4.2.1.129: squalene-hopanol cyclase
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For detailed information about squalene-hopanol cyclase, go to the full flat file.
Reaction
Synonyms
SHC, squalene-hopene cyclase
ECTree
4.2.1.129 squalene-hopanol cyclaseAdvanced search results
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results (Engineering
Engineering on EC 4.2.1.129 - squalene-hopanol cyclase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C435S/D374I/D374V/H451F
site-directed mutagenesis, inactive mutant
D377C/D377N/Y612A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
D377E/D376Q/D376R/D377R/E45K/W406V/W417A/D377C
site-directed mutagenesis, inactive mutant
E45A
-
production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
E93A
-
production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
F365A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F434A
-
production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
F437A
-
production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
F601A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F605A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
G262A
-
the mutant produces hopanol as the main product instead of hop-22(29)-ene. The mutant also produces hop-21(22)ene
I261A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
P263A
P263G
Q262A
-
the mutation results in a greatly enhanced production of hopanol along with the decreased formation of hopene. A high production of hopanol would be explained as follows. The point mutations could give rise to the perturbation around the front water. This disordered front water cannot correctly act as the catalytic base for the deprotonation reaction to form hopene, and in turn could be placed near to the final hopanyl cation, leading to a high production of hopanol without forming hopene
Q262G
Q262G/Q262A/P263G/P263A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
R127Q
-
production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
T41A
-
production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
V381A/D376C
site-directed mutagenesis, inactive mutant
W133A
-
production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
W169F/W169H/W489A/F605K
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y267A
-
production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
Y420A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y606A/W23V/W495V/W522V/W533A/W591L/W78S/E35Q/E197Q/D530N/T378A
site-directed mutagenesis, the mutant shows the same product pattern and activity as the wild-type
Y609A/Y612A/L607K
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y609F
Y612F/D376E/D376G/D377E/D377G/D377Q/E45A/E45D/F365W/T41A/E93A/R127Q/W133A/Y267A/F434A/F437A/W258L/D350N/D421N/D442N/H451R/D447N/D377N/D313N/E535Q/D374E
site-directed mutagenesis, the mutant shows the same product pattern as the wild-type with less enzyme activity
P263A
-
the mutant produces hopanol as the main product instead of hop-22(29)-ene. The mutant also produces hop-21(22)ene
P263A
-
the mutation results in a greatly enhanced production of hopanol along with the decreased formation of hopene. A high production of hopanol would be explained as follows. The point mutations could give rise to the perturbation around the front water. This disordered front water cannot correctly act as the catalytic base for the deprotonation reaction to form hopene, and in turn could be placed near to the final hopanyl cation, leading to a high production of hopanol without forming hopene
P263G
-
the mutant produces hopanol as the main product instead of hop-22(29)-ene. The mutant also produces hop-21(22)ene
P263G
-
the mutation results in a greatly enhanced production of hopanol along with the decreased formation of hopene. A high production of hopanol would be explained as follows. The point mutations could give rise to the perturbation around the front water. This disordered front water cannot correctly act as the catalytic base for the deprotonation reaction to form hopene, and in turn could be placed near to the final hopanyl cation, leading to a high production of hopanol without forming hopene
Q262G
-
the mutant produces hopanol as the main product instead of hop-22(29)-ene. The mutant also produces hop-21(22)ene
Q262G
-
the mutation results in a greatly enhanced production of hopanol along with the decreased formation of hopene. A high production of hopanol would be explained as follows. The point mutations could give rise to the perturbation around the front water. This disordered front water cannot correctly act as the catalytic base for the deprotonation reaction to form hopene, and in turn could be placed near to the final hopanyl cation, leading to a high production of hopanol without forming hopene
Y609F
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y609F
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview. The phenotype of Y609F mutein is contrarily described in two publications
