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(3beta)-3-fluorolanost-8,24-diene + S-adenosyl-L-methionine
(3beta)-3-fluoro-24-methylidenelanost-8-ene + S-adenosyl-L-homocysteine
-
catalytic competence: 16%
-
-
?
(3beta)-3-methoxylanosta-8,24-diene + S-adenosyl-L-methionine
(3beta)-3-methoxy-24-methylidenelanost-8-ene + S-adenosyl-L-homocysteine
-
catalytic competence: 18%
-
-
?
(3beta)-lanosta-8,24-dien-3-amine + S-adenosyl-L-methionine
(3beta)-24-methylidenelanost-8-en-3-amine + S-adenosyl-L-homocysteine
-
catalytic competence: 22%
-
-
?
(3beta)-lanosta-8,24-dien-3-yl acetate + S-adenosyl-L-methionine
(3beta)-24-methylidenelanost-8-en-3-yl acetate + S-adenosyl-L-homocysteine
-
catalytic competence: 29%
-
-
?
14alpha-methylergosta-8,24(28)-diene + S-adenosyl-L-methionine
?
-
-
-
-
?
14alpha-methylzymosterol + S-adenosyl-L-methionine
14alpha-methyl-24-methylenezymosterol + S-adenosyl-L-homocysteine
24(28)-methylenecycloartanol + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
-
ratio of DELTA25(27) to DELTA24(28)-product for wild-type is 100:0, 35% conversion
-
?
24(28)-methylenelophenol + S-adenosyl-L-methionine
?
-
-
-
?
24-methylenecholesterol + S-adenosyl-L-methionine
24-ethylidenecholesterol + S-adenosyl-L-homocysteine
-
5% the reaction rate of zymosterol
-
?
24-methylenelanosterol + S-adenosyl-L-methionine
pneumocysterol + S-adenosyl-L-homocysteine
-
preferred substrate
-
?
26,27-dehydrozymosterol + S-adenosyl-L-methionine
26-homo-cholesta-8(9),23(24)E,26(26')-trienol + 26-homo-cholesta-8(9),26(26')-3beta,24beta-dienol + S-adenosyl-L-homocysteine
-
mutants
-
?
26,27-dehydrozymosterol + S-adenosyl-L-methionine
? + S-adenosyl-L-homocysteine
-
in contrast to the results with zymosterol, product analysis of the 26,27-dehydrozymosterol assays shows that multiple products are produced that occurred in different ratios determined by HPLC-radiocounting of the non-saponifiable lipid fractions. In these analyses two major product classes are identified, a neutral C26 sterol monol and a pair of C26-oxygenated diols
-
-
?
31-norlanosterol + S-adenosyl-L-methionine
?
4alpha-methylzymosterol + S-adenosyl-L-methionine
?
5-dehydroepisterol + S-adenosyl-L-methionine
?
-
-
-
-
?
cholesta-5,7,24-triene + S-adenosyl-L-methionine
?
-
-
-
-
?
cholesta-7,24-diene + S-adenosyl-L-methionine
?
-
-
-
-
?
cholesterol + S-adenosyl-L-methionine
?
-
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24(28)-methylenecycloartanol + S-adenosyl-L-homocysteine
-
ratio of DELTA25(27) to DELTA24(28)-product for wild-type is 57:43, 70% conversion
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
dehydroergosterol + S-adenosyl-L-methionine
?
-
-
-
-
?
desmosterol + S-adenosyl-L-methionine
24-methylenedesmosterol + S-adenosyl-L-homocysteine
ergosta-5,8,22,24(28)-tetraene + S-adenosyl-L-methionine
?
-
-
-
-
?
ergosterol + S-adenosyl-L-methionine
?
-
-
-
-
?
lanosta-8,24-dien-3-one + S-adenosyl-L-methionine
24-methylidenelanost-8-en-3-one + S-adenosyl-L-homocysteine
-
catalytic competence: 48%
-
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
lanosterol + S-adenosyl-L-methionine
24beta-methyllanosta-8,25(27)-enol + 24(28)-methylenelanosterol + S-adenosyl-L-homocysteine
-
products are 55% 24beta-methyllanosta-8,25(27)-enol, 38% 24(28)-methylenelanosterol (eburicol), and 7% 24beta-ethyllanosta-8,25(27)-enol
-
?
lanosterol-3beta-OH + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
catalytic competence: 100%
-
-
?
obtusifoliol + S-adenosyl-L-methionine
? + 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 + 26,27-dehydrolanosterol
?
-
-
-
-
?
S-adenosyl-L-methionine + 31-norlanosterol
?
-
-
-
-
?
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
reaction of EC 2.1.1.142
-
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24-methylene-24,25-dihydrolanosterol
-
-
-
-
?
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24beta-methyl lanosta-8,25(27)-enol + 24(28)-methylene lanosterol
reaction of EC 2.1.1.142
-
-
?
S-adenosyl-L-methionine + obtusifoliol
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + zymosterol
?
-
GC-MS analysis of the enzyme-generated products from a soluble TbSMT shows the presence of four biomethylated sterols identified as ergosta-8,25(27)-dienol, ergosta-8,24(28)-dienol, ergosta-8,24(25)-dienol and 24-dimethyl ergosta-8,25(27)-dienol in a ratio of substrate/product of 7:3. The products distributed in a ratio of approximately 5:1:2:2 respectively
-
-
?
S-adenosyl-L-methionine + zymosterol
S-adenosyl-L-homocysteine + fecosterol
zymosterol + S-adenosyl-L-methionine
24-methylzymosta-8,25(27)-dienol + S-adenosyl-L-homocysteine
-
mutants D79L and E82L
-
?
zymosterol + S-adenosyl-L-methionine
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
additional information
?
-
14alpha-methylzymosterol + S-adenosyl-L-methionine
14alpha-methyl-24-methylenezymosterol + S-adenosyl-L-homocysteine
-
37% activity compared to lanosterol
-
-
?
14alpha-methylzymosterol + S-adenosyl-L-methionine
14alpha-methyl-24-methylenezymosterol + S-adenosyl-L-homocysteine
-
37% activity compared to lanosterol
-
-
?
31-norlanosterol + S-adenosyl-L-methionine
?
-
78% activity compared to lanosterol
-
-
?
31-norlanosterol + S-adenosyl-L-methionine
?
-
78% activity compared to lanosterol
-
-
?
4alpha-methylzymosterol + S-adenosyl-L-methionine
?
-
43% activity compared to lanosterol
-
-
?
4alpha-methylzymosterol + S-adenosyl-L-methionine
?
-
43% activity compared to lanosterol
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
-
-
?
desmosterol + S-adenosyl-L-methionine
24-methylenedesmosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
desmosterol + S-adenosyl-L-methionine
24-methylenedesmosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
desmosterol + S-adenosyl-L-methionine
24-methylenedesmosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
desmosterol + S-adenosyl-L-methionine
24-methylenedesmosterol + S-adenosyl-L-homocysteine
-
-
-
?
desmosterol + S-adenosyl-L-methionine
24-methylenedesmosterol + S-adenosyl-L-homocysteine
-
-
-
?
desmosterol + S-adenosyl-L-methionine
24-methylenedesmosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
desmosterol + S-adenosyl-L-methionine
24-methylenedesmosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
desmosterol + S-adenosyl-L-methionine
24-methylenedesmosterol + S-adenosyl-L-homocysteine
-
desmosterol is 5alpha-cholesta-5,24-dien-3beta-ol
-
-
?
desmosterol + S-adenosyl-L-methionine
24-methylenedesmosterol + S-adenosyl-L-homocysteine
-
desmosterol is 5alpha-cholesta-5,24-dien-3beta-ol
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
-
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
no reaction with
-
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
100% activity, lanosterol is the optimal acceptor molecule
-
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
100% activity, lanosterol is the optimal acceptor molecule
-
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
preferred substrate
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
-
-
?
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
-
-
-
-
?
S-adenosyl-L-methionine + zymosterol
S-adenosyl-L-homocysteine + fecosterol
-
-
-
-
?
S-adenosyl-L-methionine + zymosterol
S-adenosyl-L-homocysteine + fecosterol
-
-
-
?
S-adenosyl-L-methionine + zymosterol
S-adenosyl-L-homocysteine + fecosterol
-
-
-
-
?
S-adenosyl-L-methionine + zymosterol
S-adenosyl-L-homocysteine + fecosterol
-
-
-
?
S-adenosyl-L-methionine + zymosterol
S-adenosyl-L-homocysteine + fecosterol
-
-
-
-
?
S-adenosyl-L-methionine + zymosterol
S-adenosyl-L-homocysteine + fecosterol
-
the active center is composed of a set of acidic amino acids, Asp125, Asp152, Glu195 and Asp276, which contribute to initial binding of sterol and S-adenosyl-L-methionine. His90 functions subsequently in the reaction process to promote product formation
-
-
?
zymosterol + S-adenosyl-L-methionine
?
-
61% activity compared to lanosterol
-
-
?
zymosterol + S-adenosyl-L-methionine
?
-
-
-
-
?
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
-
role in biosynthesis of plant and fungi sterols
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
ratio of DELTA25(27) to DELTA24(28)-product for wild-type is 28:72, 70% conversion
-
?
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
-
-
fecosterol is 24-exomethylene-5alpha-cholesta-8,24-dien-3beta-ol
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
wild-type and mutants
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
regio- and stereospecific for substrates
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
regio- and stereospecific for substrates
-
?
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
-
zymosterol is 5alpha-cholesta-8,24-dien-3beta-ol
fecosterol is 24-exomethylene-5alpha-cholesta-8,24-dien-3beta-ol
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
role in biosynthesis of plant and fungi sterols
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
the enzyme catalyzes an enzymatic step following C-4 demethylation of 4,4-dimethylzymosterol. Erg28p anchors the C-4 demethylation enzyme complex to the endoplasmic reticulum and acts as a protein bridge to the Erg6p enzyme required for the next ergisterol biosynthetic step
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
a bisubstrate reaction that proceeds by a sequential and noncovalent reaction whereby beta-face methyl addition to the DELTA24-bond and deprotonation of C-28 proceed to give rise to a nucleophilic rearrangement in which H-24 migrates to C-25 on the reface of the substrate double bond in concert with the initial ionization to afford the bound fecosterol
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
-
-
-
?
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
-
C4-demethyl sterols with double bonds in the nucleus at positions 8, 7, or 5 are acceptable substrates
-
-
?
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
-
-
?
additional information
?
-
enzyme catalyzes a sterol methylation pathway by the algal DELTA25(27)-olefin route, where methylation proceeds by a conserved SN2 reaction and de-protonation 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
?
-
-
eburicol and obtusifoliol are no substrates
-
-
?
additional information
?
-
-
eburicol and obtusifoliol are no substrates
-
-
?
additional information
?
-
-
enzyme involved in biosynthesis of ergosterol, which is a target molecule of leishmanicidal and fungicidal amphotericin B, used for vaccine development
-
-
?
additional information
?
-
enzyme involved in biosynthesis of ergosterol, which is a target molecule of leishmanicidal and fungicidal amphotericin B, used for vaccine development
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
overview about a large number of sterol substrates of various origin, substrate specificity analysis, structures: overview
-
-
?
additional information
?
-
-
minimum requirements for productive binding and formation of catalytically active enzyme-substrate complex must be a substrate that possesses a 3beta-hydroxy group, a planar nucleus, an intact side chain that retains the length of the native substrate zymosterol, a 20-R configuration and a delta24-double bond
-
-
?
additional information
?
-
-
formation of the ergostane (C1-transfer activity) and stigmastane (C2-transfer activity) sterol side chains, stepwise mutagenesis of amino acids of Erg6p, identification of five residues within the putative active site that contribute directly to C-methylation pathways operated by fungal and plant SMT proteins
-
-
?
additional information
?
-
formation of the ergostane (C1-transfer activity) and stigmastane (C2-transfer activity) sterol side chains, stepwise mutagenesis of amino acids of Erg6p, identification of five residues within the putative active site that contribute directly to C-methylation pathways operated by fungal and plant SMT proteins
-
-
?
additional information
?
-
-
neither lanosterol nor other C4-methyl-containing sterols bind productively to the enzyme
-
-
?
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(24,S),25-epiminozymosterol
-
-
(24R)-methyl-25-thiacholesteryl iodide
-
-
(24R,S),25-epiminolanosterol
-
-
(24R,S),25-epiminozymosterol
-
-
(24S)-methyl-25-thiacholesteryl iodide
-
-
(3beta,24,R,S)-24-methyl-24-thioniacholest-5-enol
-
-
(3S,20R)-20-(propylamino-ethyl)-pregn-7-en-3-ol
-
-
(3S,20S)-20-(butylamino-methyl)-pregn-7-en-3-ol
-
-
(3S,20S)-20-(ethylamino-methyl)-pregn-7-en-3-ol
-
-
(3S,20S)-20-(methylamino-methyl)-pregn-7-en-3-ol
-
-
(3S,20S)-20-(pentylamino-methyl)-pregn-7-en-3-ol
-
-
(3S,20S)-20-(propylamino-methyl)-pregn-7-en-3-ol
-
-
(3S,20S)-20-[(1R,S)-(1,2-dimethyl-propylamino)-methyl]-pregn-7-en-3-ol
-
-
(3S,20S)-20-[(2-dimethylamino-ethylamino)-methyl]-pregn-7-en-3-ol
-
-
(3S,20S)-20-[(2-methylpropyl)amino-methyl]-pregn-7-en-3-ol
-
-
(3S,20S)-20-[(2-pyrrolidin-1-yl-ethylamino)-methyl]-pregn-7-en-3-ol
-
-
(3S,20S)-20-[(3-dimethylamino-propylamino)-methyl]-pregn-7-en-3-ol
-
-
(R,S)-24,25-epiminolanosterol
-
-
(R,S)-S-butyl-S-[(3S,20S)-(3-hydroxypregn-7-en-20-yl)-methyl]-S-methyl-sulfonium iodide
-
-
2-(3S,20R)-[(E)-2-(3-hydroxypregn-7-en-20-yl)-ethenyl]-1-methylpyridinium iodide
-
-
22,25-Diazacholesterol
-
20R and 20S isomer
22-piperidin-3-yl-pregnan-22(S),3beta-diol
-
-
24(R,S),25-epiminolanosterol
24(R,S),25-epiminozymosterol
-
reversible inhibitor, disrupts ergosterol homoeostasis by interrupting methyl addition to C-24 thereby impairing growth
24(R,S)-25-epiminolanosterol
-
-
24(S)-24-methyl-25-thiacholest-5-enol iodide
-
-
24beta-aminolanosterol
-
-
25-aza-24,25-dihydrolanosterol
-
-
25-Aza-24,25-dihydrozymosterol
-
-
25-Azacholesterol hydrochloride
-
-
25-thiacholesterol iodide
-
-
25-thialanosterol iodide
-
-
26,27-dehydrolanosterol
-
-
26-nor-25-thialanosterol
-
-
30-amino-24,25-dihydrolanosterol
-
-
4-(3S,20R)-[(E)-2-(3-hydroxypregn-7-en-20-yl)-ethenyl]-1-methylpyridinium iodide
-
-
5'-deoxy-5'-(methylthio)adenosine
-
AdoMet analog, competitive inhibitor
7-amino-24,25-dihydrolanosterol
-
-
amphotericine B
-
inhibits the wild-type at concentrations above 60 nM, inhibition can be hindered by zymosterol
cholesta-8,24(28)-dienol
-
-
ergosta-5,7,22-trienol
-
-
Filipin
-
slightly inhibiting at low concentration
methyl ([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)acetate
-
-
methyl 3-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)propanoate
-
-
methyl 4-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)butanoate
-
-
methyl 5-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)pentanoate
-
-
methyl 6-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)hexanoate
-
-
methyl 7-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)heptanoate
-
-
methyl 8-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)octanoate
-
-
Nystatin
-
slightly inhibiting at low concentration
S-adenosyl-L-homocysteine
-
-
S-isobutyladenosine
-
AdoMet analog, competitive inhibitor
sinefungin
-
AdoMet analog, competitive inhibitor
Substrate analogues
-
dead-end inhibitors
-
22,26-azasterol
-
-
23-Azacholesterol
-
-
24(R,S),25-epiminolanosterol
-
-
24(R,S),25-epiminolanosterol
-
-
25-azalanosterol
-
-
26,27-dehydrozymosterol
-
-
26,27-dehydrozymosterol
-
mechanism-based irreversible inhibition
26,27-dehydrozymosterol
-
irreversible inhibitor that binds covalently to the SMT, affinitylabels the active site to convert to a product characterized as delta23(24)-sterol
26,27-dehydrozymosterol
-
-
26,27-dehydrozymosterol
-
-
desmosterol
-
competitive versus sterol and S-adenosyl-L-methionine
desmosterol
-
competitive versus sterol and S-adenosyl-L-methionine
ergosterol
-
reversible inhibitor
ketoconazole
-
-
Zymosterol
-
competitive versus sterol and S-adenosyl-L-methionine
Zymosterol
-
competitive versus sterol and S-adenosyl-L-methionine
additional information
-
overview, diverse substrate and transition state analogues
-
additional information
newly synthesized azasterols methyl ([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)acetate, methyl 3-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)propanoate, methyl 4-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)butanoate, methyl 5-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)pentanoate, methyl 6-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)hexanoate, methyl 7-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)heptanoate, and methyl 8-([2-[(3S,8S,9S,10R,13S,14S,17R)-3-(acetyloxy)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]propyl]amino)octanoate, none show any significant inhibition against the recombinant enzyme
-
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Y110F
no significant change in products
Y110L
remodeling the active site to alter the electronics results in delayed timing of the hydride migration from methyl attack of the DELTA24-bond, that thereby produces metabolic switching of product ratios in favor of DELTA25(27)-olefins or impairs the second C1-transfer activity
C128S
-
Km (mM) (substrate: AdoMet): 30, kcat (1/sec) (substrate: AdoMet): 0.005, Kd (mM) (zymosterol): 0.005, Kd (mM) (AdoMet): 0.008
D229L
relative activity: 100%
E224L
relative activity: 74%
F183L
100% relative enzyme activity
H224L
-
the ratio of turnover-number to KM-value for zymosterol is 1.4fold lower than the wild-type ratio
K353L
56% relative enzyme activity
S87E
100% relative enzyme activity
S87Q
100% relative enzyme activity
S97E
relative activity: 100%
S97Q
relative activity: 100%
T219L
32% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
V222L
27% relative enzyme activity
Y192F
100% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
Y192L
95% relative enzyme activity
Y81A
-
Km (mM): 0.018 (zymosterol), 0.023 (26,27-dehydrozymosterol), kcat (1/sec): 0.00083 (zymosterol), 0.000116 (26,27-dehydrozymosterol), Ki (mM): 0.011 (26,27-dehydrozymosterol), 0.00019 (25-azalanosterol), 0.00013 (24(R,S),25-epiminolanosterol), 0.071 (ergosterol)
Y81I
-
Km (mM): 0.021 (zymosterol), 0.027 (26,27-dehydrozymosterol), kcat (1/sec): 0.00433 (zymosterol), 0.00025 (26,27-dehydrozymosterol), Ki (mM): 0.009 (26,27-dehydrozymosterol), 0.00020 (25-azalanosterol), 0.00016 (24(R,S),25-epiminolanosterol), 0.077 (ergosterol)
Y81V
-
Km (mM): 0.026 (zymosterol), 0.024 (26,27-dehydrozymosterol), kcat (1/sec): 0.00116 (zymosterol), 0.00011 (26,27-dehydrozymosterol), Ki (mM): 0.007 (26,27-dehydrozymosterol), 0.000195 (25-azalanosterol), 0.000145 (24(R,S),25-epiminolanosterol), 0.074 (ergosterol)
Y81W
-
Km (mM): 0.017 (zymosterol), 0.023 (26,27-dehydrozymosterol), kcat (1/sec): 0.0133 (zymosterol), 0.0033 (26,27-dehydrozymosterol), Ki (mM): 0.010 (26,27-dehydrozymosterol), 0.00039 (25-azalanosterol), 0.00036 (24(R,S),25-epiminolanosterol), 0.088 (ergosterol)
Y177F
-
mutant proteins catalyses zymosterol much less efficiently than the wild-type enzyme, with a Vmax/Km ratio 23-40% that of wild-type
Y208F
-
mutant proteins catalyses zymosterol much less efficiently than the wild-type enzyme, with a Vmax/Km ratio 23-40% that of wild-type
Y66F
-
mutant proteins catalyses zymosterol much less efficiently than the wild-type enzyme, with a Vmax/Km ratio 23-40% that of wild-type. Sterol composition of the Y66F catalysis is different. The sterol mixture possesses a significant decrease in ergosta-8,24(25)-dienol compensated by an increase in ergosta-8,25(27)-dienol and ergosta-8,24(28)-dienol
A193L
no activity
A193S
95% relative enzyme activity
A193S
relative activity: 95%
A196L
73% relative enzyme activity
A196L
relative activity: 73%
A200L
4% relative enzyme activity
A200L
relative activity: 4%
A221L
25% relative enzyme activity
A221L
relative activity: 25%
A350L
100% relative enzyme activity
A350L
relative activity: 100%
C128L
no activity
C128L
-
no activity with AdoMet as substrate, Kd (mM) (zymosterol): 0.005, Kd (mM) (AdoMet): 0.028, photolabelled: value below 1%
C198L
95% relative enzyme activity
C198L
relative activity: 95%
C198V
16% relative enzyme activity
C198V
relative activity: 16%
D125L
no activity
D125L
-
no activity with AdoMet as substrate, Kd (mM) (zymosterol): 0.006, Kd (mM) (AdoMet): 0.012, photolabelled: 30%
D152L
no activity
D152L
-
no activity with AdoMet as substrate, Kd (mM) (zymosterol): 0.005, Kd (mM) (AdoMet): 0.014, photolabelled: 35%
D189L
-
the ratio of turnover-number to KM-value for zymosterol is 1.4fold lower than the wild-type ratio
D189L
relative activity: 91%
D276L
no activity
D65L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, unchanged activity
D65L
relative activity: 100%
D79L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, not decreased activity, 1 new activity to form 24-methylzymosterol from zymosterol
D79L
relative activity: 81%
E108L
-
the ratio of turnover-number to KM-value for zymosterol is 11fold lower than the wild-type ratio
E108L
relative activity: 34%
E195L
no activity
E209L
-
the ratio of turnover-number to KM-value for zymosterol is 2.4fold lower than the wild-type ratio
E209L
relative activity: 79%
E246L
-
the ratio of turnover-number to KM-value for zymosterol is 13.5fold lower than the wild-type ratio
E246L
relative activity: 6%
E64L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, unchanged activity
E64L
relative activity: 100%
E68L
no activity
E68L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, no activity
E82D
55% relative enzyme activity
E82D
relative activity: 55%
E82L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, not decreased activity, 1 new activity to form 24-methylzymosterol from zymosterol
E82L
-
produces plant-like substrate-product profiles
E82L
relative activity: 99%
E82Q
90% relative enzyme activity
E82Q
relative activity: 90%
E98L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, unchanged activity
E98L
relative activity: 100%
F178L
34% relative enzyme activity
F178L
relative activity: 34%
F188L
2% relative enzyme activity
F188L
relative activity: 2%
F220L
29% relative enzyme activity
F220L
relative activity: 29%
F269L
no activity
F357L
100% relative enzyme activity
F357L
relative activity: 100%
F89L
100% relative enzyme activity
F89L
relative activity: 100%
F91L
15% relative enzyme activity
F91L
relative activity: 15%
G127L
1% relative enzyme activity
G127L
relative activity: 1%
G129L
no activity
G131L
5% relative enzyme activity
G131L
relative activity: 5%
G132L
50% relative enzyme activity
G132L
relative activity: 50%
G217L
100% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
G217L
relative activity: 100%
G218L
100% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
G218L
relative activity: 100%
G347L
5% relative enzyme activity
G347L
relative activity: 5%
G351L
90% relative enzyme activity
G351L
relative activity: 90%
G352L
3% relative enzyme activity
G352L
relative activity: 3%
G84L
14% relative enzyme activity
G84L
relative activity: 14%
G86L
16% relative enzyme activity
G86L
relative activity: 16%
H107L
-
the ratio of turnover-number to KM-value for zymosterol is 2.4fold lower than the wild-type ratio
H107L
relative activity: 23%
H199L
-
the ratio of turnover-number to KM-value for zymosterol is 162fold lower than the wild-type ratio
H199L
relative activity: 2%
H199Q
45% relative enzyme activity
H199Q
relative activity: 45%
H199R
20% relative enzyme activity
H199R
relative activity: 20%
H238L
-
the ratio of turnover-number to KM-value for zymosterol is 1.6fold lower than the wild-type ratio
H238L
relative activity: 85%
H90L
no activity
H90Q
no activity
H90R
no activity
I194L
67% relative enzyme activity
I194L
relative activity: 67%
K215L
100% relative enzyme activity
K215L
relative activity: 100%
P133L
no activity
P133L
-
no activity with AdoMet as substrate, Kd (mM) (zymosterol): 0.015, Kd (mM) (AdoMet): no binding, photolabelled: value below 1%
P201L
58% relative enzyme activity
P201L
relative activity: 58%
P216L
65% relative enzyme activity
P216L
relative activity: 65%
S354L
100% relative enzyme activity
S354L
relative activity: 100%
S87L
100% relative enzyme activity
S87L
relative activity: 100%
S88L
61% relative enzyme activity
S88L
relative activity: 61%
S88N
17% relative enzyme activity
S88N
relative activity: 17%
T197L
93% relative enzyme activity
T197L
relative activity: 93%
V126L
1% relative enzyme activity
V126L
relative activity: 1%
V130L
100% relative enzyme activity
V130L
relative activity: 100%
V349L
47% relative enzyme activity
V349L
relative activity: 47%
W225F
100% relative enzyme activity
W225F
relative activity: 60%
W225L
100% relative enzyme activity
W225L
relative activity: 100%
W286F
100% relative enzyme activity
W286F
relative activity: 51%
W286L
2% relative enzyme activity
W286L
relative activity: 2%
W85F
100% relative enzyme activity
W85F
relative activity: 55%
W85L
40% relative enzyme activity
W85L
relative activity: 40%
Y153F
100% relative enzyme activity
Y153F
-
Km (mM) (substrate: AdoMet): 0.016, kcat (1/sec) (substrate: AdoMet): 0.003, Kd (mM) (zymosterol): 0.007, Kd (mM) (AdoMet): 0.013, photolabelled: 55%
Y153F
relative activity: 41%
Y153L
no enzyme activity
Y153L
-
Km (mM) (substrate: AdoMet): 0.017, kcat (1/sec) (substrate: AdoMet): 0.01, Kd (mM) (zymosterol): 0.004, Kd (mM) (AdoMet): 0.004
Y153L
relative activity: 100%
Y207F
100% relative enzyme activity
Y207F
relative activity: 100%
Y207L
3% relative enzyme activity
Y207L
relative activity: 3%
Y223F
100% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
Y223F
relative activity: 100%
Y223L
100% relative enzyme activity
Y223L
relative activity: 100%
Y287L
20% relative enzyme activity
Y287L
relative activity: 20%
Y74F
100% relative enzyme activity
Y74F
relative activity: 100%
Y74L
100% relative enzyme activity
Y74L
relative activity: 100%
Y81F
-
produces plant-like substrate-product profiles
Y81F
-
Km (mM): 0.017 (zymosterol), 0.026 (26,27-dehydrozymosterol), kcat (1/sec): 0.0108 (zymosterol), 0.0025 (26,27-dehydrozymosterol), Ki (mM): 0.010 (26,27-dehydrozymosterol), 0.00036 (25-azalanosterol), 0.00031 (24(R,S),25-epiminolanosterol), 0.082 (ergosterol)
Y81F
relative activity: 100%
Y81L
90% relative enzyme activity
Y81L
-
Km (mM): 0.018 (zymosterol), 0.024 (26,27-dehydrozymosterol), kcat (1/sec): 0.00416 (zymosterol), 0.00033 (26,27-dehydrozymosterol), Ki (mM): 0.011 (26,27-dehydrozymosterol), 0.00021 (25-azalanosterol), 0.00018 (24(R,S),25-epiminolanosterol), 0.078 (ergosterol)
Y81L
relative activity: 90%
Y83F
95% relative enzyme activity
Y83F
relative activity: 95%
Y83L
90% relative enzyme activity
Y83L
relative activity: 90%
Y83W
100% relative enzyme activity
Y83W
relative activity: 100%
additional information
-
natural amphotericine B-resistant mutant strain
additional information
-
C57BL/6 mice immunized with a vaccine candidate consisting of 24-c-methyltransferase as an antigene formulated monophosphoryl lipid A (MPL-SE) show Ag-specific Th1 immune responses characterized by robust production of IFN-gamma upon specific Ag re-exposure in vitro. Upon challenge with Leishmania infantum, mice immunized with SMT plus MPL-SE show significant lower parasite burdens in both spleens and livers compared with non-immunized mice or mice injected with adjuvant alone
additional information
C57BL/6 mice immunized with a vaccine candidate consisting of 24-c-methyltransferase as an antigene formulated monophosphoryl lipid A (MPL-SE) show Ag-specific Th1 immune responses characterized by robust production of IFN-gamma upon specific Ag re-exposure in vitro. Upon challenge with Leishmania infantum, mice immunized with SMT plus MPL-SE show significant lower parasite burdens in both spleens and livers compared with non-immunized mice or mice injected with adjuvant alone
additional information
-
Leishmania major promastigotes cells overproducing the enzyme do not have increased resistance to the sterol methenyltransferase inhibitor 22,26-azasterol
additional information
-
by photoaffinity labeling and mutational analysis the AdoMet binding site is defined. Results indicate that one or both of Cys128 and Pro133 are covalently bound to AdoMet
additional information
-
scanning mutagenesis experiments involving a leucine replacement of 52 amino acids in Erg6p followed by substitution of key residues with functionally or structurally similar amino acids indicate that 5 new residues at positions Y192, G217, G218, T219 and Y223 can switch the course of C1-transfer activity to include plant-like C2-transfer activity. The data support a model in which several conserved and non-conserved amino acids located in distinct regions of the Saccharomyces cerevisiae Erg6p regulate the course of the C-methylation reaction toward product differences
additional information
scanning mutagenesis experiments involving a leucine replacement of 52 amino acids in Erg6p followed by substitution of key residues with functionally or structurally similar amino acids indicate that 5 new residues at positions Y192, G217, G218, T219 and Y223 can switch the course of C1-transfer activity to include plant-like C2-transfer activity. The data support a model in which several conserved and non-conserved amino acids located in distinct regions of the Saccharomyces cerevisiae Erg6p regulate the course of the C-methylation reaction toward product differences
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Moore, J.T.; Gaylor, J.L.
Isolation and purification of an S-adenosylmethionine: delta 24-sterol methyltransferase from yeast
J. Biol. Chem.
244
6334-6340
1969
Saccharomyces cerevisiae
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Mechanism and inhibition of delta 24-sterol methyltransferase from Candida albicans and Candida tropicalis
Biochemistry
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9633-9640
1989
Candida albicans, Candida tropicalis
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Oelschlager, A.C.; Angus, R.H.; Pierce, A.M.; Pierce, H.D.; Srinivasan, R.
Azasterol inhibition of delta 24-sterol methyltransferase in Saccharomyces cerevisiae
Biochemistry
23
3582-3589
1984
Saccharomyces cerevisiae
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Bansal, S.K.; Knoche, H.W.
Sterol methyltransferase from Uromyces phaseoli: an investigation of the first and the second transmethylation reactions
Phytochemistry
20
1269-1277
1981
Uromyces phaseoli
-
brenda
Lin, H.K.; Knoche, H.W.
A sterol methyltransferase from bean rust uredospores Uromyces phaseoli
Phytochemistry
15
683-687
1976
Uromyces phaseoli
-
brenda
Bailey, R.B.; Thompson, E.D.; Parks, L.W.
Kinetic properties od S-adenosyl-L-methionine:24DELTA-sterol methyltransferase enzyme(s) in mitochondrial structures of Saccharomyces cerevisiae
Biochim. Biophys. Acta
334
127-136
1974
Saccharomyces cerevisiae
-
brenda
Mukhtar, H.; Hakkou, A.; Bonaly, R.
Studies on the activity of Kluyveromyces lactis S-adenosylmethionine:DELTA 24-sterol methyltransferase in presence of polyenic antifungal agents
Mycopathologia
126
75-83
1994
Kluyveromyces lactis
brenda
Nes, W.D.
Sterol methyl transferase: enzymology and inhibition
Biochim. Biophys. Acta
1529
63-88
2000
Saccharomyces cerevisiae, Candida albicans
brenda
Venkatramesh, M.; Guo, D.A.; Jia, Z.; Nes, W.D.
Mechanism and structural requirements for transformation of substrates by the (S)-adenosyl-L-methionine:DELTA24(25)-sterol methyl transferase from Saccharomyces cerevisiae
Biochim. Biophys. Acta
1299
313-324
1996
Saccharomyces cerevisiae
brenda
Nes, W.D.; Guo, D.a.; Zhou, W.
Substrate-based inhibitors of the (S)-adenosyl-L-methionine: DELTA24(25)- to DELTA24(28)-sterol methyltransferase from Saccharomyces cerevisiae
Arch. Biochem. Biophys.
342
68-81
1997
Saccharomyces cerevisiae
brenda
Nes, W.D.; McCourt, B.S.; Zhou, W.X.; Ma, J.; Marshall, J.A.; Peek, L.A.; Brennan, M.
Overexpression, purification, and stereochemical studies of the recombinant (S)-adenosyl-L-methionine: DELTA24(25)-to DELTA24(28)-sterol methyl transferase enzyme from Saccharomyces cerevisiae
Arch. Biochem. Biophys.
353
297-311
1998
Saccharomyces cerevisiae
brenda
Kaneshiro, E.S.; Rosenfeld, J.A.; Basselin-Eiweida, M.; Stringer, J.R.; Keely, S.P.; Smulian, A.G.; Giner, J.L.
The Pneumocystis carinii drug target s-adenosyl-L-methionine:Sterol C-24 methyl transferase has a unique substrate preference
Mol. Microbiol.
44
989-999
2002
Pneumocystis carinii
brenda
Acuna-Johnson, A.P.; Oehlschlager, A.C.; Pierce, A.M.; Pierce, H.D., Jr.; Czyzewska, E.K.
Stereochemistry of yeast DELTA24-sterol methyl transferase
Bioorg. Med. Chem.
5
821-832
1997
Saccharomyces cerevisiae
brenda
Nes, W.D.; Marshall, J.A.; Jia, Z.; Jaradat, T.T.; Song, Z.; Jayasimha, P.
Active site mapping and substrate channeling in the sterol methyltransferase pathway
J. Biol. Chem.
277
42549-42556
2002
Saccharomyces cerevisiae
brenda
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S-adenosyl-L-methionine inhibitors DELTA24-sterol methyltransferase and DELTA24(28)-sterol methylreductase as possible agents against Paracoccidioides brasiliensis
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Paracoccidioides brasiliensis
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Sterol methyltransferase: functional analysis of highly conserved residues by site-directed mutagenesis
Biochemistry
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Saccharomyces cerevisiae
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Mo, C.; Valachovic, M.; Bard, M.
The ERG28-encoded protein, Erg28p, interacts with both the sterol C-4 demethylation enzyme complex as well as the late biosynthetic protein, the C-24 sterol methyltransferase (Erg6p)
Biochim. Biophys. Acta
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2004
Saccharomyces cerevisiae
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Gros, L.; Castillo-Acosta, V.M.; Jimenez, C.J.; Sealey-Cardona, M.; Vargas, S.; Estevez, A.M.; Yardley, V.; Rattray, L.; Croft, S.L.; Ruiz-Perez, L.M.; Urbina, J.A.; Gilbert, I.H.; Gonzalez-Pacanowska, D.
New azasterols against Trypanosoma brucei: role of 24-sterol methyltransferase in inhibitor action
Antimicrob. Agents Chemother.
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Trypanosoma brucei rhodesiense, Trypanosoma brucei brucei (Q45KX5), Trypanosoma brucei rhodesiense STIB900, Trypanosoma brucei brucei 427 (Q45KX5)
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Nes, W.D.
Enzyme redesign and interactions of substrate analogues with sterol methyltransferase to understand phytosterol diversity, reaction mechanism and the nature of the active site
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Saccharomyces cerevisiae, Candida albicans, Fusarium sp., Trypanosoma brucei
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Zhou, W.; Lepesheva, G.I.; Waterman, M.R.; Nes, W.D.
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Trypanosoma brucei
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Yeast sterol C24-methyltransferase: role of highly conserved tyrosine-81 in catalytic competence studied by site-directed mutagenesis and thermodynamic analysis
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Saccharomyces cerevisiae
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Ganapathy, K.; Jones, C.W.; Stephens, C.M.; Vatsyayan, R.; Marshall, J.A.; Nes, W.D.
Molecular probing of the Saccharomyces cerevisiae sterol 24-C methyltransferase reveals multiple amino acid residues involved with C2-transfer activity
Biochim. Biophys. Acta
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2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P25087)
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Jayasimha, P.; Nes, W.D.
Photoaffinity labeling and mutational analysis of 24-C-sterol methyltransferase defines the AdoMet binding site
Lipids
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2008
Saccharomyces cerevisiae
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Jimenez-Jimenez, C.; Carrero-Lerida, J.; Sealey-Cardona, M.; Ruiz Perez, L.M.; Urbina, J.A.; Gonzalez Pacanowska, D.
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Leishmania major
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Goto, Y.; Bogatzki, L.Y.; Bertholet, S.; Coler, R.N.; Reed, S.G.
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Leishmania infantum, Leishmania infantum (A4IDL2)
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Nes, W.D.; Zhou, W.; Ganapathy, K.; Liu, J.; Vatsyayan, R.; Chamala, S.; Hernandez, K.; Miranda, M.
Sterol 24-C-methyltransferase: an enzymatic target for the disruption of ergosterol biosynthesis and homeostasis in Cryptococcus neoformans
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481
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Cryptococcus neoformans, Cryptococcus neoformans 76484
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Renard, D.; Perruchon, J.; Giera, M.; Mueller, J.; Bracher, F.
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Yarrowia lipolytica
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Leishmania infantum sterol 24-c-methyltransferase formulated with MPL-SE induces cross-protection against L. major infection
Vaccine
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2009
Leishmania infantum
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Ganapathy, K.; Kanagasabai, R.; Nguyen, T.T.; Nes, W.D.
Purification, characterization and inhibition of sterol C24-methyltransferase from Candida albicans
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Candida albicans
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Howard, A.L.; Liu, J.; Elmegeed, G.A.; Collins, E.K.; Ganatra, K.S.; Nwogwugwu, C.A.; Nes, W.D.
Sterol C24-methyltransferase: Physio- and stereo-chemical features of the sterol C3 group required for catalytic competence
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521
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Paracoccidioides brasiliensis
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Effect of substrate features and mutagenesis of active site tyrosine residues on the reaction course catalysed by Trypanosoma brucei sterol C-24-methyltransferase
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Trypanosoma brucei
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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
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2010
Paracoccidioides brasiliensis
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Kaneshiro, E.S.; Johnston, L.Q.; Nkinin, S.W.; Romero, B.I.; Giner, J.L.
Sterols of Saccharomyces cerevisiae erg6 knockout mutant expressing the Pneumocystis carinii S-adenosylmethionine:sterol C-24 methyltransferase
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Pneumocystis carinii (Q96WX4), Pneumocystis carinii
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Haubrich, B.A.; Collins, E.K.; Howard, A.L.; Wang, Q.; Snell, W.J.; Miller, M.B.; Thomas, C.D.; Pleasant, S.K.; Nes, W.D.
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)
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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)
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Mukherjee, S.; Xu, W.; Hsu, F.; Patel, J.; Huang, J.; Zhang, K.
Sterol methyltransferase is required for optimal mitochondrial function and virulence in Leishmania major
Mol. Microbiol.
111
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2019
Leishmania major (Q4Q1I2), Leishmania major (Q4Q1I3)
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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)
brenda