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Enzyme Nomenclature
Information on EC 2.1.1.142 - cycloartenol 24-C-methyltransferase
Word Map on EC 2.1.1.142
- 2.1.1.142
- ergosterol
-
c-methylation
- lanosterol
-
phytosterols
- sitosterol
-
delta24-sterols
- azasterols
- pneumocystis
-
kinact
- carinii
-
24-ethyl
-
24-alkylated
-
brassinosteroids
- fecosterol
-
glycoalkaloids
- campesterol
-
delta7
-
schizotrypanum
-
enzyme-generated
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.1.1.142
-
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RECOMMENDED NAME
GeneOntology No.
cycloartenol 24-C-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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 + (24R)-24-methylcycloart-25-en-3beta-ol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transfer of methyl group
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37257-07-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
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
-
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
-
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
-
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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
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-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
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
(24R)-24-methylcycloart-25-en-3beta-ol + S-adenosyl-L-homocysteine
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24(28)-methylenecycloartenol + S-adenosyl-L-homocysteine
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartenol + S-adenosyl-L-homocysteine
cyclobranol + S-adenosyl-L-methionine
9beta-25-methylidene-9,19-cyclolanost-1-ene-1,3-diol + S-adenosyl-L-homocysteine
-
-
-
-
?
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
-
-
?
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)-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 + 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 + 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-methylene cycloartenol
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24-methylenecycloartenol
-
-
-
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartenol + S-adenosyl-L-homocysteine
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartenol + 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-methylenecycloartenol + S-adenosyl-L-homocysteine
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartenol + S-adenosyl-L-homocysteine
64% of the effectiveness with 24(28)-methylene lophenol
-
-
?
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-methylene cycloartenol
-
-
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24-methylene cycloartenol
-
active-site topography and reaction mechanisms analyzed with substrate analogs
-
-
?
S-adenosyl-L-methionine + cycloartenol
S-adenosyl-L-homocysteine + 24-methylene cycloartenol
-
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 + ?
-
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 + 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 + ?
-
-
-
-
?
S-adenosyl-L-methionine + parkeol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + zymosterol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
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
?
-
-
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
?
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
(24R)-24-methylcycloart-25-en-3beta-ol + S-adenosyl-L-homocysteine
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartenol + 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
-
-
?
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-methylene cycloartenol
-
-
-
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
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
Q43445
-
-
-
?
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
-
?
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
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
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
-
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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
-
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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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.036
24-bromocycloartenol
-
; competitive inhibition, concentration of substrate analogs varied at 5, 15, 25, and 50 microM; pH 7.5, 35°C, versus cycloartenol
0.032
24-fluorocycloartenol
-
competitive inhibition, concentration of substrate analogs varied at 5, 15, 25, and 50 microM; pH 7.5, 35°C, versus cycloartenol
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
0.25
24(28)-methylene cycloartanol
-
pH 7.4, 35°C, substrate cycloartenol
0.045
citrostadienol
-
pH 7.4, 35°C, substrate: 24(28)-methylenelophenol
additional information
additional information
-
inhibition kinetics, overview
-
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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
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
160000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially purified, recombinant protein, SDS-PAGE; recombinant enzyme from Escherichia coli to homogeneity
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, recombinant protein; expression in Escherichia coli
-
expressed in Escherichia coli; expressed in Escherichia coli, critical 24H replaced by a fluorine atome
-
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)
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y83F
-
Km and kcat, of wild-type enzyme and mutant enzyme are similar for cycloartenol as substrate
Y83L
-
Km and kcat, of wild-type enzyme and mutant enzyme are similar for cycloartenol as substrate
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
-
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.142)
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