Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.142 extracted from

  • Nes, W.D.; Song, Z.; Dennis, A.L.; Zhou, W.; Nam, J.; Miller, M.B.
    Biosynthesis of phytosterols. Kinetic mechanism for the enzymatic C-methylation of sterols (2003), J. Biol. Chem., 278, 34505-34516.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Glycine max

Inhibitors

Inhibitors Comment Organism Structure
24(28)-methylenecycloartanol competitive with respect to S-adenosyl-L-methionine Glycine max
25-Azacycloartenol noncompetitive inhibitor versus cycloartenol, uncompetitive inhibitor versus S-adenosyl-L-methionine Glycine max
cyclolaudenol dead end inhibitor analog, competitive versus cycloartenol, uncompetitive versus S-adenosyl-L-methionine Glycine max
S-adenosyl-L-homocysteine noncompetitive with respect to S-adenosyl-L-methionine Glycine max

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
24(28)-methylenelanosterol
-
Glycine max
0.022
-
24(28)-methylenecycloartanol
-
Glycine max
0.027
-
lanosterol
-
Glycine max
0.03
-
Cycloartenol
-
Glycine max
0.03
-
24(28)-methylenelophenol
-
Glycine max
0.032
-
31-norcycloartenol
-
Glycine max
0.035
-
Zymosterol
-
Glycine max
0.043
-
parkeol
-
Glycine max
0.045
-
24-dehydropollinstanol
-
Glycine max

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41500
-
4 * 41500, SDS-PAGE Glycine max
161000
-
gel filtration Glycine max

Organism

Organism UniProt Comment Textmining
Glycine max
-
recombinant enzyme
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Glycine max

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Glycine max

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + 24(28)-methylenecycloartanol
-
Glycine max S-adenosyl-L-homocysteine + ?
-
?
S-adenosyl-L-methionine + 24(28)-methylenelanosterol
-
Glycine max S-adenosyl-L-homocysteine + ?
-
?
S-adenosyl-L-methionine + 24(28)-methylenelophenol
-
Glycine max S-adenosyl-L-homocysteine + ?
-
?
S-adenosyl-L-methionine + 24-dehydropollinstanol
-
Glycine max S-adenosyl-L-homocysteine + ?
-
?
S-adenosyl-L-methionine + 31-norcycloartenol
-
Glycine max S-adenosyl-L-homocysteine + ?
-
?
S-adenosyl-L-methionine + cycloartenol 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 Glycine max S-adenosyl-L-homocysteine + ?
-
?
S-adenosyl-L-methionine + lanosterol
-
Glycine max S-adenosyl-L-homocysteine + ?
-
?
S-adenosyl-L-methionine + parkeol
-
Glycine max S-adenosyl-L-homocysteine + ?
-
?
S-adenosyl-L-methionine + zymosterol
-
Glycine max S-adenosyl-L-homocysteine + ?
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 41500, SDS-PAGE Glycine max

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00004
-
25-Azacycloartenol inhibition versus cycloartenol Glycine max
0.0001
-
25-Azacycloartenol inhibition versus S-adenosyl-L-methionine Glycine max
0.007
-
cyclolaudenol inhibition versus cycloartenol Glycine max
0.009
-
24(28)-methylene cycloartanol inhibition versus S-adenosyl-L-methionine Glycine max
0.009
-
cyclolaudenol inhibition versus S-adenosyl-L-methionine Glycine max
0.047
-
S-adenosyl-L-homocysteine inhibition versus cycloartenol Glycine max
0.056
-
S-adenosyl-L-homocysteine inhibition versus S-adenosyl-L-methionine Glycine max
0.171
-
24(28)-methylene cycloartanol inhibition versus cycloartenol Glycine max