Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

4.2.3.6: trichodiene synthase

This is an abbreviated version!
For detailed information about trichodiene synthase, go to the full flat file.

Word Map on EC 4.2.3.6

Reaction

(2E,6E)-farnesyl diphosphate
=
trichodiene
 +
diphosphate

Synonyms

EC 4.1.99.6, sesquiterpene cyclase, synthase, trichodiene, TDN synthase, trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase, tri5, trichodiene synthase, trichodiene synthetase

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.6 trichodiene synthase

Engineering

Engineering 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.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C146A
-
complete loss of activity
C190A
-
significantly reduced enzymatic activity
D100E
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
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
D109E
-
the mutant with increased activity shows more stability than the wild type enzyme, an increased number of electrostatic interactions and better binding energies with the ligand
D109E/D248Y
-
the mutant with increased activity shows more stability than the wild type enzyme, an increased number of electrostatic interactions and better binding energies with the ligand
D248Y
-
the mutant with increased activity shows more stability than the wild type enzyme, an increased number of electrostatic interactions and better binding energies with the ligand
additional information