Table 3.

Specific activities (nmol resorufin/min/nmol P450) of alkoxyresorufin O-dealkylation by CYP102A1 M11 mutants and wild-type CYP102A1

No.	Residue	Side chain
		Methyl	Ethyl	n-Propyl	n-Butyl	n-Pentyl	n-Hexyl	n-Heptyl	n-Octyl	Benzyl
Nonpolar side chain
1	Phe87	ND	ND	ND	ND	ND	0.11	0.16	0.060	0.29
2	Gly87	ND	ND	ND	1.01	3.80	2.59	0.74	0.14	4.02
3	Ala87	ND	0.16	1.53	4.37	11.05	1.83	0.34	0.10	3.79
4	Leu87	ND	ND	ND	ND	0.042	0.024	0.051	0.024	0.23
5	Ile87	ND	ND	ND	ND	0.35	0.010	0.062	ND	0.031
6	Val87a	ND	ND	0.75	1.08	1.64	0.42	0.11	0.068	5.43
7	Met87	ND	ND	ND	ND	ND	ND	ND	ND	ND
8	Pro87	–	–	–	–	–	–	–	–	–
9	Trp87	ND	ND	ND	ND	ND	ND	ND	ND	ND
Uncharged polar side chain
10	Ser87	–	–	–	–	–	–	–	–	–
11	Thr87	ND	ND	ND	0.12	ND	0.10	0.055	0.060	0.12
12	Asn87	ND	ND	ND	ND	ND	0.021	0.053	0.057	0.14
13	Gln87	ND	ND	ND	ND	ND	0.077	0.097	0.064	0.51
14	Tyr87	ND	0.024	0.13	0.14	0.55	0.076	0.017	0.031	0.92
15	Cys87	ND	ND	ND	ND	ND	0.026	ND	ND	ND
Charged polar side chain
16	Lys87	ND	ND	ND	ND	ND	ND	ND	ND	ND
17	Arg87	ND	ND	ND	ND	ND	0.013	0.010	0.028	0.038
18	His87	ND	ND	ND	ND	ND	0.046	0.022	0.046	ND
19	Asp87	–	–	–	–	–	–	–	–	–
20	Glu87	–	–	–	–	–	–	–	–	–
21	Wild type (Phe87)	ND	ND	ND	ND	ND	ND	0.17	0.18	ND

Specific activities observed with 20 µM alkoxyresorufin and 20 nM P450 BM3. THe values represent averages of three measurements, standard deviations were less than 10%

ND not detectable (less than 0.01 nmol/min/nmol P450)

^aCYP102A1 M11 containing R47L, E64G, F81I, F87V, E143G, L188Q, E267V, and G415S [22]