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2.1.1.41: sterol 24-C-methyltransferase

This is an abbreviated version!
For detailed information about sterol 24-C-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.41

Reaction

S-adenosyl-L-methionine
+
5alpha-cholesta-8,24-dien-3beta-ol
=
S-adenosyl-L-homocysteine
+
24-methylene-5alpha-cholest-8-en-3beta-ol

Synonyms

(S)-adenosyl-L-methionine:DELTA24(25)-sterol methyl transferase, 24-C-sterol methyltransferase, 24-SMT, 24-sterol C-methyltransferase, C-24 sterol methyltransferase, C24-methyltransferase, DELTA(24,25)-SMT, DELTA24-methyltransferase, DELTA24-sterol methyltransferase, Erg6, Erg6p, LMJF_36_2380, LMJF_36_2390, methyltransferase, DELTA24-sterol, PbSMT, phytosterol methyltransferase, S-adenosyl-4-methionine:sterol DELTA24-methyltransferase, S-adenosyl-L-methionine:DELTA24(23)-sterol methyltransferase, SAM:SMT, SMT, SMT protein, SMT1, SMT80, SMT90, sterol 24-C-methyltransferase, sterol C24-methyltransferase, sterol methyltransferase, STM, TbSMT, zymosterol 24-methyltransferase, zymosterol-24-methyltransferase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.41 sterol 24-C-methyltransferase

Engineering

Engineering on EC 2.1.1.41 - sterol 24-C-methyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
A193L
A193S
A196L
A200L
A221L
A350L
C128L
C128S
-
Km (mM) (substrate: AdoMet): 30, kcat (1/sec) (substrate: AdoMet): 0.005, Kd (mM) (zymosterol): 0.005, Kd (mM) (AdoMet): 0.008
C198L
C198V
D125L
D152L
D189L
D229L
relative activity: 100%
D276L
E108L
E195L
E209L
E224L
relative activity: 74%
E246L
F178L
F183L
100% relative enzyme activity
F188L
F220L
F269L
F357L
G127L
G129L
G131L
G132L
G217L
G218L
G347L
G351L
G352L
H107L
H199L
H199Q
H199R
H224L
-
the ratio of turnover-number to KM-value for zymosterol is 1.4fold lower than the wild-type ratio
H238L
I194L
K215L
K353L
56% relative enzyme activity
P133L
P201L
P216L
S354L
S87E
100% relative enzyme activity
S87Q
100% relative enzyme activity
S97E
relative activity: 100%
S97Q
relative activity: 100%
T197L
T219L
32% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
V126L
V130L
V222L
27% relative enzyme activity
V349L
W225F
W225L
W286F
W286L
Y153F
Y153L
Y192F
100% relative enzyme activity, mutant can perform C2-transfer activity to give 24-ethyl(idene)-sterols
Y192L
95% relative enzyme activity
Y207F
Y207L
Y223F
Y223L
Y287L
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
additional information