Information on EC 4.2.3.6 - trichodiene synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.2.3.6
-
RECOMMENDED NAME
GeneOntology No.
trichodiene synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-C bond cleavage
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
calonectrin biosynthesis
-
-
Sesquiterpenoid and triterpenoid biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl diphosphate diphosphate-lyase (cyclizing, trichodiene-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
101915-76-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
BL21 DE3 /pZW03
-
-
Manually annotated by BRENDA team
strain PH-1, teleomorph Gibberella zeae
UniProt
Manually annotated by BRENDA team
NRLL 3299
-
-
Manually annotated by BRENDA team
UAMH 5334
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
UAMH 1369
UniProt
Manually annotated by BRENDA team
UAMH 1369
UniProt
Manually annotated by BRENDA team
CBS 203.61
UniProt
Manually annotated by BRENDA team
UAMH 7122
UniProt
Manually annotated by BRENDA team
UAMH 7748
UniProt
Manually annotated by BRENDA team
UAMH 7748
UniProt
Manually annotated by BRENDA team
CBS 304.54
UniProt
Manually annotated by BRENDA team
UAMH 3195
UniProt
Manually annotated by BRENDA team
CBS 388.73
UniProt
Manually annotated by BRENDA team
UAMH 7746
UniProt
Manually annotated by BRENDA team
CBS 186.79
UniProt
Manually annotated by BRENDA team
UAMH 7747
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
DAOM 57205
UniProt
Manually annotated by BRENDA team
UAMH 7839
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
(3R)-nerolidyl diphosphate
?
show the reaction diagram
(7S)-6,7-dihydrofarnesyl diphosphate
dihydrofarnesene isomers + (E)-6,7-dihydrofarnesol + (3S,7S)-6,7-dihydronerolidol
show the reaction diagram
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
(Z,E)-farnesyl diphosphate
?
show the reaction diagram
-
-
-
-
?
2-fluorofarnesyl diphosphate
?
show the reaction diagram
-
-
sesquiterpene mixture
-
?
4-methylfarnesyl diphosphate
?
show the reaction diagram
-
-
sesquiterpene mixture
-
?
trans,trans-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
additional information
?
-
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
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
trans,trans-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
additional information
?
-
-
involved in biosynthesis of trichothecene mycotoxins
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
at 0.01 mM, can partially replace Mg2+, inhibition at higher concentration
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(7R)-(E)-6,7-dihydrofarnesyl diphosphate
-
-
(7S)-(E)-6,7-dihydrofarnesyl diphosphate
-
modestly competitive
10-cyclopropylidene farnesyl diphosphate
-
mechanism-based inhibitor
10-fluorofarnesyl diphosphate
-
-
benzyl triethylammonium cation
-
BTAC alone does not inhibit the trichodiene synthase, 5-30 microM acts as a competitive inhibitor in the presence of 5-20 microM PPi
diphosphate
-
PPi
farnesyl diphosphate analogs
Mn2+
-
0.01 mM, can partially replace Mg2+, inhibition at higher concentration
additional information
-
identification of active site residues by site-directed mutagenesis
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000089
(3R)-nerolidyl diphosphate
-
pH 7.5
0.00009
(E,E)-farnesyl diphosphate
-
pH 7.5
0.000036
(Z,E)-farnesyl diphosphate
-
pH 7.5
0.000065 - 0.006
farnesyl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 0.138
farnesyl diphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00022
(7R)-(E)-6,7-dihydrofarnesyl diphosphate
-
-
0.000395
(7S)-(E)-6,7-dihydrofarnesyl diphosphate
-
-
0.000663
10-cyclopropylidene farnesyl diphosphate
-
-
0.000016
10-fluorofarnesyl diphosphate
-
pH 7.5
0.036
benzyl triethylammonium cation
-
induced inhibition constant for BTAC in the presence of PPi
0.00049 - 0.0007
diphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
pH 6.0: about 40% of activity maximum, pH 8.0: about 70% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 45000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized by the hanging drop vapor diffusion method, in complex with Mg2+, PPi, the benzyl triethylammonium cation, at a resolution of 2.85 A
-
mutant D100E and its complex with diphosphate
-
recombinant enzyme, both unliganded and in complex with diphosphate
-
the structures of the mutants are solved at resolutions ranging from 2.1 to 2.7 A
-
X-ray crystal structures of mutant R304K and its complexes with diphosphate and aza analogues of the bisabolyl carbocation intermediate
-
X-ray structures of the Y305F and D100E mutants and their complexes with diphosphate and aza analogues of the bisabolyl carbocation intermediate
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
BL21 DE3/pZW03
expressed in Escherichia coli, partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
expresssion in Trichoderma harzianum CECT 2413
for expression in Escherichia coli BL21DE3 cells
-
homologous overexpression in Trichoderma Brevicompactum
TRI5 gene is deleted using the split-marker technique, tri5 mutant shows reduced virulence when inoculated into wheat florets
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is up-regulated in media with glucose, H2O2 or glycerol
tri5 repression is observed in cultures supplemented with the antioxidants ferulic acid and tyrosol
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C146A
-
complete loss of activity
C190A
-
significantly reduced enzymatic activity
D102E
-
mutation in substrate binding domain, mutant generates anomalous sesquiterpenes
D104E
-
mutant generates anomalous sesquiterpenes, proportion of anomalous products increases if enzyme is incubated in presence of Mn2+
D98E
-
mutation in substrate binding domain, mutant generates anomalous sesquiterpenes
D99E
-
mutation in substrate binding domain, mutant generates anomalous sesquiterpenes
N225D
-
mutation in the fungal NSE motif, responsible for chelating Mg2+, mutant generates a different distribution of sesquiterpene products
N225D, S229T
-
mutation in the fungal NSE motif, responsible for chelating Mg2+, inactive mutant
R304K
-
mutant with significant loss in activity
S229T
-
mutation in the fungal NSE motif, responsible for chelating Mg2+, mutant generates a different distribution of sesquiterpene products
Y295F
-
mutation in the fungal NSE motif, responsible for chelating Mg2+, mutant generates a different distribution of sesquiterpene products
Y305F
-
mutant with few local variations in the active site
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
mutants D98E, D99E, D102E generate varying proportions of anomalous sesquiterpenes