Table 2.

Nicotinamide‐free isomerization of 1 a and 2 a to 1 b and 2 b catalyzed by OYEs.^[a]

Entry	Substrate	Protein	Concentration [μm]	Conv. [%]
1	1 a	OYE2‐wt	2.8	45
2	1 a	OYE2‐wt[b]	2.8	13
3	1 a	OYE3‐wt[c]	2.8	35
4	1 a	OYE2‐H192A	2.8	40
5	1 a	OYE2‐Y197F	2.8	<1
6	1 a	OYE2‐Y197F[d]	741	30
7	1 a	BSA	600	<1
8	1 a	OYE2 denatured[e]	2.8	<1
9	2 a	OYE2‐wt	2.8	49[f]
10	2 a	OYE2‐H192A	2.8	25
11	2 a	OYE2‐Y197F	2.8	15[g]

[a] Tris‐HCl buffer (50 mm, pH 7.5), 2 h reaction time; wt=wild type. [b] pH 6. [c] 24 h reaction time. [d] Corresponds to TTN of approximately 4 (3 mm 1 b). [e] Denaturation procedure: OYE2 sample was heated to 95 °C for 10 min, allowed to cool down, and used in the reaction as such. [f] No trace of 2 a. [g] Control (no enzyme) also showed 15 % of 2 b.