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
4.2.3.6
-
RECOMMENDED NAME
GeneOntology No.
trichodiene synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
show the reaction diagram
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
stereochemistry, mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-C bond cleavage
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Sesquiterpenoid and triterpenoid biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl diphosphate diphosphate-lyase (cyclizing, trichodiene-forming)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sesquiterpene cyclase
-
-
-
-
synthase, trichodiene
-
-
-
-
trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase
-
-
-
-
trichodiene synthetase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
101915-76-8
-
ORGANISM
COMMENTARY
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
R-6380, Fusarium sambucinum, regulation of enzyme
-
-
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
Fusarium verticillioides NRRL 20956
-
-
-
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
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
Q6A1B7
expression of enzyme gene tri5 in the biocontrol strain Trichoderma harzianum CECT 2413 results in production of trichodiene in parallel with a reduction of ergosterol biosynthesis and an increase in the level of squalene. Transformants expressing tri5 display low chitinase activity and induced expression of Botrytis cinerea BOT genes, although their total antagonistic potential against phytopathogenic fungi is not reduced. Volatile organic compounds released by the tri5-transformant induce expression of tomato defence genes related to salicylic acid, and trichodiene itself strongly induces the expression of salicylic acid-responsive genes and reduces the development of lateral roots
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
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
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
Fusarium verticillioides, Fusarium verticillioides NRRL 20956
-
-
biosynthesis occurs via the (R)-bisabolyl cation to the (S)-cuprenyl cation by a 1,5-proton transfer. This conversion proceeds via a 7Si,11Re cyclisation and without exchange of the migrating proton. Side products (-)-alpha-cedrene, (+)-beta-cedrene, and (+)-alpha-funebrene found in Fusarium verticillioides can originate via the (R)-bisabolyl cation
-
?
(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
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
Fusarium sambucinum, Fusarium sporotrichioides NRLL 3299
-
-
-
?
additional information
?
-
-
involved in biosynthesis of trichothecene mycotoxins
-
-
-
METALS and IONS
ORGANISM
UNIPROT
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
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
diphosphate
-
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]
SUBSTRATE
ORGANISM
UNIPROT
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]
SUBSTRATE
ORGANISM
UNIPROT
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]
INHIBITOR
ORGANISM
UNIPROT
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]
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
pH 6.0: about 40% of activity maximum, pH 8.0: about 70% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
-
gel filtration
648334
89000
-
-
677828, 677834
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 45000, SDS-PAGE
?
-
x * 43999, calculated from nucleotide sequence
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
TRI5 gene is deleted using the split-marker technique, tri5 mutant shows reduced virulence when inoculated into wheat florets
Q00909
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
for expression in Escherichia coli BL21DE3 cells
-
homologous overexpression in Trichoderma Brevicompactum
F4MJM0
expresssion in Trichoderma harzianum CECT 2413
Q6A1B7
EXPRESSION
ORGANISM
UNIPROT
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
COMMENTARY
LITERATURE
C146A
-
complete loss of activity
C190A
-
significantly reduced enzymatic activity
D100E
-
crystal structure
D100E
-
mutant generates anomalous sesquiterpenes, proportion of anomalous products increases if enzyme is incubated in presence of Mn2+
D100E
-
mutant with different binding of diphosphate
D101E
-
mutant generates anomalous sesquiterpenes, proportion of anomalous products increases if enzyme is incubated in presence of Mn2+
D101E
-
Km-value for farneyl diphosphate: 124 nM
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
Y305F
-
mutant with few local variations in the active site
additional information
-
hybrid of enzyme from both organisms, site directed mutagenesis of hybrid
D99E
-
mutation in substrate binding domain, mutant generates anomalous sesquiterpenes
additional information
-
hybrid of enzyme from both organisms, site directed mutagenesis of hybrid
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
mutants D98E, D99E, D102E generate varying proportions of anomalous sesquiterpenes