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Information on EC 2.1.1.41 - sterol 24-C-methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P25087
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2.1.1.41 sterol 24-C-methyltransferaseIUBMB Comments
Requires glutathione. Acts on a range of sterols with a 24(25)-double bond in the sidechain. While zymosterol is the preferred substrate it also acts on desmosterol, 5alpha-cholesta-7,24-dien-3beta-ol, 5alpha-cholesta-5,7,24-trien-3beta-ol, 4alpha-methylzymosterol and others. S-Adenosyl-L-methionine attacks the Si-face of the 24(25) double bond and the C-24 hydrogen is transferred to C-25 on the Re face of the double bond.
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Word Map
- 2.1.1.41
- ergosterol
- leishmaniasis
- lanosterol
- infantum
- medicine
- tomatidine
-
24-alkyl
- drug development
-
24-ethyl
-
c24-methylation
- agriculture
-
c1-transfer
- degradation
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
erg6p, sterol 24-c-methyltransferase, c-24 sterol methyltransferase, tbsmt, pbsmt, c24-methyltransferase, 24-c-sterol methyltransferase, (s)-adenosyl-l-methionine:delta24(25)-sterol methyl transferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
24-sterol C-methyltransferase
-
-
-
-
DELTA24-methyltransferase
-
-
-
-
DELTA24-sterol methyltransferase
-
-
-
-
methyltransferase, DELTA24-sterol
-
-
-
-
phytosterol methyltransferase
-
-
-
-
S-adenosyl-4-methionine:sterol DELTA24-methyltransferase
-
-
-
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S-adenosyl-L-methionine:DELTA24(23)-sterol methyltransferase
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-
-
-
SMT1
zymosterol-24-methyltransferase
-
-
-
-
SMT1
-
-
-
-
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
substrate analogue inhibitor binding site structure
-
S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol = S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
kinetic and inhibition mechanism
-
S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol = S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
active site model, termed steric-electric plug model, consists of a non-covalent mechanism involving the intermediacy of a 24beta-methyl (or ethyl) sterol bound to the ternary complex
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S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol = S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
substrate binding, amino acid sequence
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:zymosterol 24-C-methyltransferase
Requires glutathione. Acts on a range of sterols with a 24(25)-double bond in the sidechain. While zymosterol is the preferred substrate it also acts on desmosterol, 5alpha-cholesta-7,24-dien-3beta-ol, 5alpha-cholesta-5,7,24-trien-3beta-ol, 4alpha-methylzymosterol and others. S-Adenosyl-L-methionine attacks the Si-face of the 24(25) double bond and the C-24 hydrogen is transferred to C-25 on the Re face of the double bond.
CAS REGISTRY NUMBER
COMMENTARY
37257-07-1
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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
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
-
-
?
cycloartenol + S-adenosyl-L-methionine
24-methylenecycloartanol + S-adenosyl-L-homocysteine
-
-
-
?
lanosterol + S-adenosyl-L-methionine
24-methylene-24,25-dihydrolanosterol + S-adenosyl-L-homocysteine
-
-
-
?
zymosterol + S-adenosyl-L-methionine
24-methylzymosta-8,25(27)-dienol + S-adenosyl-L-homocysteine
-
mutants D79L and E82L
-
?
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
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
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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
-
-
?
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
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-
?
additional information
?
-
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overview about a large number of sterol substrates of various origin, substrate specificity analysis, structures: overview
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-
?
additional information
?
-
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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
-
-
?
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
zymosterol + S-adenosyl-L-methionine
fecosterol + S-adenosyl-L-homocysteine
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-
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24(R,S),25-epiminozymosterol
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reversible inhibitor, disrupts ergosterol homoeostasis by interrupting methyl addition to C-24 thereby impairing growth
5'-deoxy-5'-(methylthio)adenosine
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AdoMet analog, competitive inhibitor
additional information
-
overview, diverse substrate and transition state analogues
-
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
overview, diverse substrate and transition state analogues
-
0.0000017
(24R)-methyl-25-thiacholesteryl iodide
-
versus S-adenosyl-L-methionine
0.0000023
(24S)-methyl-25-thiacholesteryl iodide
-
versus S-adenosyl-L-methionine
0.0000046
(24S)-methyl-25-thiacholesteryl iodide
-
versus zymosterol
0.0000011
25-thiacholesterol iodide
-
versus S-adenosyl-L-methionine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
prediction of secondary structure, eight residues at positions 79, 81, 82, 192, 217, 218, 219 and 223 critical for catalysis, scanning mutagenesis experiments involving a leucine replacement of 52 amino acids, substitution of key residues with functionally or structurally similar amino acids, 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, model supported in which several conserved and non-conserved amino acids located in distinct regions regulate course of the C-methylation reaction toward product differences
additional information
prediction of secondary structure, eight residues at positions 79, 81, 82, 192, 217, 218, 219 and 223 critical for catalysis, scanning mutagenesis experiments involving a leucine replacement of 52 amino acids, substitution of key residues with functionally or structurally similar amino acids, 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, model supported in which several conserved and non-conserved amino acids located in distinct regions regulate course of the C-methylation reaction toward product differences
additional information
-
activity at various concentrations of glutathione
additional information
-
relative activity using 26,27-dehydrozymosterol as a substrate: wild-type 100%, mutant Y81F 300%, mutant Y81W 450%, mutant Y81I 25%, mutant Y81L 40%, mutant Y81V 15%, mutant Y81A 15%
additional information
-
relative activity using zymosterol as a substrate: wild-type 100%, mutant Y81F 92%, mutant Y81W 124%, mutant Y81I 32%, mutant Y81L 37%, mutant Y81V 8%, mutant Y81A 8%
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G217L
100% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
G218L
100% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
T219L
32% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
Y192F
100% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
Y223F
100% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
C128L
C128S
-
Km (mM) (substrate: AdoMet): 30, kcat (1/sec) (substrate: AdoMet): 0.005, Kd (mM) (zymosterol): 0.005, Kd (mM) (AdoMet): 0.008
D125L
D152L
D189L
D276L
D65L
D79L
E108L
E195L
E209L
E246L
E64L
E68L
E82L
E98L
H107L
H199L
H224L
-
the ratio of turnover-number to KM-value for zymosterol is 1.4fold lower than the wild-type ratio
H238L
H90L
P133L
Y153F
Y153L
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)
Y81F
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)
Y81L
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)
additional information
C128L
-
no activity with AdoMet as substrate, Kd (mM) (zymosterol): 0.005, Kd (mM) (AdoMet): 0.028, photolabelled: value below 1%
D125L
-
no activity with AdoMet as substrate, Kd (mM) (zymosterol): 0.006, Kd (mM) (AdoMet): 0.012, photolabelled: 30%
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
D65L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, unchanged activity
D79L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, not decreased activity, 1 new activity to form 24-methylzymosterol from zymosterol
E108L
-
the ratio of turnover-number to KM-value for zymosterol is 11fold lower than the wild-type ratio
E209L
-
the ratio of turnover-number to KM-value for zymosterol is 2.4fold lower than the wild-type ratio
E246L
-
the ratio of turnover-number to KM-value for zymosterol is 13.5fold lower than the wild-type ratio
E64L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, unchanged activity
E68L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, no activity
E82L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, not decreased activity, 1 new activity to form 24-methylzymosterol from zymosterol
E98L
-
potentially responsible for substrate binding to leucine by site directed mutagenesis, unchanged activity
H107L
-
the ratio of turnover-number to KM-value for zymosterol is 2.4fold lower than the wild-type ratio
H199L
-
the ratio of turnover-number to KM-value for zymosterol is 162fold lower than the wild-type ratio
H238L
-
the ratio of turnover-number to KM-value for zymosterol is 1.6fold lower than the wild-type ratio
P133L
-
no activity with AdoMet as substrate, Kd (mM) (zymosterol): 0.015, Kd (mM) (AdoMet): no binding, photolabelled: value below 1%
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%
Y153L
-
Km (mM) (substrate: AdoMet): 0.017, kcat (1/sec) (substrate: AdoMet): 0.01, Kd (mM) (zymosterol): 0.004, Kd (mM) (AdoMet): 0.004
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)
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)
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.1 M Tris-HCl buffer, 1 mM Mg2+, 90% loss of activity overnight
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type SMT is expressed and partially purified by anionic-exchange chromatography to generate ca. 85% pure Erg6p as determined by SDS-PAGE quantification of the target protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, recombinant protein, site-directed mutagenesis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
construction of transgenic plants with modified sterol profile via recombinant sterol 24-C-methyltransferase shall protect crops against damage by insect infestation
degradation
-
active site of the yeast SMT has the necessary amino acids to generate products common to SMT catalysis of plants and protozoa, minor perturbations in the active site topography brought about by mutagenesis are sufficient to recognize new substrates
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
-
Nes, W.D.
Sterol methyl transferase: enzymology and inhibition
Biochim. Biophys. Acta
1529
63-88
2000
Candida albicans, Saccharomyces cerevisiae
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
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
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
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
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
Nes, W.D.; Jayasimha, P.; Zhou, W.; Kanagasabai, R.; Jin, C.; Jaradat, T.T.; Shaw, R.W.; Bujnicki, J.M.
Sterol methyltransferase: functional analysis of highly conserved residues by site-directed mutagenesis
Biochemistry
43
569-576
2004
Saccharomyces cerevisiae
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
1686
30-36
2004
Saccharomyces cerevisiae
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
Biochem. Soc. Trans.
33
1189-1196
2005
Candida albicans, Fusarium sp., Saccharomyces cerevisiae, Trypanosoma brucei
Nes, W.D.; Jayasimha, P.; Song, Z.
Yeast sterol C24-methyltransferase: role of highly conserved tyrosine-81 in catalytic competence studied by site-directed mutagenesis and thermodynamic analysis
Arch. Biochem. Biophys.
477
313-323
2008
Saccharomyces cerevisiae
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
1781
344-351
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P25087)
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