Information on EC 2.1.1.263 - botryococcene C-methyltransferase

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The expected taxonomic range for this enzyme is: Botryococcus braunii

EC NUMBER
COMMENTARY hide
2.1.1.263
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RECOMMENDED NAME
GeneOntology No.
botryococcene C-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + C30 botryococcene = 2 S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
show the reaction diagram
overall reaction
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S-adenosyl-L-methionine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene = S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
show the reaction diagram
(2b)
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S-adenosyl-L-methionine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene = S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
show the reaction diagram
(1b)
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S-adenosyl-L-methionine + C30 botryococcene = S-adenosyl-L-homocysteine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene
show the reaction diagram
(2a)
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S-adenosyl-L-methionine + C30 botryococcene = S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene
show the reaction diagram
(1a)
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:botryococcene C-methyltransferase
Isolated from the green alga Botryococcus braunii BOT22. Shows a very weak activity with squalene.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + C30 botryococcene
2 S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
show the reaction diagram
-
overall reaction
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ir
S-adenosyl-L-methionine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene
S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
show the reaction diagram
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?
S-adenosyl-L-methionine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene
S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
show the reaction diagram
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-
?
S-adenosyl-L-methionine + C30 botryococcene
S-adenosyl-L-homocysteine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene
show the reaction diagram
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-
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-
?
S-adenosyl-L-methionine + C30 botryococcene
S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene
show the reaction diagram
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additional information
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mono- and dimethylated products with terminal carbons C-22/C-20 as the atomic acceptor sites for the methyl additions to botryococcene, NMR analysis, overview. TMT-3 shows only low activity with squalene
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + C30 botryococcene
2 S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
show the reaction diagram
-
overall reaction
-
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ir
S-adenosyl-L-methionine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene
S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
show the reaction diagram
-
-
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-
?
S-adenosyl-L-methionine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene
S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
show the reaction diagram
-
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-
?
S-adenosyl-L-methionine + C30 botryococcene
S-adenosyl-L-homocysteine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene
show the reaction diagram
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?
S-adenosyl-L-methionine + C30 botryococcene
S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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Michaelis-Menten enzyme kinetics for TMT-3
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.25
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recombinant enzyme, pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression of TMT-3 in Saccharomyces cerevisiae microsomes leading to mono- and dimethylated products, co-expression of various TMT and SMT-like genes in Saccharomyces cerevisiae strain TN-7
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