Any feedback?
Information on EC 2.1.1.142 - cycloartenol 24-C-methyltransferase
for references in articles please use BRENDA:EC2.1.1.142Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.1.1.142 cycloartenol 24-C-methyltransferaseIUBMB Comments
S-Adenosyl-L-methionine methylates the Si face of the 24(25)-double bond with elimination of a hydrogen atom from the pro-Z methyl group at C-25.
Specify your search results
Word Map
- 2.1.1.142
- ergosterol
- sitosterol
- phytosterols
- lanosterol
-
24-ethyl
-
delta24-sterols
- azasterols
-
24-alkylated
-
c24-methylation
- campesterol
-
c1-transfer
-
schizotrypanum
- obtusifoliol
-
delta7
- fecosterol
- analysis
- synthesis
- degradation
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
24-smt, sterol methyltransferase, sterol methyl transferase, sterol c24-methyltransferase, sam:smt, sterol c-24 methyltransferase, ghsmt2-1, ghsmt2-2, sterol methyltransferase2, smt2-1, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-adenosyl-L-methionine-DELTA24-sterol methyltransferase
-
-
-
-
(S)-adenosyl-L-methionine:DELTA24(25)-sterol methyltransferase
-
-
-
-
DELTA24(25)-sterol methyltransferase
-
-
-
-
DELTA24-sterol methyltransferase
-
-
-
-
Erg6
SAM-DELTA24 sterol transmethylase
-
-
-
-
SAM:SMT
SMT
SMT1
SMT2
sterol C-methyltransferase
-
-
-
-
sterol C24-methyltransferase
sterol methyltransferase
zymosterol-24-methyltransferase
-
-
-
-
additional information
-
the enzyme belongs to a family of sterol 24-C-methyltransferases that perform distinct C1-activities, two different alkylations at C24 or C28, alkylation of the latter affects membrane fluidity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol = S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol = S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
mechanism
-
S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol = S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
-
-
-
-
S-adenosyl-L-methionine + cycloartenol = S-adenosyl-L-homocysteine + cyclolaudenol
mechanism
-
S-adenosyl-L-methionine + cycloartenol = S-adenosyl-L-homocysteine + cyclolaudenol
structure-function relationship
-
S-adenosyl-L-methionine + cycloartenol = S-adenosyl-L-homocysteine + cyclolaudenol
mechanism, S-adenosyl-L-methionine mehtylates the Si face of the 24(25)-double bond with elimination of a hydrogen atom from the pro-Z methyl group at C-25
-
S-adenosyl-L-methionine + cycloartenol = S-adenosyl-L-homocysteine + cyclolaudenol
kinetic and inhibition mechanism
-
S-adenosyl-L-methionine + cycloartenol = S-adenosyl-L-homocysteine + cyclolaudenol
steric substrate preferences: 3beta-hydroxy group, planar nucleus, side chain orientated into right-handed structure
-
S-adenosyl-L-methionine + cycloartenol = S-adenosyl-L-homocysteine + cyclolaudenol
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transfer of methyl group
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:cycloartenol 24-C-methyltransferase
S-Adenosyl-L-methionine methylates the Si face of the 24(25)-double bond with elimination of a hydrogen atom from the pro-Z methyl group at C-25.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37257-07-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3beta,13alpha,17alpha)-3-fluorolanost-8,24-diene + S-adenosyl-L-methionine
(3beta,13alpha,17alpha)-3-fluoro-24-methylidenelanost-8-ene + S-adenosyl-L-homocysteine
-
-
conversion into a single 24(28)-methylene product
-
?
14alpha-methylzymosterol + S-adenosyl-L-methionine
14alpha-methyl-24-methylenezymosterol + S-adenosyl-L-homocysteine
-
14alpha-methylzymosterol is 14alpha-methylcholesta-8,24-dien-3beta-ol
-
-
?
24(28)-methylene lophenol + S-adenosyl-L-methionine
24(28)Z-ethylidene lophenol + S-adenosyl-L-homocysteine
-
-
-
?
24,25-dehydro-27-methenyl-cycloartenol + S-adenosyl-L-methionine
?
-
CA-8, i.e. cycloartenol nucleus substrate analogue with double bond at C8, an enzyme inhibitor, is a poor substrate
-
-
?
24,25-dehydro-27-methylene-cycloartenol + S-adenosyl-L-methionine
?
-
CA-14, i.e. cycloartenol nucleus substrate analogue with double bond at C14, an enzyme inhibitor, is a poor substrate
-
-
?
24,25-dehydropollinastanol + S-adenosyl-L-methionine
?
-
24,25-dehydropollinastanol is 14alpha-methyl-9beta,19-cyclo-5alpha-cholest-24-en-3beta-ol
-
-
?
24-fluorocycloartenol + S-adenosyl-L-methionine
(24R)-24-methyl-24-fluoro-cycloart-25-en-3beta-ol + S-adenosyl-L-homocysteine
-
allylic substrate analog
-
-
?
26,27-dehydrozymosterol + S-adenosyl-L-methionine
26-homocholesta-8(9),23(24)E,26(26')-trienol + 26-homocholesta-8(9),26(26')-3beta,24beta-dienol
-
-
-
-
?
26-difluorocycloartenol + S-adenosyl-L-methionine
26-difluoro-25-hydroxy-24-methylcycloartanol + S-adenosyl-L-homocysteine
-
-
products are 26-difluorocyclolaudenol (monol), 26-difluoro-24(28)-methylenecycloartanol (monol) and 26-difluoro-25-hydroxy-24-methylcycloartanol (diol) distributed in a ratio of 6:4:90 at approximately 1% yield
-
?
26-fluorocycloartenol + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
-
reaction affords a bound intermediate that converts in favour of the DELTA25(27)-olefin product via the cyclolaudenol cation formed initially during the C-24-methylation reaction
hydrolysis of the product gives 26-fluoro-25-hydroxy-24-methylcycloartanol
-
?
26-homocycloartenol + S-adenosyl-L-methionine
24-methylene-26-homocycloartenol + S-adenosyl-L-homocysteine
-
-
single product
-
?
31-norcycloartenol + S-adenosyl-L-methionine
24-methylene-31-norcycloartenol + S-adenosyl-L-homocysteine
-
31-norcycloartenol is 4,14alpha-dimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3beta-ol
-
-
?
agnosterol + S-adenosyl-L-methionine
24-methyleneagnosterol + S-adenosyl-L-homocysteine
-
agnosterol is 4,4,14alpha-trimethyl-5alpha-cholesta-7(8),9(11),24-trien-3beta-ol
-
-
?
cycloartenol + S-adenosyl-L-methionine
(24S)-24-methylcycloart-25-en-3beta-ol + S-adenosyl-L-homocysteine
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24(28)-methylene cycloartanol + S-adenosyl-L-homocysteine
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
cycloartenol 3-ketone + S-adenosyl-L-methionine
?
-
cycloartenol 3-ketone is 4,4,14alpha-trimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3-one
-
-
?
cyclobranol + S-adenosyl-L-methionine
9beta-25-methylidene-9,19-cyclolanost-1-ene-1,3-diol + S-adenosyl-L-homocysteine
-
-
-
-
?
desmosterol + S-adenosyl-L-methionine
24-methylenedesmosterol + S-adenosyl-L-homocysteine
-
desmosterol is 5alpha-cholesta-5,24-dien-3beta-ol
-
-
?
ergosta-7,24(28)-dienol + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
fecosterol and ergosta-7,24(28)-dienol which lack C4-and C14-methyl groups in the nucleus are catalyzed equally effectively by SMT2-2 as the natural substrate 24(28)-methylene lophenol
-
-
?
fecosterol + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
fecosterol and ergosta-7,24(28)-dienol which lack C4-and C14-methyl groups in the nucleus are catalyzed equally effectively by SMT2-2 as the natural substrate 24(28)-methylene lophenol
-
-
?
lanost-24-enol + S-adenosyl-L-methionine
24-methylene-lanost-24-erol + S-adenosyl-L-homocysteine
-
lanost-24-enol is 4,4,14alpha-trimethyl-5alpha-cholesta-9(11),24-dien-3beta-ol
-
-
?
lanosta-7,24-dienol + S-adenosyl-L-methionine
24-methylene-lanost-7,24-dienol + S-adenosyl-L-homocysteine
-
lanosta-7,24-dienol is 4,4,14alpha-trimethyl-5alpha-cholesta-7(8),24-dien-3beta-ol
-
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
lanosterol + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + 14alpha-methylzymosterol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 24(28)-methylene cycloartenol
S-adenosyl-L-homocysteine + 24(28)-ethylidene cycloartenol
-
-
-
?
S-adenosyl-L-methionine + 24(28)-methylene lophenol
S-adenosyl-L-homocysteine + 24(28)-ethylidene lophenol
-
-
-
?
S-adenosyl-L-methionine + 24(28)-methylenecycloartanol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 24(28)-methylenelanosterol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 24(28)-methylenelophenol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 24-dehydropollinstanol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 24-fluorocycloartenol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 24-methyl-9,19-cyclolanost-24-en-3-ol
S-adenosyl-L-homocysteine + 25-methyl-24-methylidene-9,19-cyclolanostan-3-ol
-
i.e. cyclobranol
-
-
?
S-adenosyl-L-methionine + 26,27-dehydrocycloartenol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 26,27-dehydrolanosterol
?
-
Formation of a reversibly bound enzymesubstrate complex, followed by catalysis to an intermediate that can be converted to a methyl product or the intermediate can be intercepted through covalent modification and hence irreversible inhibition, lanosterol or 26,27-dehydrolanosterol can lead to distinct intermediates that convert to methylated sterol products
-
-
?
S-adenosyl-L-methionine + 30,31-dinorcycloartenol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol
S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
-
3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 work in concert to control carbon flux into end-product sterols. Sterol composition can be controlled by the temporal activity of the promoters driving transgene expression
-
-
?
S-adenosyl-L-methionine + cholesta-5,20(22)E,24-trienol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + cholesta-5,7,22E,24-tetraenol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + cholesta-5,7,24-trienol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + cholesta-7,24-dienol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24(28)-methylenecycloartanol
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24(28)methylene cycloartanol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24-methylenecycloartanol
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + cyclolaudenol + 24(28)-methylene cycloartanol
-
-
-
?
S-adenosyl-L-methionine + desmosterol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24beta-methyl lanosta-8,25(27)-enol + 24(28)-methylene lanosterol
-
-
-
?
S-adenosyl-L-methionine + obtusifoliol
S-adenosyl-L-homocysteine + ?
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24(28)-methylene cycloartanol + S-adenosyl-L-homocysteine
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24(28)-methylene cycloartanol + S-adenosyl-L-homocysteine
optimal substrate for SMT1
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
SMT2 has a position-specific substrate specificity for DELTA24(25)-sterols and contains a single active center to catalyze the consecutive C1-transfer activities by substrate reaction channels similar to the fungal SMT1
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
-
single product
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
rate-limiting initial step in the conversion of phytosterol
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
64% of the effectiveness with 24(28)-methylene lophenol
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
cycloartenol is 4,4,14alpha-trimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3beta-ol
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
cycloartenol is 4,4,14alpha-trimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3beta-ol
-
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
lanosterol is 4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3-ol
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
regiospecific
-
-
?
S-adenosyl-L-methionine + 31-norcycloartenol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 31-norcycloartenol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24(28)-methylenecycloartanol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24(28)-methylenecycloartanol
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24-methylenecycloartanol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24-methylenecycloartanol
-
active-site topography and reaction mechanisms analyzed with substrate analogs
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24-methylenecycloartanol
-
fluorine-modified sterol side chains designed to examine the electrophilic nature of the common C-methylation reaction affecting C1 and C2-activities, might retard C-methylation reaction to afford protein alkylation
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24-methylenecycloartanol
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + ?
-
successive C-methylations of the DELTA24 bond occurs at the same active center. The two methylation steps can proceed by a change in chemical mechanism resulting from differences in sterol structure, concerted versus carbocation. The kinetic mechanism remains the same during the consecutive methylation of the DELTA24 bond
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + ?
-
the first C1-transfer is 24(28) methylenecycloartenol, SN2-type and non-stop, ternary complex mechanism. The second C1-transfer is a mixture of 24-ethyl olefins, SN2-type and step-wise. Ordered pathway with S-adenosyl-L-methionine binding first
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + cyclolaudenol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + cyclolaudenol
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + cyclolaudenol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + cyclolaudenol
-
-
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
-
PbSMT synthesizes a single product, eburicol 24(28)-methylene-24,25-dihydro-lanosterol, from lanosterol
i.e. eburicol
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
-
PbSMT catalysis of the sterol acceptor lead to a C24-methyl product in which the 1,2-hydride migration of C24 to C25 occurs specifically from the Re-face of the original substrate double bond undergoing transalkylation
i.e. eburicol
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
-
PbSMT synthesizes a single product, eburicol 24(28)-methylene-24,25-dihydro-lanosterol, from lanosterol
i.e. eburicol
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
-
PbSMT catalysis of the sterol acceptor lead to a C24-methyl product in which the 1,2-hydride migration of C24 to C25 occurs specifically from the Re-face of the original substrate double bond undergoing transalkylation
i.e. eburicol
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
-
-
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
-
-
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + parkeol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + zymosterol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + zymosterol
S-adenosyl-L-homocysteine + fecosterol
-
-
-
?
S-adenosyl-L-methionine + zymosterol
S-adenosyl-L-homocysteine + fecosterol
-
-
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
zymosterol is 5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
24(28)-methylenelophenol + S-adenosyl-L-methionine
additional information
-
-
-
a mixture of three stereochemical related products with DELTA24(28)Z-ethylidene, DELTA24(28)-ethylidene and DELTA25(27)-24beta-ethyl side chains
-
?
additional information
?
-
-
no activity with cycloartanol, 3-deoxycycloartenol, or cyclolaudenol
-
-
?
additional information
?
-
enzyme catalyzes both the reactions of EC 2.1.1.142, cycloartenol 24-C-methyltransferase and EC 2.1.1.143, 24-methylenesterol C-methyltransferase. SMT1 catalyzes a sterol methylation pathway by the algal Delta25(27)-olefin route, where methylation proceeds by a conserved SN2 reaction and deprotonation proceeds from the pro-Z methyl group on lanosterol corresponding to C27
-
-
-
additional information
?
-
-
enzyme catalyzes both the reactions of EC 2.1.1.142, cycloartenol 24-C-methyltransferase and EC 2.1.1.143, 24-methylenesterol C-methyltransferase. SMT1 catalyzes a sterol methylation pathway by the algal Delta25(27)-olefin route, where methylation proceeds by a conserved SN2 reaction and deprotonation proceeds from the pro-Z methyl group on lanosterol corresponding to C27
-
-
-
additional information
?
-
-
the SMT from soybean plants is bifunctional, performing methyl transferations to C24 and to C28 of the substrate, the enzyme also converts the inhibitor 24,25-dehydro-27-methenyl-cycloartenol, i.e. cycloartenol nucleus substrate analogue with double bond at C8, to a 24,27-dimethenyl-cycloartenol, CA-11, compound, overview
-
-
?
additional information
?
-
-
achieving the cyclolaudenyl cation intermediate by electrophilic alkylation of cycloartenol is significant to the overall reaction rate. The evolution of variant sterol C-24-methylation patterns is driven by competing reaction channels that have switched in algae from formation of primarily DELTA25(27) products that convert into ergosterol to, in land plants, formation of DELTA24(28) products that convert into sitosterol
-
-
?
additional information
?
-
-
GC-MS analysis shows that the fungus synthesizes 12 compounds of which lanosterol, ergosterol and brassicasterol make up approximately 80% of the sterol mixture
-
-
?
additional information
?
-
-
SMT recognition of lanosterol and cycloartenol versus zymosterol is the C3-OH group, whose orientation in the A-ring and hydrogen bonding ability can affect productive binding of the acceptor molecule. The recombinant enzyme expressed in Escherichia coli possesess a substrate specificity for lanosterol and generates a single exocyclic methylene product. Regiospecific conversion of the pro-Z methyl group of the DELTA24(25)-substrate to the pro-R isopropyl methyl group of the product and the migration of H24 to C25 on the Re-face of the original substrate double bond undergoing C24-methylation, NMR and mass spectrometric analysis, overview. No activity with 24(28)-methylenelophenol, fecosterol, or eburicol
-
-
?
additional information
?
-
-
GC-MS analysis shows that the fungus synthesizes 12 compounds of which lanosterol, ergosterol and brassicasterol make up approximately 80% of the sterol mixture
-
-
?
additional information
?
-
-
SMT recognition of lanosterol and cycloartenol versus zymosterol is the C3-OH group, whose orientation in the A-ring and hydrogen bonding ability can affect productive binding of the acceptor molecule. The recombinant enzyme expressed in Escherichia coli possesess a substrate specificity for lanosterol and generates a single exocyclic methylene product. Regiospecific conversion of the pro-Z methyl group of the DELTA24(25)-substrate to the pro-R isopropyl methyl group of the product and the migration of H24 to C25 on the Re-face of the original substrate double bond undergoing C24-methylation, NMR and mass spectrometric analysis, overview. No activity with 24(28)-methylenelophenol, fecosterol, or eburicol
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cycloartenol + S-adenosyl-L-methionine
(24S)-24-methylcycloart-25-en-3beta-ol + S-adenosyl-L-homocysteine
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol
S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
-
3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 work in concert to control carbon flux into end-product sterols. Sterol composition can be controlled by the temporal activity of the promoters driving transgene expression
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24(28)-methylenecycloartanol
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24-methylenecycloartanol
-
-
-
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
SMT2 has a position-specific substrate specificity for DELTA24(25)-sterols and contains a single active center to catalyze the consecutive C1-transfer activities by substrate reaction channels similar to the fungal SMT1
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
rate-limiting initial step in the conversion of phytosterol
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
cycloartenol is 4,4,14alpha-trimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3beta-ol
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24(28)-methylenecycloartanol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24(28)-methylenecycloartanol
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + cyclolaudenol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + cyclolaudenol
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + cyclolaudenol
-
-
-
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
-
PbSMT synthesizes a single product, eburicol 24(28)-methylene-24,25-dihydro-lanosterol, from lanosterol
i.e. eburicol
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
-
PbSMT synthesizes a single product, eburicol 24(28)-methylene-24,25-dihydro-lanosterol, from lanosterol
i.e. eburicol
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
additional information
?
-
-
GC-MS analysis shows that the fungus synthesizes 12 compounds of which lanosterol, ergosterol and brassicasterol make up approximately 80% of the sterol mixture
-
-
?
additional information
?
-
-
GC-MS analysis shows that the fungus synthesizes 12 compounds of which lanosterol, ergosterol and brassicasterol make up approximately 80% of the sterol mixture
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3beta24R,S)-24-methyl-24-thionacycloart-3-ol iodide
-
reversible, non-competitive-type
24,25-dehydro-27-methenyl-cycloartenol
-
i.e. cycloartenol nucleus substrate analogue with double bond at C8
24,25-dehydro-27-methylene-cycloartenol
-
i.e. cycloartenol nucleus substrate analogue with double bond at C14, non-competitive
24-bromocycloartenol
-
competitive; competitive inhibitor relative to cycloartenol; time-dependent inhibition kinetics
24-fluorocycloartenol
-
allylic substrate analog, time-dependent inhibition kinetics, consistent with the action of a suicide substrate that irreversibly inactivates the enzyme; competitive, the electron-withdrawing alpha-fluorine substituent suppresses the rate of the C-methylation reaction
24-Methyl-25,26,27-trisnor-24-trimethylammonium cycloartenol iodide
-
24R and 24S isomer
25-azalanosterol
-
substrate analogue, competitive-type inhibitor, a potent inhibitor of cell growth promoting lanosterol accumulation and 24-alkyl sterol depletion
26,27-dehydrolanosterol
-
substrate analogue, competitive-type inhibitor, pseudofirst-order, time-dependent inactivation of the PbSMT. Formation of a reversibly bound enzyme-substrate complex, followed by catalysis to an intermediate that can be converted to a methyl product or the intermediate can be intercepted through covalent modification and hence irreversible inhibition, lanosterol or 26,27-dehydrolanosterol can lead to distinct intermediates that convert to methylated sterol products
26,27-dehydrozymosterol
-
mechanism-based inhibitor, specific covalent modification of SMT2
26-methenylcycloartenol
-
pseudo-first-order time-dependent inactivation, less potency of inhibition
26-methynylcycloartenol
-
inhibition kinetics non-competitive and time-dependent, less potency of inhibition
citrostadienol
-
competitive with cycloartenol or 24(28)-methylenelophenol
cyclolaudenol
-
dead end inhibitor analog, competitive versus cycloartenol, uncompetitive versus S-adenosyl-L-methionine
S-adenosyl-L-homocysteine
-
noncompetitive with respect to S-adenosyl-L-methionine
24(28)-methylenecycloartanol
-
competitive with respect to S-adenosyl-L-methionine
25-Azacycloartenol
-
competitive with cycloartenol or 24(28)-methylenelophenol; noncompetitive
25-Azacycloartenol
-
noncompetitive inhibitor versus cycloartenol, uncompetitive inhibitor versus S-adenosyl-L-methionine
additional information
-
non-competitive inhibitors are ammonium group substituted for carbon at C25, C24, C23 and C22; overview, diverse substrate and transition state analogues
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Chagas Disease
Preparation of transition-state analogues of sterol 24-methyl transferase as potential anti-parasitics.
Chagas Disease
Ultrastructural alterations in Trypanosoma (Schizotrypanum) cruzi induced by Delta(24(25)) sterol methyl transferase inhibitors and their combinations with ketoconazole.
Infections
Antiproliferative effects of delta 24(25) sterol methyl transferase inhibitors on Trypanosoma (Schizotrypanum) cruzi: in vitro and in vivo studies.
Infections
Growth inhibition and ultrastructural alterations induced by Delta24(25)-sterol methyltransferase inhibitors in Candida spp. isolates, including non-albicans organisms.
Leishmaniasis
Binding pattern analysis and structural insight into the inhibition mechanism of Sterol 24-C methyltransferase by docking and molecular dynamics approach.
Leishmaniasis
Preparation of transition-state analogues of sterol 24-methyl transferase as potential anti-parasitics.
Leishmaniasis
Repurposing of FDA-approved drugs as inhibitors of sterol C-24 methyltransferase of Leishmania donovani to fight against leishmaniasis.
Leishmaniasis
Virtual screening of natural compounds for potential inhibitors of Sterol C-24 methyltransferase of Leishmania donovani to overcome leishmaniasis.
Pneumonia, Pneumocystis
Evidence for multiple sterol methyl transferase pathways in Pneumocystis carinii.
Sporotrichosis
?(24)-Sterol Methyltransferase Plays an Important Role in the Growth and Development of Sporothrix schenckii and Sporothrix brasiliensis.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state kinetics and thermodynamics of wild-type and mutant enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000083
24,25-dehydro-27-methylene-cycloartenol
-
pH 7.5, 35°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00005
(24R,S)-24-Methyl-25,26,27-trisnor-24-dimethylsulfonium cycloartenol iodide
-
-
0.000025
(24R,S)-24-Methyl-25,26,27-trisnor-24-trimethylarsonium cycloartenol iodide
-
-
0.000014
25-azalanosterol
-
pH 7.5, 30°C, recombinant wild-type enzyme
0.054
26,27-dehydrolanosterol
-
pH 7.5, 30°C, recombinant wild-type enzyme
0.047
26-methenylcycloartenol
-
rate of inactivation saturable, comparable to values obtained for cycloartenol
0.116
24(28)-methylene cycloartanol
substrate 24(28)-methylene lophenol
0.25
24(28)-methylene cycloartanol
-
pH 7.4, 35°C, substrate cycloartenol
0.036
24-bromocycloartenol
-
competitive inhibition, concentration of substrate analogs varied at 5, 15, 25, and 50 microM
0.032
24-fluorocycloartenol
-
competitive inhibition, concentration of substrate analogs varied at 5, 15, 25, and 50 microM
0.045
citrostadienol
-
pH 7.4, 35°C, substrate: 24(28)-methylenelophenol
additional information
additional information
-
overview, diverse substrate and transition state analogues
-
additional information
additional information
-
inhibition kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00003
25-azalanosterol
Paracoccidioides brasiliensis
-
pH 7.5, 30°C, recombinant wild-type enzyme
0.067
26-methynylcycloartenol
Glycine max
-
co-incubation with 50 microM or 100 microM cycloartenol affords protection against inactivation generating 25% and 45% C-methylation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
C-methylation reaction analyzed with substrate analogs containing a cycloartenol nucleus and a double bond or triple bond attached to C26, mass spectra of enzyme-generated products indicated, time-dependent inhibition kinetics reveals active-site directed process and partitioning to produce novel products
additional information
-
synthesis and kinetic analysis of the fluorinated substrate analog 24-fluorocycloartenol, electron-withdrawing alpha-fluorine substituent suppresses the rate of the C-methylation reaction by one order of magnitude, critical hydride shift of H24 to C25 to afford time-dependent enzyme inactivation prevented by analyzed substrate analog
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5 - 8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme catalyzes both the reactions of EC 2.1.1.41 and EC 2.1.1.142
UniProt
brenda
enzyme catalyzes both the reactions of EC 2.1.1.41 and EC 2.1.1.142
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
expression of GhSMT2-1 is 10times higher than expression of GhSMT2-2
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
due to differences in its overall amino acid composition and substrate-dependent partitioning pathways, Paracoccidiodes brasiliensis SMT has to be grouped into a fourth and new class of SMT
evolution
-
due to differences in its overall amino acid composition and substrate-dependent partitioning pathways, Paracoccidiodes brasiliensis SMT has to be grouped into a fourth and new class of SMT
-
malfunction
-
Deficiency of SMT2 in the cvp1 mutant results in moderate developmental defects, including aberrant cotyledon vein patterning, serrated floral organs, and reduced stature, but plants are viable, suggesting that SMT3 activity can substitute for the loss of SMT2. The overexpression of SMT3 complements the cotyledon venation pattern defects of cvp1 (SMT2) mutants
malfunction
-
smt3 single mutants appear wild type, cvp1 smt3 double mutants show enhanced defects relative to cvp1 mutants, such as discontinuous cotyledon vein pattern, and produce novel phenotypes, including defective root growth, loss of apical dominance, sterility, and homeotic floral transformations. Antisense smt3 plants did not display a phenotype, suggesting that SMT3 and SMT2 are functionally redundant
malfunction
-
the SMT2 genes of soybean (SMT2-1 and SMT2-2) are shown to complement the SMT deficient cvp1 mutant Arabidopsis plants
malfunction
-
transgenic Arabidopsis seeds expressing GmSMT1 or GmSMT2 show modifications in the ratio of 24-methyl to 24-ethyl sterol in the direction of sitosterol formation
metabolism
-
the enzyme is involved in the first metabolic step in the 24-alkyl sterol synthetic pathway of Paracoccidiodes brasiliensis involves the C24-methylation of lanosterol. PbSMT cannot perform the second alkylation step, consistent with the absence of sterols 24(28)-methylenelophenol, fecosterol or eburicol in wild-type cells. Alternate pathways and mechanisms for the conversion of ?24(25)-containing sterol side chains to methylated product, detailed overview
metabolism
-
the enzyme is involved in the first metabolic step in the 24-alkyl sterol synthetic pathway of Paracoccidiodes brasiliensis involves the C24-methylation of lanosterol. PbSMT cannot perform the second alkylation step, consistent with the absence of sterols 24(28)-methylenelophenol, fecosterol or eburicol in wild-type cells. Alternate pathways and mechanisms for the conversion of ?24(25)-containing sterol side chains to methylated product, detailed overview
-
physiological function
enzyme transfers either one or two methyl groups to the C-24 position of the sterol side chain producing both C28 and C29 24-alkylsterols in approximately the same proportions. Expression of SAM:SMT in a Saccharomyces cerevisiae Erg6 mutant restores its ability to produce ergosterol as the major sterol, and also results in low levels of C29 sterols such as pneumocysterol
physiological function
-
enzyme transfers either one or two methyl groups to the C-24 position of the sterol side chain producing both C28 and C29 24-alkylsterols in approximately the same proportions. Expression of SAM:SMT in a Saccharomyces cerevisiae Erg6 mutant restores its ability to produce ergosterol as the major sterol, and also results in low levels of C29 sterols such as pneumocysterol
-
additional information
-
residue Tyr88 in the native protein can contribute to stabilization of the active-site topography
additional information
-
residue Tyr88 in the native protein can contribute to stabilization of the active-site topography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
40000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
?
x * 38620, calculated from sequence, x * 80000, SDS-PAGE of recombinant protein including MBP-tag
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F82I
-
continues to catalyze strongly both the first and second C1-transfer activities and generates product sets similar to the control
F82L
-
first C1-transfer activity is relatively unaffected, loss of the second C1-transfer activity
F85L
-
first C1-transfer activity is relatively unaffected, loss of the second C1-transfer activity
F91L
-
first C1-transfer activity reduced from the control activity, loss of the second C1-transfer activity
F93L
-
first C1-transfer activity reduced from the control activity, loss of the second C1-transfer activity
W87L
-
first and second C1-transfer activities are greatly reduced from the control activities
Y83F
Y83L
Y81F
-
site-directed mutagenesis, the mutation causes a preferential change in affinity for DELTA24-sterols that affords alter partitioning in the direction of 24-ethyl(idene) product formation
Y81L
-
site-directed mutagenesis, the mutation causes a preferential change in affinity for DELTA24-sterols that affords alter partitioning in the direction of 24-ethyl(idene) product formation
Y88F
-
site-directed mutagenesis, the mutation causes a 10% loss in activity compared to the wild-type enzyme
Y88L
-
site-directed mutagenesis, the mutation causes a 50% loss in activity compared to the wild-type enzyme
Y81F
-
site-directed mutagenesis, the mutation causes a preferential change in affinity for DELTA24-sterols that affords alter partitioning in the direction of 24-ethyl(idene) product formation
-
Y81L
-
site-directed mutagenesis, the mutation causes a preferential change in affinity for DELTA24-sterols that affords alter partitioning in the direction of 24-ethyl(idene) product formation
-
Y88F
-
site-directed mutagenesis, the mutation causes a 10% loss in activity compared to the wild-type enzyme
-
Y88L
-
site-directed mutagenesis, the mutation causes a 50% loss in activity compared to the wild-type enzyme
-
additional information
Y83F
-
first C1-transfer activity is relatively unaffected whereas the second C1-transfer activity generates different amounts of product compared to the control
Y83F
-
Km and kcat, of wild-type enzyme and mutant enzyme are similar for cycloartenol as substrate
Y83L
-
first C1-transfer activity greatly reduced from the control activity, loss of the second C1-transfer activity
Y83L
-
Km and kcat, of wild-type enzyme and mutant enzyme are similar for cycloartenol as substrate
additional information
-
overexpression of SMT2 gene in a mutant strain leads to an accumulation of sitosterol and to an altered phenotype, some of the changes can be restored by brassinosteroid treatment, some cannot, sterol profile of wild-type and mutant plants
additional information
construction of SMT1-deficient mutants with altered phenotype, reduced fertility and root growth defects, transgenic plant seedlings are sensitive against brassinosteroids and transfection with a genomic clone or a SMT1 cDNA can complement the mutants
additional information
-
GhSMT2-1 and GhSMT2-2 have high homology with the SMT2 from Arabidopsis thaliana and Nicotiana tabacum. The typical conserved structures characterized by the sterol C-24 methyltransferase, such as region I (LDVGCGVGGPMRAI), region II (IEATCHAP), and region III (YEWGWGQSFHF), are present in both deduced proteins
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform SMT2-2 is purified to homogeneity by column chromatography, gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of the catalytic domain of Hevea brasiliensis 3-hydroxy-3-methylglutaryl CoA reductase and Nicotiana tabacum C24-sterol methyltransferase type 1 in tobacco, under control of both constitutive and seed-specific promoters, resulting in increased accumulation of total sterol in seed tissue by 2.5fold and 2.1fold, respectively
-
expression as FLAG-fusion protein in Escherichia coli, amino acid sequence analysis
expression in Escherichia coli
expression in Saccharomyces cerevisiae mutant line erg6, which is deleted in the SMT1 gene, complementation of the yeast
gene PbSMT, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression of soluble His-tagged wild-type and mutant enzymes in Escherichia coli strains BL21(DE3) and BL21(C43)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of SMT1 is highly up-regulated in cell suspension cultures treated with methyl jasmonate
transcriptional regulation of soybean SMT2 genes is influenced by environmental conditions to some extent: analysis of transcript abundance by qRT-PCR reveals that both the genes SMT2-1 and SMT2-2 are down-regulated after dehydration and markedly induced under cold conditions. ABA treatment elicits an increase in transcript levels for both the genes. A reduction in expression is associated with the salinity treatment for both the genes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
in hydroponically-grown Nicotiana benthamiana, using a virus-induced gene silencing system, the transcript levels of 3-hydroxy-3-methylglutaryl-CoA reductase 1 (HMGR1), cycloartenol synthase 1 (CAS1), sterol side chain reductase 2 (SSR2) and S-adenosyl-L-Met-dependent C-24 sterol methyltransferase 1 (SMT1) have been reduced in leaf, stem and root tissues in approximately 2 weeks
degradation
-
the amino acids of Region 1 provide a tight substrate orientation imposed by hydrophobic interactions between the sterol side chain and the SMT active site contacts and control the production and processing of the transmethylation pathways governed by the first and second C1-transfer activities
synthesis
-
rational drug target design based on structure-function-relation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mangla, A.T.; Nes, W.D.
Sterol C-methyl transferase from Prototheca wickerhamii mechanism, sterol specificity and inhibition
Bioorg. Med. Chem.
8
925-936
2000
Prototheca wickerhamii
brenda
Schaeffer, A.; Bronner, R.; Benveniste, P.; Schaller, H.
The ratio of campesterol to sitosterol that modulates growth in Arabidopsis is controlled by sterol methyltransferase 2;1
Plant J.
25
605-615
2001
Arabidopsis thaliana
brenda
Nes, W.D.; Janssen, G.G.; Bergenstrahle, A.
Structural requirements for transformation of substrates by the (S)-adenosyl-L-methionine:delta 24(25)-sterol methyl transferase
J. Biol. Chem.
266
15202-15212
1991
Helianthus annuus
brenda
Rahier, A.; Genot, J.C.; Schuber, F.; Benveniste, P.; Narula, A.S.
Inhibition of S-adenosyl-L-methionine sterol-C-24-methyltransferase by analogues of a carbocationic ion high-energy intermediate. Structure activity relationships for C-25 heteroatoms (N, As, S) substituted triterpenoid derivatives
J. Biol. Chem.
259
15215-15223
1984
Zea mays
brenda
Diener, A.C.; Li, H.; Zhou, W.X.; Whoriskey, W.J.; Nes, W.D.; Fink, G.R.
Sterol methyltransferase 1 controls the level of cholesterol in plants
Plant Cell
12
853-870
2000
Arabidopsis thaliana (Q9LM02)
brenda
Shi, J.; Gonzales, R.A.; Bhattacharyya, M.K.
Identification and characterization of an S-adenosyl-L-methionine:DELTA24-sterol-C-methyltransferase cDNA from soybean
J. Biol. Chem.
271
9384-9389
1996
Glycine max, Glycine max (Q43445)
brenda
Holmberg, N.; Harker, M.; Wallace, A.D.; Clayton, J.C.; Gibbard, C.L.; Safford, R.
Co-expression of N-terminal truncated 3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 in transgenic tobacco enhances carbon flux towards end-product sterols
Plant J.
36
12-20
2003
Nicotiana tabacum
brenda
Zhou, W.; Nes, W.D.
Sterol methyltransferase2: purification, properties, and inhibition
Arch. Biochem. Biophys.
420
18-34
2003
Arabidopsis thaliana
brenda
Nes, W.D.; Song, Z.; Dennis, A.L.; Zhou, W.; Nam, J.; Miller, M.B.
Biosynthesis of phytosterols. Kinetic mechanism for the enzymatic C-methylation of sterols
J. Biol. Chem.
278
34505-34516
2003
Glycine max
brenda
Zhou, W.; Song, Z.; Kanagasabai, R.; Liu, J.; Jayasimha, P.; Sinha, A.; Veeramachanemi, P.; Miller, M.B.; Nes, W.D.
Mechanism-based enzyme inactivators of phytosterol biosynthesis
Molecules
9
185-203
2004
Glycine max
brenda
Zhou, W.; Song, Z.; Liu, J.; Miller, M.B.; Nes, W.D.
24-Thiacycloartanol, a potent mechanism-based inactivator of plant sterol methyltransferase
Tetrahedron Lett.
45
875-878
2004
Glycine max
-
brenda
Nes, W.D.; Sinha, A.; Jayasimha, P.; Zhou, W.; Song, Z.; Dennis, A.L.
Probing the sterol binding site of soybean sterol methyltransferase by site-directed mutagenesis: functional analysis of conserved aromatic amino acids in Region 1
Arch. Biochem. Biophys.
448
23-30
2006
Glycine max
brenda
Song, Z.; Nes, W.D.
Inactivation of soybean sterol 24-C-methyltransferase by elongated sterol side chains at C26
Bioorg. Med. Chem. Lett.
17
5902-5906
2007
Glycine max
brenda
Wang, J.; Liu, J.; Song, Z.; Nes, W.D.
Sterol C24-methyltransferase: Mechanistic studies of the C-methylation reaction with 24-fluorocycloartenol
Bioorg. Med. Chem. Lett.
18
232-235
2008
Glycine max
brenda
Luo, M.; Tan, K.; Xiao, Z.; Hu, M.; Liao, P.; Chen, K.
Cloning and expression of two sterol C-24 methyltransferase genes from upland cotton (Gossypium hirsuturm L.)
J. Genet. Genomics
35
357-363
2008
Gossypium hirsutum
brenda
Wang, J.; Nes, W.D.
Cyclobranol: a substrate for C25-methyl sterol side chains and potent mechanism-based inactivator of plant sterol methyltransferase
Bioorg. Med. Chem. Lett.
18
3878-3881
2008
Glycine max
brenda
Neelakandan, A.K.; Song, Z.; Wang, J.; Richards, M.H.; Wu, X.; Valliyodan, B.; Nguyen, H.T.; Nes, W.D.
Cloning, functional expression and phylogenetic analysis of plant sterol 24C-methyltransferases involved in sitosterol biosynthesis
Phytochemistry
70
1982-1998
2009
Glycine max, Glycine max (D2D5G4), Glycine max (Q43445)
brenda
Pereira, M.; Song, Z.; Santos-Silva, L.K.; Richards, M.H.; Nguyen, T.T.; Liu, J.; de Almeida Soares, C.M.; da Silva Cruz, A.H.; Ganapathy, K.; Nes, W.D.
Cloning, mechanistic and functional analysis of a fungal sterol C24-methyltransferase implicated in brassicasterol biosynthesis
Biochim. Biophys. Acta
1801
1163-1174
2010
Paracoccidioides brasiliensis, Paracoccidioides brasiliensis Pb0, ATCC MYA-826
brenda
Neelakandan, A.K.; Nguyen, H.T.; Kumar, R.; Tran, L.S.; Guttikonda, S.K.; Quach, T.N.; Aldrich, D.L.; Nes, W.D.; Nguyen, H.T.
Molecular characterization and functional analysis of Glycine max sterol methyl transferase 2 genes involved in plant membrane sterol biosynthesis
Plant Mol. Biol.
74
503-518
2010
Arabidopsis thaliana, Glycine max
brenda
Carland, F.; Fujioka, S.; Nelson, T.
The sterol methyltransferases SMT1, SMT2, and SMT3 influence Arabidopsis development through nonbrassinosteroid products
Plant Physiol.
153
741-756
2010
Arabidopsis thaliana
brenda
Patkar, P.; Haubrich, B.A.; Qi, M.; Nguyen, T.T.; Thomas, C.D.; Nes, W.D.
C-24-methylation of 26-fluorocycloartenols by recombinant sterol C-24-methyltransferase from soybean: evidence for channel switching and its phylogenetic implications
Biochem. J.
456
253-262
2013
Glycine max
brenda
Neelakandan, A.; Chamala, S.; Valliyodan, B.; Nes, W.; Nguyen, H.
Metabolic engineering of soybean affords improved phytosterol seed traits
Plant Biotechnol. J.
10
12-19
2012
Glycine max (Q43445)
brenda
Kaneshiro, E.; Johnston, L.; Nkinin, S.; Romero, B.; Giner, J.
Sterols of Saccharomyces cerevisiae erg6 knockout mutant expressing the Pneumocystis carinii S-adenosylmethionine sterol C-24 methyltransferase (SAM SMT)
J. Eukaryot. Microbiol.
62
298-306
2015
Pneumocystis carinii (Q96WX4), Pneumocystis carinii, Pneumocystis carinii B80 (Q96WX4)
brenda
Guan, H.; Zhao, Y.; Su, P.; Tong, Y.; Liu, Y.; Hu, T.; Zhang, Y.; Zhang, X.; Li, J.; Wu, X.; Huang, L.; Gao, W.
Molecular cloning and functional identification of sterol C24-methyltransferase gene from Tripterygium wilfordii
Acta Pharm. Sin. B
7
603-609
2017
Tripterygium wilfordii (A0A2U7MCR4), Tripterygium wilfordii
brenda
Guan, H.Y.; Su, P.; Zhao, Y.J.; Zhang, X.N.; Dai, Z.B.; Guo, J.; Tong, Y.R.; Liu, Y.J.; Hu, T.Y.; Yin, Y.; Gao, L.H.; Gao, W.; Huang, L.Q.
Cloning and functional analysis of two sterol-C24-methyltransferase 1 (SMT1) genes from Paris polyphylla
J. Asian Nat. Prod. Res.
20
595-604
2018
Paris polyphylla (A0A2R2UK37)
brenda
Haubrich, B.; Collins, E.; Howard, A.; Wang, Q.; Snell, W.; Miller, M.; Thomas, C.; Pleasant, S.; Nes, W.
Characterization, mutagenesis and mechanistic analysis of an ancient algal sterol C24-methyltransferase Implications for understanding sterol evolution in the green lineage
Phytochemistry
113
64-72
2015
Chlamydomonas reinhardtii (A8IJ34), Chlamydomonas reinhardtii
brenda
Zhou, W.; Debnath, A.; Jennings, G.; Hahn, H.; Vanderloop, B.; Chaudhuri, M.; Nes, W.; Podust, L.
Enzymatic chokepoints and synergistic drug targets in the sterol biosynthesis pathway of Naegleria fowleri
PLoS Pathog.
14
e1007245
2018
Naegleria fowleri
brenda
Atsumi, G.; Kagaya, U.; Tabayashi, N.; Matsumura, T.
Analysis of the mechanisms regulating the expression of isoprenoid biosynthesis genes in hydroponically-grown Nicotiana benthamiana plants using virus-induced gene silencing
Sci. Rep.
8
14804
2018
Nicotiana benthamiana
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.1.1.142)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
