Information on EC 5.5.1.15 - terpentedienyl-diphosphate synthase

for references in articles please use BRENDA:EC5.5.1.15
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
5.5.1.15
-
top print hide
RECOMMENDED NAME
GeneOntology No.
terpentedienyl-diphosphate synthase
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranylgeranyl diphosphate = terpentedienyl diphosphate
show the reaction diagram
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
terpentecin biosynthesis
-
-
Biosynthesis of antibiotics
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
terpentedienyl-diphosphate lyase (decyclizing)
Requires Mg2+. Contains a DXDD motif, which is a characteristic of diterpene cylases whose reactions are initiated by protonation at the 14,15-double bond of geranylgeranyl diphosphate (GGDP) [2]. The triggering proton is lost at the end of the cyclization reaction [3]. The product of the reaction, terpentedienyl diphosphate, is the substrate for EC 4.2.3.36, terpentetriene synthase and is a precursor of the diterpenoid antibiotic terpentecin.
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
429681-55-0
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
geranylgeranyl diphosphate
terpentedienyl diphosphate
show the reaction diagram
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
the enzyme activity of the Cyc1 is highest at a concentration of 1 mM but slightly inhibited at a concentration of 10 mM (decreased 40%)
additional information
-
no activity is detected with other divalent metal ions such as Ca2+, Co2+, Cu2+, Fe2+, Mn2+, and Zn2+ at both 1 and 10 mM
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
geranylgeranyl diphosphate
-
above 0.05 mM
top print hide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
20% glycerol, 5 mM 2-mercaptoethanol, and 0.1% Tween 80 are required for the full activity of the Cyc1
-
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0642
geranylgeranyl diphosphate
-
-
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
Tris-HCl buffer
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
-
25-30: optimum, 50°C, no activity detected above
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
gel filtration
top print hide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
full activity after incubation at 30°C in 0.05 M Tris-HCl buffer for 1 h
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
heterologous expression of the cyclase genes in Streptomyces lividans and Escherichia coli
-
top
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 5.5.1.15)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)