Information on EC 4.2.3.7 - pentalenene synthase

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The expected taxonomic range for this enzyme is: Streptomyces

EC NUMBER
COMMENTARY
4.2.3.7
-
RECOMMENDED NAME
GeneOntology No.
pentalenene synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(2E,6E)-farnesyl diphosphate = pentalenene + diphosphate
show the reaction diagram
the initial step in the reaction is probably a cyclization of farnesyl diphosphate to form humulene. The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics
-
-
-
(2E,6E)-farnesyl diphosphate = pentalenene + diphosphate
show the reaction diagram
stereochemistry
-
(2E,6E)-farnesyl diphosphate = pentalenene + diphosphate
show the reaction diagram
mechanism; stereochemistry
-
(2E,6E)-farnesyl diphosphate = pentalenene + diphosphate
show the reaction diagram
stereochemistry, SE reaction type
-
(2E,6E)-farnesyl diphosphate = pentalenene + diphosphate
show the reaction diagram
mechanism
-
(2E,6E)-farnesyl diphosphate = pentalenene + diphosphate
show the reaction diagram
mechanism; stereochemistry; stereochemistry; stereochemistry, SE reaction type
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cyclization
Q55012
-
P-O bond cleavage
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
neopentalenoketolactone and pentalenate biosynthesis
-
pentalenolactone biosynthesis
-
Sesquiterpenoid and triterpenoid biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl diphosphate diphosphate-lyase (cyclizing, pentalenene-forming)
Isolated from Streptomyces avermitilis. The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics. The 9si hydrogen of farnesyl diphosphate undergoes a 1,2-hydride shift where it becomes the 1alpha hydrogen of pentalenene.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EC 4.6.1.5
-
-
formerly
-
pentalenene synthase
Q55012
-
pentalenene synthetase
-
-
-
-
synthetase, pentalenene
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
90597-46-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
in this theoretical study Streptomyces is given as an example for a pentalenene synthesizing organism
SwissProt
Manually annotated by BRENDA team
Streptomyces sp. UC53 19
-
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
Streptomyces sp. UC53 19
Q55012
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
-
-
2-trans,6-trans-farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
Q55012
the study describes theoretical studies on the cyclization reaction
-
-
?
2-trans,6-trans-farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
-
-
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
Q55012
-
-
-
-
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
the initial step in the reaction is probably a cyclization of farnesyl diphosphate to form humulene
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
trans,trans
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
trans,trans
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-, trans,trans
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-, the initial step in the reaction is probably a cyclization of farnesyl diphosphate to form humulene
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-, trans,trans
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
Q55012
-
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-trans,6-trans-farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
Q55012
the study describes theoretical studies on the cyclization reaction
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
farnesyl diphosphate
pentalenene + diphosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
divalent metal required, Mg2+ or Mn2+
Mg2+
-
absolute requirement
Mg2+
-
required
Mn2+
-
divalent metal required, Mg2+ or Mn2+, inhibition above 2.5 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
diphosphate
-
plus pentalene: no inhibition alone, both products bind cooperatively at the active site
diphosphate
-
-
Mn2+
-
divalent metal required, Mg2+ or Mn2+, inhibition above 2.5 mM
Pentalenene plus diphosphate
-
no inhibition alone, both products bind cooperatively at the active site
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00077
-
(E,E)-farnesyl diphosphate
-
30C, pH 8.4
0.0003
-
farnesyl diphosphate
-
30C, pH 8.2
0.00031
-
farnesyl diphosphate
-
30C, pH 8.2
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0032
-
diphosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.287
-
-
30C, pH 8.4
0.324
-
-
30C, pH 8.2
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.2
8.4
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
from a 60 h cell culture
Manually annotated by BRENDA team
-
from a 60 h cell culture
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
57000
-
-
gel filtration
57000
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 41000, SDS-PAGE
?
-
x * 41000, SDS-PAGE
-
monomer
-
1 * 42500
monomer
Streptomyces sp. UC53 19
-
1 * 42500
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method, using 1-1.4 M sodium citrate or 1.4-1.8 M ammonium sulfate as precipitant
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, crude enzyme stable for up to 6 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydroxyapatite column chromatography and Sephadex 200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F77Y
-
compared to wild type, kcat/Km value is 20fold lower
H309A
-
retains enzymatic activity, minor increase in Km-value
H309C
-
retains enzymatic activity, minor increase in Km-value
H309F
-
retains enzymatic activity, minor increase in Km-value
H309F
-
reaction products are pentalene plus varying proportions of (+)-germacrene A and protoilludene
H309S
-
retains enzymatic activity, minor increase in Km-value
N219A
-
catalytically inactive
N219D
-
compared to wild type, kcat/Km value is 3300fold lower, reaction products are pentalene plus beta-caryophyllene
N219L
-
catalytically inactive
W308F
-
reaction products are pentalene plus varying proportions of (+)-germacrene A
W308F/H309F
-
reaction products are pentalene plus varying proportions of (+)-germacrene A