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Information on EC 4.2.3.6 - trichodiene synthase and Organism(s) Fusarium sporotrichioides and UniProt Accession P13513

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.6 trichodiene synthase
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Select one or more organisms in this record: ?
This record set is specific for:
Fusarium sporotrichioides
UNIPROT: P13513 not found.
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The taxonomic range for the selected organisms is: Fusarium sporotrichioides
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
trichodiene synthase, trichodiene synthetase, tdn synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trichodiene synthase
-
sesquiterpene cyclase
-
-
-
-
synthase, trichodiene
-
-
-
-
trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase
-
-
-
-
trichodiene synthase
trichodiene synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate = trichodiene + diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-C bond cleavage
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl diphosphate diphosphate-lyase (cyclizing, trichodiene-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
101915-76-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
trans,trans-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(2E,6E)-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
trichodiene + diphosphate + isochamigrene
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
?
-
-
involved in biosynthesis of trichothecene mycotoxins
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
trans,trans-farnesyl diphosphate
trichodiene + diphosphate
show the reaction diagram
-
-
-
?
(2E,6E)-farnesyl diphosphate
trichodiene + diphosphate + isochamigrene
show the reaction diagram
-
-
-
-
?
(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
INHIBITOR
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
0.000069 - 0.006
farnesyl diphosphate
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 - 0.000124
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TRI5_FUSSP
374
0
44000
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43999
-
x * 43999, calculated from nucleotide sequence
45000
80000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 45000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
crystallized by the hanging drop vapor diffusion method, in complex with Mg2+, PPi, the benzyl triethylammonium cation, at a resolution of 2.85 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D100E
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
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+
D101E
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
additional information
-
hybrid of enzyme from both organisms, site directed mutagenesis of hybrid
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, partial
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli BL21
for expression in Escherichia coli BL21DE3 cells
for expression in Escherichia coli BL21DE3 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
mutants D98E, D99E, D102E generate varying proportions of anomalous sesquiterpenes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hohn, T.M.; Vanmiddlesworth, F.
Purification and characterization of the sesquiterpene cyclase trichodiene synthetase from Fusarium sporotrichioides
Arch. Biochem. Biophys.
251
756-761
1986
Fusarium sporotrichioides
Manually annotated by BRENDA team
Cane, D.E.; Yang, G.; Xue, Q.; Shim, J.H.
Trichodiene synthase. Substrate specificity and inhibition
Biochemistry
34
2471-2479
1995
Fusarium sporotrichioides
Manually annotated by BRENDA team
Cane, D.E.; Shim, J.H.; Xue, Q.; Fitzsimons, B.C.
Trichodiene synthase. Identification of active site residues by site-directed mutagenesis
Biochemistry
34
2480-2488
1995
Fusarium sambucinum, Fusarium sporotrichioides
Manually annotated by BRENDA team
Cane, D.E.; Ha, H.J.
Trichodiene biosynthesis and the enzymatic cyclization of nerolidyl pyrophosphate
J. Am. Chem. Soc.
108
3097-3099
1986
Fusarium sporotrichioides, Trichothecium roseum
-
Manually annotated by BRENDA team
Cane, D.E.; Yang, G.
Trichodiene syntase. Stereochemical studies of the cryptic allylic diphosphate isomerase activity using an anomalous substrate
J. Org. Chem.
59
5794-5798
1994
Escherichia coli, Fusarium sporotrichioides
-
Manually annotated by BRENDA team
Cane, D.E.; Pawlak, J.L.; Horak, R.M.
Studies of the cryptic allylic pyrophosphate isomerase activity of trichodiene synthase using the anomalous substrate 6,7-dihydrofarnesyl pyrophosphate
Biochemistry
29
5476-5490
1990
Fusarium sporotrichioides
Manually annotated by BRENDA team
Hohn, T.M.; Beremand, M.N.
Regulation of trichodiene synthase in Fusarium sporotrichioides and Gibberella pulicaris (Fusarium sambucinum)
Appl. Environ. Microbiol.
55
1500-1503
1989
Fusarium sambucinum, Fusarium sporotrichioides, Fusarium sporotrichioides NRLL 3299
Manually annotated by BRENDA team
Hohn, T.M.; Beremand, P.D.
Isolation and nucleotide sequence of a sesquiterpene cyclase gene from the trichothecene-producing fungus Fusarium sporotrichioides
Gene
79
131-138
1989
Fusarium sporotrichioides
Manually annotated by BRENDA team
Hohn, T.M.; Plattner, R.D.
Expression of the trichodiene synthase gene of Fusarium sporotrichioides in Escherichia coli results in sesquiterpene production
Arch. Biochem. Biophys.
275
92-97
1989
Fusarium sporotrichioides
Manually annotated by BRENDA team
Hohn, T.M.; Ohlrogge, J.B.
Expression of a fungal sesquiterpene cyclase in transgenic tobacco
Plant Physiol.
97
460-462
1991
Fusarium sporotrichioides
Manually annotated by BRENDA team
Cane, D.E.; Xue, Q.
Trichodiene Synthase. Enzymic Formation of Multiple Sesquiterpenes by Alteration of the Cyclase Active Site
J. Am. Chem. Soc.
118
1563-1564
1996
Fusarium sporotrichioides
-
Manually annotated by BRENDA team
Cane, D.E.; Chiu, H.T.; Liang, P.H.; Anderson, K.S.
Pre-steady-state kinetic analysis of the trichodiene synthase reaction pathway
Biochemistry
36
8332-8339
1997
Fusarium sporotrichioides
Manually annotated by BRENDA team
Cane, D.E.; Xue, Q.; Fitzsimons, B.C.
Trichodiene synthase. Probing the role of the highly conserved aspartate-rich region by site-directed mutagenesis
Biochemistry
35
12369-12376
1996
Fusarium sporotrichioides
Manually annotated by BRENDA team
Cane, D.E.; Bowser, T.E.
Trichodiene synthase: mechanism-based inhibition of a sesquiterpene cyclase
Bioorg. Med. Chem. Lett.
9
1127-1132
1999
Fusarium sporotrichioides
Manually annotated by BRENDA team
Rynkiewicz, M.J.; Cane, D.E.; Christianson, D.W.
X-ray crystal structures of D100E trichodiene synthase and its pyrophosphate complex reveal the basis for terpene product diversity
Biochemistry
41
1732-1741
2002
Fusarium sporotrichioides (P13513)
Manually annotated by BRENDA team
Rynkiewicz, M.J.; Cane, D.E.; Christianson, D.W.
Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade
Proc. Natl. Acad. Sci. USA
98
13543-13548
2001
Fusarium sporotrichioides (P13513), Fusarium sporotrichioides
Manually annotated by BRENDA team
Vedula, L.S.; Cane, D.E.; Christianson, D.W.
Role of arginine-304 in the diphosphate-triggered active site closure mechanism of trichodiene synthase
Biochemistry
44
12719-12727
2005
Fusarium sporotrichioides (P13513)
Manually annotated by BRENDA team
Vedula, L.S.; Rynkiewicz, M.J.; Pyun, H.J.; Coates, R.M.; Cane, D.E.; Christianson, D.W.
Molecular recognition of the substrate diphosphate group governs product diversity in trichodiene synthase mutants
Biochemistry
44
6153-6163
2005
Fusarium sporotrichioides (P13513)
Manually annotated by BRENDA team
Vedula, L.S.; Zhao, Y.; Coates, R.M.; Koyama, T.; Cane, D.E.; Christianson, D.W.
Exploring biosynthetic diversity with trichodiene synthase
Arch. Biochem. Biophys.
466
260-266
2007
Fusarium sporotrichioides
Manually annotated by BRENDA team
Vedula, L.S.; Jiang, J.; Zakharian, T.; Cane, D.E.; Christianson, D.W.
Structural and mechanistic analysis of trichodiene synthase using site-directed mutagenesis: probing the catalytic function of tyrosine-295 and the asparagine-225/serine-229/glutamate-233-Mg2+B motif
Arch. Biochem. Biophys.
469
184-194
2008
Fusarium sporotrichioides (P13513), Fusarium sporotrichioides
Manually annotated by BRENDA team
Koster, B.; Wong, B.; Straus, N.; Malloch, D.
A multi-gene phylogeny for Stachybotrys evidences lack of trichodiene synthase (tri5) gene for isolates of one of three intrageneric lineages
Mycol. Res.
113
877-886
2009
Fusarium sporotrichioides (D0FL92), Fusarium sporotrichioides UAMH 5334 (D0FL92), Memnoniella dichroa (D0FL91), Memnoniella dichroa UAMH 7748 (D0FL91), Memnoniella echinata (D0FL85), Memnoniella echinata CBS 304.54 (D0FL85), Memnoniella echinata UAMH 3195 (D0FL85), Paramyrothecium roridum (D0FL95), Paramyrothecium roridum UAMH 1369 (D0FL95), Stachybotrys cylindrospora (D0FL84), Stachybotrys cylindrospora (D0FL88), Stachybotrys cylindrospora CBS 203.61 (D0FL84), Stachybotrys cylindrospora UAMH 7122 (D0FL88), Stachybotrys kampalensis (D0FL86), Stachybotrys kampalensis (D0FL89), Stachybotrys kampalensis CBS 388.73 (D0FL86), Stachybotrys kampalensis UAMH 7746 (D0FL89), Stachybotrys microspora (D0FL83), Stachybotrys microspora (D0FL90), Stachybotrys microspora CBS 186.79 (D0FL83), Stachybotrys microspora UAMH 7747 (D0FL90), Trichothecium roseum (D0FL93), Trichothecium roseum DAOM 57205 (D0FL93), Trichothecium roseum UAMH 7839 (D0FL93)
Manually annotated by BRENDA team
Hong, Y.J.; Tantillo, D.J.
Modes of inactivation of trichodiene synthase by a cyclopropane-containing farnesyldiphosphate analog
Org. Biomol. Chem.
7
4101-4109
2009
Fusarium sporotrichioides
Manually annotated by BRENDA team
Burkhardt, I.; Dickschat, J.S.
The absolute configuration of isochamigrene new insights into the cyclisation mechanism of trichodiene synthase
Chem. Commun. (Camb.)
54
3540-3542
2018
Fusarium sporotrichioides, Fusarium sporotrichioides DSM 62425
Manually annotated by BRENDA team