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Information on EC 2.1.1.255 - geranyl diphosphate 2-C-methyltransferase and Organism(s) Streptomyces coelicolor and UniProt Accession Q9F1Y5
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EC Tree
2.1.1.255 geranyl diphosphate 2-C-methyltransferaseIUBMB Comments
This enzyme, along with EC 4.2.3.118, 2-methylisoborneol synthase, produces 2-methylisoborneol, an odiferous compound produced by soil microorganisms with a strong earthy/musty odour.
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Word Map
- 2.1.1.255
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cyclization
- 2-methylisoborneol
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terpenoids
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c-methylation
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taste
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monoterpene
- coelicolor
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carbocation
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odor
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actinomycete
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isoprenoids
- cyanobacteria
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terpene
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sam-dependent
- limnetica
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s-adenosyl-l-methionine-dependent
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unpleasant
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dimethylallyl
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farnesyl
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pseudanabaena
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t-butyl
- ethylbenzene
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intermediacy
- lanosterol
The taxonomic range for the selected organisms is: Streptomyces coelicolor
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
gppmt, c-methyl transferase, sco7701, gpp methyltransferase, sco7701 protein, geranyl pyrophosphate methyltransferase, geranyl diphosphate c-methyltransferase, geranyl diphosphate 2-methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-methyl-GPP synthase
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geranyl pyrophosphate methyltransferase
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-
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GPP methyltransferase
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-
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GPPMT
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-
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MGPPS
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-
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SCO7701
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-
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-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + geranyl diphosphate = S-adenosyl-L-homocysteine + (E)-2-methylgeranyl diphosphate
catalytic reaction mechanism, detailed overview
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:geranyl-diphosphate 2-C-methyltransferase
This enzyme, along with EC 4.2.3.118, 2-methylisoborneol synthase, produces 2-methylisoborneol, an odiferous compound produced by soil microorganisms with a strong earthy/musty odour.
CAS REGISTRY NUMBER
COMMENTARY
57219-74-6
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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
S-adenosyl-L-methionine + (E)-2-methylgeranyl diphosphate
S-adenosyl-L-homocysteine + 2-methylisoborneol
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-
-
?
S-adenosyl-L-methionine + geranyl diphosphate
S-adenosyl-L-homocysteine + (E)-2-methylgeranyl diphosphate
S-adenosyl-L-methionine + geranyl diphosphate
S-adenosyl-L-homocysteine + (E)-2-methylgeranyl diphosphate
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-
-
?
S-adenosyl-L-methionine + geranyl diphosphate
S-adenosyl-L-homocysteine + (E)-2-methylgeranyl diphosphate
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-
-
-
?
S-adenosyl-L-methionine + geranyl diphosphate
S-adenosyl-L-homocysteine + (E)-2-methylgeranyl diphosphate
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GC-MS analysis of the products from recombinant SCO7700 reveals the formation of a complex mixture of cyclic monoterpenes, consisting of alpha-pinene at 6%, beta-pinene at 23%, limonene at 32%, gamma-terpinene at 29%, and delta-terpinene at 10% accompanied by traces of the monoterpene alcohols beta-terpineol, 4-terpineol, and alpha-terpineol
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?
additional information
?
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SCO7701 shows no activity with with farnesyl diphosphate or geranylgeranyl diphosphate
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?
additional information
?
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SCO7701 shows no activity with with farnesyl diphosphate or geranylgeranyl diphosphate
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?
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
S-adenosyl-L-methionine + geranyl diphosphate
S-adenosyl-L-homocysteine + (E)-2-methylgeranyl diphosphate
S-adenosyl-L-methionine + geranyl diphosphate
S-adenosyl-L-homocysteine + (E)-2-methylgeranyl diphosphate
-
-
-
?
S-adenosyl-L-methionine + geranyl diphosphate
S-adenosyl-L-homocysteine + (E)-2-methylgeranyl diphosphate
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-
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.026
(E)-2-methylgeranyl diphosphate
pH 7.0, 37°C, recombinant enzyme
0.0131
geranyl diphosphate
pH and temperature not specified in the publication
0.0043
S-adenosyl-L-methionine
pH 7.0, 37°C, recombinant enzyme
0.0043
S-adenosyl-L-methionine
pH and temperature not specified in the publication
additional information
additional information
steady-state kinetics, Michaelis-Menten kinetics
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additional information
additional information
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steady-state kinetics, Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.039
(E)-2-methylgeranyl diphosphate
pH 7.0, 37°C, recombinant enzyme
0.0075
geranyl diphosphate
pH and temperature not specified in the publication
0.0075
S-adenosyl-L-methionine
pH 7.0, 37°C, recombinant enzyme
0.0075
S-adenosyl-L-methionine
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
geranyl diphosphate C-methyltransferase is the methyltransferase that modifies an acyclic isoprenoid diphosphate, geranyl diphosphate, to yield a noncanonical acyclic allylic diphosphate product, 2-methylgeranyl diphosphate, which serves as the substrate for a subsequent cyclization reaction catalyzed by a terpenoid cyclase, methylisoborneol synthase
metabolism
geranyl diphosphate C-methyltransferase is the methyltransferase that modifies an acyclic isoprenoid diphosphate, geranyl diphosphate, to yield a noncanonical acyclic allylic diphosphate product, 2-methylgeranyl diphosphate, which serves as the substrate for a subsequent cyclization reaction catalyzed by a terpenoid cyclase, methylisoborneol synthase
metabolism
the C-methyl transferase SCO7701 catalyzes the two-step conversion of geranyl diphosphate to 2-methyl-isoborneol by way of 2-methylgeranyl diphosphate
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
49937
x * 49937, recombinant N-terminally His6-tagged soluble SCO7700, mass spectrometry, x * 49955, sequence calculation
49955
x * 49937, recombinant N-terminally His6-tagged soluble SCO7700, mass spectrometry, x * 49955, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 49937, recombinant N-terminally His6-tagged soluble SCO7700, mass spectrometry, x * 49955, sequence calculation
hexamer
hexameric quaternary structure of geranyl diphosphate methyltransferase in the crystal, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged wild-type enzyme in complex with S-adenosyl-L-methionine and monoterpenoid ligands geranyl-S-thiolodiphosphate, a substrate analogue, or geranyl diphosphate, sitting drop vapor diffusion method, 4°C, mixing of 0.001 ml protein solution conatining 6 mg/mL enzyme, 50 mM PIPES, pH 6.7, 20% glycerol, 5 mM BME, 15 mM MgCl2, 100 mM NaCl, 10 mM S-adenosyl-L-methionine, and 1 mM monoterpenoid ligand with 0.001 ml of precipitant solution containing 100 mM HEPES, pH 7.5, 25% polyethylene glycol 3350, and 200 mM (NH4)2SO4 for cocrystallization with geranyl-S-thiolodiphosphate, 100 mM Bis-Tris, pH 6.5, 25% polyethylene glycol 3350, and 200 mM (NH4)2SO4 for cocrystallization with geranyl diphosphate and equilibrated against a 0.1 ml reservoir of precipitant solution at 21°C, 1 day, X-ray diffraction structure determination and analysis at 2.05 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y51F
site-directed mutagenesism the utant shows a 2fold reduction in kcat and no effect on KM for either substrate compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged soluble SCO7700 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity and over 95% purity
soluble recombinant His6-tagged wild-type and mutant geranyl diphosphate methyltransferase from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene sco7700, DNA and amino acid sequence determination and analysis, expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
wild-type and mutant geranyl diphosphate methyltransferase expression as His6-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, C.M.; Cane, D.E.
Biochemistry and molecular genetics of the biosynthesis of the earthy odorant methylisoborneol in Streptomyces coelicolor
J. Am. Chem. Soc.
130
8908-8909
2008
Streptomyces coelicolor (Q9F1Y5), Streptomyces coelicolor
Koeksal, M.; Chou, W.K.; Cane, D.E.; Christianson, D.W.
Structure of geranyl diphosphate C-methyltransferase from Streptomyces coelicolor and implications for the mechanism of isoprenoid modification
Biochemistry
51
3003-3010
2012
Streptomyces coelicolor (Q9F1Y5), Streptomyces coelicolor, Streptomyces coelicolor A3(2) (Q9F1Y5), Streptomyces coelicolor A3(2)
EXTERNAL LINKS (specific for EC-Number 2.1.1.255)
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Release 2023.1 (January 2023)
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