Information on EC 4.2.3.6 - trichodiene synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
4.2.3.6
-
RECOMMENDED NAME
GeneOntology No.
trichodiene synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
show the reaction diagram
-
-
-
-
(2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
show the reaction diagram
stereochemistry, mechanism
-
(2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
show the reaction diagram
mechanism
-
(2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
show the reaction diagram
mechanism, kinetics, isomerization of farnesyl diphosphate to nerolidyl diphosphate is the rate limiting step
-
(2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C-C bond cleavage
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Sesquiterpenoid and triterpenoid biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl diphosphate diphosphate-lyase (cyclizing, trichodiene-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EC 4.1.99.6
-
-
formerly
-
sesquiterpene cyclase
-
-
-
-
synthase, trichodiene
-
-
-
-
trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase
-
-
-
-
tri5
F4MJM0
gene name
tri5
Trichoderma brevicompactum IBT40841
F4MJM0
gene name
-
trichodiene synthase
-
-
trichodiene synthase
D0FL92
-
trichodiene synthase
P13513
-
trichodiene synthase
Fusarium sporotrichioides UAMH 5334
D0FL92
-
-
trichodiene synthase
-
gene tri5
trichodiene synthase
Q00909
-
trichodiene synthase
D0FL95
-
trichodiene synthase
Myrothecium roridum UAMH 1369
D0FL95
-
-
trichodiene synthase
D0FL84, D0FL88
-
trichodiene synthase
Stachybotrys cylindrospora CBS 203.61
D0FL84
-
-
trichodiene synthase
Stachybotrys cylindrospora UAMH 7122
D0FL88
-
-
trichodiene synthase
D0FL91
-
trichodiene synthase
Stachybotrys dichroa UAMH 7748
D0FL91
-
-
trichodiene synthase
D0FL84, D0FL85
-
trichodiene synthase
Stachybotrys echinata CBS 304.54
D0FL85
-
-
trichodiene synthase
Stachybotrys echinata UAMH 3195
D0FL84
-
-
trichodiene synthase
D0FL86, D0FL89
-
trichodiene synthase
Stachybotrys kampalensis CBS 388.73
D0FL86
-
-
trichodiene synthase
Stachybotrys kampalensis UAMH 7746
D0FL89
-
-
trichodiene synthase
D0FL83, D0FL90
-
trichodiene synthase
Stachybotrys microspora CBS 186.79
D0FL83
-
-
trichodiene synthase
Stachybotrys microspora UAMH 7747
D0FL90
-
-
trichodiene synthase
D0FL93
-
trichodiene synthase
Trichothecium roseum DAOM 57205, Trichothecium roseum UAMH 7839
D0FL93
-
-
trichodiene synthetase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
101915-76-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
BL21 DE3 /pZW03
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
expression in Nicotiana tabacum
-
-
Manually annotated by BRENDA team
mutant C146A and C190A constructed by site-directed mutagenesis; recombinant enzyme from Escherichia coli BL21 DE3/pZW03
-
-
Manually annotated by BRENDA team
native enzyme; recombinant enzyme from Escherichia coli BL21 DE3/pZW03
-
-
Manually annotated by BRENDA team
Fusarium sporotrichioides NRLL 3299
NRLL 3299
-
-
Manually annotated by BRENDA team
Fusarium sporotrichioides UAMH 5334
UAMH 5334
UniProt
Manually annotated by BRENDA team
R-6380, Fusarium sambucinum, regulation of enzyme
-
-
Manually annotated by BRENDA team
strain PH-1, teleomorph Gibberella zeae
UniProt
Manually annotated by BRENDA team
UAMH 1369
UniProt
Manually annotated by BRENDA team
Myrothecium roridum UAMH 1369
UAMH 1369
UniProt
Manually annotated by BRENDA team
Stachybotrys cylindrospora CBS 203.61
CBS 203.61
UniProt
Manually annotated by BRENDA team
Stachybotrys cylindrospora UAMH 7122
UAMH 7122
UniProt
Manually annotated by BRENDA team
UAMH 7748
UniProt
Manually annotated by BRENDA team
Stachybotrys dichroa UAMH 7748
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
Stachybotrys echinata CBS 304.54
CBS 304.54
UniProt
Manually annotated by BRENDA team
Stachybotrys echinata UAMH 3195
UAMH 3195
UniProt
Manually annotated by BRENDA team
Stachybotrys kampalensis CBS 388.73
CBS 388.73
UniProt
Manually annotated by BRENDA team
Stachybotrys kampalensis UAMH 7746
UAMH 7746
UniProt
Manually annotated by BRENDA team
Stachybotrys microspora CBS 186.79
CBS 186.79
UniProt
Manually annotated by BRENDA team
Stachybotrys microspora UAMH 7747
UAMH 7747
UniProt
Manually annotated by BRENDA team
Trichoderma brevicompactum IBT40841
-
UniProt
Manually annotated by BRENDA team
DAOM 57205; UAMH 7839
UniProt
Manually annotated by BRENDA team
Trichothecium roseum DAOM 57205
DAOM 57205
UniProt
Manually annotated by BRENDA team
Trichothecium roseum UAMH 7839
UAMH 7839
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
F4MJM0, -
tri5 overexpression leads to an increased production of trichodermin and tyrosol. Of these, only trichodermin has antifungal activity against Saccharomyces cerevisiae, Kluyveromyces marxianus, Candida albicans, Candida glabrata, Candida tropicalis and Aspergillus fumigatus
physiological function
Trichoderma brevicompactum IBT40841
-
tri5 overexpression leads to an increased production of trichodermin and tyrosol. Of these, only trichodermin has antifungal activity against Saccharomyces cerevisiae, Kluyveromyces marxianus, Candida albicans, Candida glabrata, Candida tropicalis and Aspergillus fumigatus
-
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
trichodiene + diphosphate
show the reaction diagram
-
-
-
-
?
(3R)-nerolidyl 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
-
-
-
-
?
(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
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
formation of trichodiene involves initial generation of (3R)-nerolidyl diphosphate
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
formation of trichodiene involves initial generation of (3R)-nerolidyl diphosphate
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
formation of trichodiene involves initial generation of (3R)-nerolidyl diphosphate
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
formation of trichodiene involves initial generation of (3R)-nerolidyl diphosphate
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
which cyclizes via the anti-boat conformation
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
Fusarium sporotrichioides NRLL 3299
-
-
-
?
(Z,E)-farnesyl diphosphate
?
show the reaction diagram
-
-
-
-
?
2-fluorofarnesyl diphosphate
?
show the reaction diagram
-
-
sesquiterpene mixture
-
?
trans,trans-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
-
?
trans,trans-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
Q00909
the initial committing step into the trichothecene biosynthetic pathway, enzyme controls mycotoxin biosynthesis
-
-
?
4-methylfarnesyl diphosphate
?
show the reaction diagram
-
-
sesquiterpene mixture
-
?
additional information
?
-
-
reaction proceeds via isomerization of farnesyl diphosphate to (3R)-nerolidyl diphosphate and further to trichodiene
-
-
-
additional information
?
-
-
reaction proceeds via isomerization of farnesyl diphosphate to (3R)-nerolidyl diphosphate and further to trichodiene
-
-
-
additional information
?
-
-
involved in biosynthesis of trichothecene mycotoxins
-
-
-
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
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
trans,trans-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
-
?
trans,trans-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
Q00909
the initial committing step into the trichothecene biosynthetic pathway, enzyme controls mycotoxin biosynthesis
-
-
?
(E,E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
Gibberella pulicaris, Fusarium sporotrichioides NRLL 3299
-
-
-
?
additional information
?
-
-
involved in biosynthesis of trichothecene mycotoxins
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
required, optimum concentration: 1.0 mM, Km: 0.1 mM
Mn2+
-
at 0.01 mM, can partially replace Mg2+, inhibition at higher concentration
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
farnesyl diphosphate analogs
-
-
farnesyl diphosphate analogs
-
10-fluorofarnesyl diphosphate is the most effective competitive inhibitor
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
farnesyl diphosphate
-
30C, pH 7.5
0.000069
-
farnesyl diphosphate
-
mutant Y295F
0.000078
-
farnesyl diphosphate
-
15C, pH 7.8
0.000078
-
farnesyl diphosphate
-
wild-type
0.00009
-
farnesyl diphosphate
-
30C, pH 7.8
0.000124
-
farnesyl diphosphate
-
30C, pH 7.8, mutant D101E
0.000485
-
farnesyl diphosphate
-
mutant N225D
0.006
-
farnesyl diphosphate
-
mutant S229T
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.005
-
farnesyl diphosphate
-
mutant N225D
0.015
-
farnesyl diphosphate
-
mutant S229T
0.111
-
farnesyl diphosphate
-
mutant Y295F
0.138
-
farnesyl diphosphate
-
wild-type
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
diphosphate
-
-
0.0007
-
diphosphate
-
apparent inhibition constant of PPi in the prensence of BTAC
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
Q00909
both the wild-type PH-1 strain and the tri5 mutant exhibit full pathogenicity on Arabidopsis floral tissue; tri5 mutants in strain PH-1 exhibit reduced virulence on wheat ears; wild-type strain inoculations cause high levels of disease in both plant species and significant deoxynivalenol mycotoxin production. The tri5 mutant unable to produce deoxynivalenol mycotoxin exhibits reduced pathogenicity on wheat ears, causing only discrete eye-shaped lesions on spikelets which failed to infect the rachis. The tri5 mutant retains full pathogenicity on Arabidopsis floral tissue
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.8
-
-
activity assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
pH 6.0: about 40% of activity maximum, pH 8.0: about 70% of activity maximum
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
30
-
-
activity assay
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 43999, calculated from nucleotide sequence
?
-
x * 45000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
BL21 DE3/pZW03
-
expressed in Escherichia coli, partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
for expression in Escherichia coli BL21DE3 cells
-
TRI5 gene is deleted using the split-marker technique, tri5 mutant shows reduced virulence when inoculated into wheat florets
Q00909
homologous overexpression in Trichoderma Brevicompactum
F4MJM0, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
tri5 repression is observed in cultures supplemented with the antioxidants ferulic acid and tyrosol
F4MJM0, -
expression is up-regulated in media with glucose, H2O2 or glycerol
F4MJM0, -
tri5 repression is observed in cultures supplemented with the antioxidants ferulic acid and tyrosol
Trichoderma brevicompactum IBT40841
-
-
expression is up-regulated in media with glucose, H2O2 or glycerol
Trichoderma brevicompactum IBT40841
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C146A
-
complete loss of activity
C190A
-
significantly reduced enzymatic activity
D100E
-
mutant generates anomalous sesquiterpenes, proportion of anomalous products increases if enzyme is incubated in presence of Mn2+
D100E
-
crystal structure
D100E
-
mutant with different binding of diphosphate
D101E
-
Km-value for farneyl diphosphate: 124 nM
D101E
-
mutant generates anomalous sesquiterpenes, proportion of anomalous products increases if enzyme is incubated in presence of Mn2+
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
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
D99E
-
mutation in substrate binding domain, mutant generates anomalous sesquiterpenes
additional information
-
hybrid of enzyme from both organisms, site directed mutagenesis of hybrid
Y305F
-
mutant with few local variations in the active site
additional information
-
hybrid of enzyme from both organisms, site directed mutagenesis of hybrid
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
mutants D98E, D99E, D102E generate varying proportions of anomalous sesquiterpenes