Evolved CYP102A1 (P450BM3) variants oxidise a range of non-natural substrates and offer new selectivity options.
The evolution of CYP102A1 variants with enhanced activity and altered specificity characteristics.
Main Authors: | Whitehouse, C, Bell, S, Tufton, H, Kenny, R, Ogilvie, L, Wong, L |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2008
|
Similar Items
-
Evolved CYP102A1 (P450BM3) variants oxidise a range of non-natural substrates and offer new selectivity options.
by: Whitehouse, C, et al.
Published: (2008) -
Structure, electronic properties and catalytic behaviour of an activity-enhancing CYP102A1 (P450(BM3)) variant.
by: Whitehouse, C, et al.
Published: (2011) -
P450(BM3) (CYP102A1): connecting the dots.
by: Whitehouse, C, et al.
Published: (2012) -
Desaturation of alkylbenzenes by cytochrome P450(BM3) (CYP102A1).
by: Whitehouse, C, et al.
Published: (2008) -
Dearomatisation of o-xylene by P450BM3 (CYP102A1).
by: Whitehouse, C, et al.
Published: (2011)