6)
COT: 
CORT_0C04430
YLI: 
YALI0F08701g
CLU: 
CLUG_02673
NCR: 
NCU02502 NCU03006
SMP: 
SMAC_01214 SMAC_05969
PAN: 
PODANSg4053
TTT: 
THITE_68084
MTM: 
MYCTH_110670
MGR: 
MGG_10568 MGG_10860
FGR: 
FG02783.1 FG05740.1
NHE: 
NECHADRAFT_33136 NECHADRAFT_59530
VAL: 
VDBG_01914
SSL: 
SS1G_03467
BFU: 
BC1G_07905
ANI: 
AN7146.2
NFI: 
NFIA_029790 NFIA_106980
AFM: 
AFUA_4G03630 AFUA_4G09190
AOR: 
AOR_1_1074144(AO090023000624) AOR_1_480054(AO090011000289)
ANG: 
ANI_1_256124(An14g01590)
AFV: 
AFLA_021770 AFLA_041230 AFLA_110370
ACT: 
ACLA_048560 ACLA_054780
PCS: 
Pc12g14840 Pc21g10300
CIM: 
CIMG_06139 CIMG_08444
CPW: 
CPC735_061140
PBL: 
PAAG_01575
URE: 
UREG_02519 UREG_04245
ABE: 
ARB_05210 ARB_05997
TVE: 
TRV_02353 TRV_06345
AJE: 
HCAG_07564
PNO: 
SNOG_08443
PTE: 
PTT_11273
ZTR: 
MYCGRDRAFT_33363 MYCGRDRAFT_70113(ERG6) MYCGRDRAFT_98820
TML: 
GSTUM_00004489001
SPO: 
SPBC16E9.05(erg6)
CNE: 
CNB03100
CNB: 
CNBB2600
CGI: 
CGB_A3260C
PPL: 
POSPLDRAFT_89636
LBC: 
LACBIDRAFT_184995(erg6)
MPR: 
MPER_11323
CCI: 
CC1G_07728
SCM: 
SCHCODRAFT_55726 SCHCODRAFT_59858 SCHCODRAFT_85906 SCHCODRAFT_85907
UMA: 
UM03182.1
MGL: 
MGL_2877
PGR: 
PGTG_02203 PGTG_17346
MBR: 
MONBRDRAFT_33702
NGR: 
NAEGRDRAFT_81379 NAEGRDRAFT_83028
DDI: 
DDB_G0288907(smt1)
DPP: 
DICPUDRAFT_92595
TBR: 
Tb10.6k15.3820
TCR: 
504191.10 505683.10 510185.10
LMA: 
LMJF_36_2380 LMJF_36_2390(LmSMT)
LIF: 
LINJ_36_2510 LINJ_36_2520
LDO: 
LDBPK_362510 LDBPK_362520
LMI: 
LMXM_36_2380 LMXM_36_2390
LBZ: 
LBRM_35_2600
PTI: 
PHATRDRAFT_10824
TPS: 
THAPSDRAFT_32029 THAPSDRAFT_36203(SMT1)
SRI: 
SELR_21420
 » show all
Taxonomy
Reference
1  [PMID:5354959]
  Authors
Moore JT, Gaylor JL.
  Title
Isolation and purification of an S-adenosylmethionine: delta 24-sterol methyltransferase from yeast.
  Journal
J. Biol. Chem. 244 (1969) 6334-40.
  Organism
Saccharomyces cerevisiae [GN:sce]
Reference
2  [PMID:8597586]
  Authors
Venkatramesh M, Guo DA, Jia Z, Nes WD.
  Title
Mechanism and structural requirements for transformation of substrates by the (S)-adenosyl-L-methionine:delta 24(25)-sterol methyl transferase from Saccharomyces cerevisiae.
  Journal
Biochim. Biophys. Acta. 1299 (1996) 313-24.
  Organism
Saccharomyces cerevisiae [GN:sce]
Reference
3
  Authors
Tong, Y., McCourt, B.S., Guo, D., Mangla, A.T., Zhou, W.X., Jenkins, M.D., Zhou, W., Lopez, M. and Nes, W.D.
  Title
, 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.
  Journal
Tetrahedron Lett. 38 (1997) 6115-6118.
Reference
4  [PMID:9746350]
  Authors
Bouvier-Nave P, Husselstein T, Benveniste P.
  Title
Two families of sterol methyltransferases are involved in the first and the second methylation steps of plant sterol biosynthesis.
  Journal
Eur. J. Biochem. 256 (1998) 88-96.
  Organism
Nicotiana tabacum
Reference
5  [PMID:9606964]
  Authors
Nes WD, McCourt BS, Zhou WX, Ma J, Marshall JA, Peek LA, Brennan M.
  Title
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.
  Journal
Arch. Biochem. Biophys. 353 (1998) 297-311.
  Organism
Saccharomyces cerevisiae [GN:sce]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37257-07-1
DBGET integrated database retrieval system