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. Author manuscript; available in PMC: 2021 Jan 1.
Published in final edited form as: Nat Chem Biol. 2019 Nov 25;16(1):87–94. doi: 10.1038/s41589-019-0402-7

Table 2 |.

Conversion of a range of substrates using NMN+ as the cycling cofactor

Substrate Product Enzyme Substrate concentrationa Conversion (%)
graphic file with name nihms-1634252-t0001.jpg graphic file with name nihms-1634252-t0002.jpg XenA 33 mM >99
graphic file with name nihms-1634252-t0003.jpg graphic file with name nihms-1634252-t0004.jpg XenA 10 mM 76 ± 2
graphic file with name nihms-1634252-t0005.jpg graphic file with name nihms-1634252-t0006.jpg XenA 50 mM 49 ± 3
graphic file with name nihms-1634252-t0007.jpg graphic file with name nihms-1634252-t0008.jpg OYE3 5 mM >99
graphic file with name nihms-1634252-t0009.jpg graphic file with name nihms-1634252-t0010.jpg NfsB 2 mM 92 ± 1
Cytochrome c (oxidized) Cytochrome c (reduced) P450 BM3 W1046S 50 μM >99

Reactions were preformed in 200 mM potassium phosphate buffer (pH 7.5), 1 M NaCl, 300 mM d-glucose, 6 mM NMN+, and substrates at 30 °C while mixing for 24 h. Bs GDH was supplied at 0.33 mg ml−1. XenA, OYE3, NsfB, and P450 BM3 W1046S were supplied at 0.75 mg ml−1. Values are an average of at least three replicates with values after ± represent one standard deviation.

a

Substrate concentration was limited by substrate solubility in the buffer.