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Information on EC 4.2.3.150 - cembrene A synthase
for references in articles please use BRENDA:EC4.2.3.150
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IUBMB Comments
Requires Mg2+. Isolated from the bacterium Streptomyces sp. SANK 60404. This trifunctional enzyme, which contains a [4Fe-4S] cluster, also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
showSynonyms
CAS, DtcycB, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CAS
DtcycB
DtcycB
-
-
-
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DtcycB
gene name. The trifunctional enzyme also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase
DtcycB
gene name. The trifunctional enzyme also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranylgeranyl diphosphate = (R)-cembrene A + diphosphate
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-
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geranylgeranyl diphosphate = (R)-cembrene A + diphosphate
the cyclization mechanism from geranylgeranyl diphosphate to cembrene A requires a 1,14-cyclization to the ent-cembranyl cation and deprotonation of one of the geminal methyl groups, reaction mechanism, overview
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geranylgeranyl diphosphate = (R)-cembrene A + diphosphate
the cyclization mechanism from geranylgeranyl diphosphate to cembrene A requires a 1,14-cyclization to the ent-cembranyl cation and deprotonation of one of the geminal methyl groups, reaction mechanism, overview
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SYSTEMATIC NAME
IUBMB Comments
geranylgeranyl-diphosphate diphosphate-lyase [(R)-cembrene-A-forming]
Requires Mg2+. Isolated from the bacterium Streptomyces sp. SANK 60404. This trifunctional enzyme, which contains a [4Fe-4S] cluster, also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geranylgeranyl diphosphate
(R)-cembrene A + diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
(R)-cembrene A + diphosphate
Substrates: the trifunctional enzyme also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase
Products: (R)-cembrene A i.e. (1E,5E,9E,12R)-1,5,9-trimethyl-12-(propan-2-en-2-yl)cyclotetradeca-1,5,9-triene
Products: (R)-cembrene A i.e. (1E,5E,9E,12R)-1,5,9-trimethyl-12-(propan-2-en-2-yl)cyclotetradeca-1,5,9-triene
?
geranylgeranyl diphosphate
(R)-cembrene A + diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
(R)-cembrene A + diphosphate
Substrates: the trifunctional enzyme also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol. See EC 4.2.3.149, nephthenol synthase and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase
Products: (R)-cembrene A i.e. (1E,5E,9E,12R)-1,5,9-trimethyl-12-(propan-2-en-2-yl)cyclotetradeca-1,5,9-triene
Products: (R)-cembrene A i.e. (1E,5E,9E,12R)-1,5,9-trimethyl-12-(propan-2-en-2-yl)cyclotetradeca-1,5,9-triene
?
geranylgeranyl diphosphate
(R)-cembrene A + diphosphate
-
Substrates: reaction of enzyme mutant W753H, cembrene A is only a side product for the wild-type enzyme
Products: -
Products: -
?
geranylgeranyl diphosphate
(S)-(+)-cembrene A + diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
(S)-(+)-cembrene A + diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
cembrene A + diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
cembrene A + diphosphate
-
Substrates: activity of enzyme mutants F107A and W186L, not of wild-type enzyme
Products: -
Products: -
?
geranylgeranyl diphosphate
cembrene A + diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
cembrene A + diphosphate
-
Substrates: activity of enzyme mutants F107A and W186L, not of wild-type enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: product identification by NMR spectroscopic analysis. Development of a method that uses the stereoselectively deuterated precursors (S)- and (R)-(1-13C,1-2H)farnesyl diphosphate and (S)- and (R)-(1-13C,1-2H)geranyl diphosphate to determine the absolute configurations of terpenes
Products: -
Products: -
?
additional information
?
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-
Substrates: product identification by NMR spectroscopic analysis. Development of a method that uses the stereoselectively deuterated precursors (S)- and (R)-(1-13C,1-2H)farnesyl diphosphate and (S)- and (R)-(1-13C,1-2H)geranyl diphosphate to determine the absolute configurations of terpenes
Products: -
Products: -
?
additional information
?
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Substrates: the mutants F107A and W186L follow a different reaction mechanism compared to wild-type CotB2, and produce the different product cembrane A
Products: -
Products: -
?
additional information
?
-
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Substrates: the mutants F107A and W186L follow a different reaction mechanism compared to wild-type CotB2, and produce the different product cembrane A
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geranylgeranyl diphosphate
(R)-cembrene A + diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
(R)-cembrene A + diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
(S)-(+)-cembrene A + diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
(S)-(+)-cembrene A + diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
cembrene A + diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
cembrene A + diphosphate
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
the enzyme seems to be not expressed in laboratory cultures
brenda
additional information
-
the enzyme seems to be not expressed in laboratory cultures
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brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D212E
F107A
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site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product cembrane A instead of cyclooctat-9-en-7-ol
W186L
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site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different products cembrane A and 3,7,18-dolabellatriene and only low amounts of cyclooctat-9-en-7-ol
F107A
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site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product cembrane A instead of cyclooctat-9-en-7-ol
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W186L
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site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different products cembrane A and 3,7,18-dolabellatriene and only low amounts of cyclooctat-9-en-7-ol
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W753H
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the mutation leads to the exclusive formation of side product cembrene A. The simulations of the W753H mutant shows that, in the mutant structure, the His side chain is in the perfect position to deprotonate the cembrenyl cation en route to cembrene formation and that this abortive deprotonation is an energetically facile process
additional information
D212E
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site-directed mutagenesis, the mutation results in strongly decreased activity with Mg2+ and Mn2+
D212E
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site-directed mutagenesis, the mutation results in strongly decreased activity with Mg2+ and Mn2+
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additional information
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mutational analysis of the atypical aspartate-rich motif of CotB2 (EC 4.2.3.146). The substrate specificity of the CotB2 mutants can be completely changed. Proposed cyclization mechanism for CotB2 and its mutants, overview
additional information
-
mutational analysis of the atypical aspartate-rich motif of CotB2 (EC 4.2.3.146). The substrate specificity of the CotB2 mutants can be completely changed. Proposed cyclization mechanism for CotB2 and its mutants, overview
-
additional information
-
a mutation Y841H, analogous to W753H mutation, can possibly lead to formation of verticillane
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cotB2, recombinant expression of His-tagged mutant enzymes in Escherichia coli strain BL21(DE3)
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phylogenetic tree, recombinant expression of wild-type and mutant enzymes in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Meguro, A.; Tomita, T.; Nishiyama, M.; Kuzuyama, T.
Identification and characterization of bacterial diterpene cyclases that synthesize the cembrane skeleton
ChemBioChem
14
316-321
2013
Streptomyces sp. (M1VDX3), Streptomyces sp. SANK 60404 (M1VDX3)
brenda
Tomita, T.; Kim, S.Y.; Teramoto, K.; Meguro, A.; Ozaki, T.; Yoshida, A.; Motoyoshi, Y.; Mori, N.; Ishigami, K.; Watanabe, H.; Nishiyama, M.; Kuzuyama, T.
Structural insights into the CotB2-catalyzed cyclization of geranylgeranyl diphosphate to the diterpene cyclooctat-9-en-7-ol
ACS Chem. Biol.
12
1621-1628
2017
Streptomyces melanosporofaciens, Streptomyces melanosporofaciens MI614-43F2
brenda
Rinkel, J.; Lauterbach, L.; Rabe, P.; Dickschat, J.
Two diterpene synthases for spiroalbatene and cembrene A from allokutzneria albata
Angew. Chem. Int. Ed. Engl.
57
3238-3241
2018
Allokutzneria albata, Allokutzneria albata DSM 44149
brenda
Ansbacher, T.; Freud, Y.; Major, D.
Slow-starter enzymes role of active-site architecture in the catalytic control of the biosynthesis of taxadiene by taxadiene synthase
Biochemistry
57
3773-3779
2018
Taxus brevifolia
brenda
EXTERNAL LINKS (specific for EC-Number 4.2.3.150)
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