Information on EC 5.5.1.12 - copalyl diphosphate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.5.1.12
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RECOMMENDED NAME
GeneOntology No.
copalyl diphosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranylgeranyl diphosphate = (+)-copalyl diphosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclization
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bifunctional enzyme that catalyzes two sequential cyclization reactions in distinct active sites
intramolecular cyclization
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
abietic acid biosynthesis
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Biosynthesis of secondary metabolites
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carnosate bioynthesis
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dehydroabietic acid biosynthesis
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Diterpenoid biosynthesis
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isopimaric acid biosynthesis
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levopimaric acid biosynthesis
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Metabolic pathways
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neoabietic acid biosynthesis
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palustric acid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(+)-copalyl-diphosphate lyase (decyclizing)
In some plants, such as Salvia miltiorrhiza, this enzyme is monofunctional. In other plants this activity is often a part of a bifunctional enzyme. For example, in Selaginella moellendorffii this activity is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.131, miltiradiene synthase, while in the tree Abies grandis (grand fir) it is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.18, abietadiene synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
157972-08-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
LAS1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
farnesyl diphosphate
(E)-beta-farnesene
show the reaction diagram
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-
-
-
?
geranylgeranyl diphosphate
(+)-copalyl diphosphate
show the reaction diagram
geranylgeranyl diphosphate
(-)-abietadiene
show the reaction diagram
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-
-
-
?
geranylgeranyl diphosphate
copalyl diphosphate
show the reaction diagram
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class II terpene synthase reaction
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r
additional information
?
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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
geranylgeranyl diphosphate
(+)-copalyl diphosphate
show the reaction diagram
geranylgeranyl diphosphate
copalyl diphosphate
show the reaction diagram
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class II terpene synthase reaction
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r
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
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100 mM included in assay medium
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14,15-dihydro-15-aza-geranylgeranyl diphosphate
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14,15-dihydro-15-azageranylgeranyl diphosphate
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diethyl dicarbonate
geranylgeranyl diphosphate
norpimarenylamine
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p-hydroxymercuribenzoate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004 - 0.007
geranylgeranyl diphosphate
additional information
geranylgeranyl diphosphate
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mutant T769A, value not determined
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
farnesyl diphosphate
Abies grandis
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0.003 - 2.2
geranylgeranyl diphosphate
additional information
geranylgeranyl diphosphate
Abies grandis
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mutant T769A, value below 10000
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0214
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AgAS is purified using Ni-NTA His-bind resin in batch mode
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of His-tagged enzyme in Escherichia coli
Site-directed mutagenesis is carried out via PCR amplification with overlapping mutagenic primers, and the mutant genes verify by complete sequencing. The resulting wild type and mutant genes are then transferred via directional recombination to the T7-promoter and N-terminal 6xhis fusion expression vector pDEST17. Use of the pDEST17 vector results in a 25 amino acid residue linker between the 6 His-tag and the cloned protein.
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D361A
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lower turnover with geranylgeranyl diphosphate than wild-type
D402A
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lower turnover with geranylgeranyl diphosphate than wild-type
D402E
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lower turnover with geranylgeranyl diphosphate than wild-type
D402N
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lower turnover with geranylgeranyl diphosphate than wild-type
D404E
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lower turnover with geranylgeranyl diphosphate than wild-type
D404N
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lower turnover with geranylgeranyl diphosphate than wild-type
D405A
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lower turnover with geranylgeranyl diphosphate than wild-type
D405E
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lower turnover with geranylgeranyl diphosphate than wild-type
D405N
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lower turnover with geranylgeranyl diphosphate than wild-type
D625A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
D766A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
D845A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
DELTA:107-868
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lower turnover with copalyl diphosphate than wild-type
DELTA:85-849
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no turnover with copalyl diphosphate
E499A
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lower turnover with geranylgeranyl diphosphate than wild-type
E589A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
E699A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
E773A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
E778A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
N765A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
R365A
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lower turnover with geranylgeranyl diphosphate than wild-type
R411A
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lower turnover with geranylgeranyl diphosphate than wild-type
R454A
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lower turnover with geranylgeranyl diphosphate than wild-type
R584A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
R586A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
R762A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
rAS:D96A
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nearly the same turnover with copalyl diphosphate like wild-type
rAS:K86A/R87A
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lower turnover with copalyl diphosphate than wild-type
S721A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
T617A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
T769G
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enzyme activity
T769S
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enzyme activity
T848A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
W358A
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lower turnover with geranylgeranyl diphosphate than wild-type
Y520A
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lower turnover with geranylgeranyl diphosphate than wild-type
Y841F
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
D391G/D392G
site-directed mutagenesis of DIDD motif residues, the mutant lacks type-B activity
D611G/D612G
site-directed mutagenesis of DDLMD motif residues, the mutant lacks type-A cyclase activity