. 2010 Jul 30;192(19):5220–5227. doi: 10.1128/JB.00723-10

TABLE 3.

Oxygenation specificity of StyA1 and other styrene monooxygenases

Substrate/product	Specific oxygenase activity in U mg⁻¹ (relative activity %) and, if determined, % enantiomeric excess (preferred enantiomer) for indicated oxygenase and reductase^b
Substrate/product	StyA1 of R. opacus 1CP and StyA2B of R. opacus 1CP^a^,^c	StyA2B of R. opacus 1CP and StyA2B of R. opacus 1CP^c	StyA1 + StyA2B of R. opacus 1CP and StyA2B of R. opacus 1CP^c	StyA of Pseudomonas sp. VLB120 and electrochemical FAD reduction^d	Unknown SMO, metagenome, and PheA2 of Geobacillus thermoglucosidasius^e
Styrene/styrene oxide	0.214 (100) >96 (S)	0.019 (100) >94 (S)	0.233 (100) >94 (S)	0.204 (100) 98 (S)	0.80 (100) >99 (S)
2-Chlorostyrene/2-chlorostyrene oxide	<0.001 (<0.1)	0.007 (37)	0.007 (3)	ND	ND
3-Chlorostyrene/3-chlorostyrene oxide	0.162 (76)	0.044 (232)	0.206 (88)	ND	ND
4-Chlorostyrene/4-chlorostyrene oxide	0.078 (36)	0.011 (58) >82	0.089 (38)	0.312 (153) 98	0.23 (29) >99 (S)
4-Methylstyrene/4-methylstyrene oxide	0.102 (48)	0.006 (32)	0.108 (46)	0.312 (153)	ND
Dihydronaphthalene/dihydronaphthalene oxide	0.171 (80)	0.011 (58)	0.182 (78)	0.376 (184) 99	ND
Methylphenylsulfide/methylphenylsulfoxide	0.325 (152)	0.012 (63)	0.337 (145)	0.226 (111) 26	0.11 (14) 75 (R)

Values for StyA1 were obtained from total activities of StyA1/StyA2B by subtracting oxygenation rates of StyA2B.

ND, not determined.

This study and reference 40.

Reference 17. A maximum activity of 2.1 U mg⁻¹ for the recombinant StyA/StyB system was reported later (27).

Reference 45.