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. 2024 Feb 8;4(2):411–418. doi: 10.1021/jacsau.3c00814

Table 1. Screening of ADHs Utilizing 1a as the Model Substratea.

graphic file with name au3c00814_0005.jpg

entry enzyme sources types 2a [%] 3a [%] ee [%] configuration of 2a
1 ADH-R1 Burkholderia gladioli SDR 94.3 ± 3.1 3.0 ± 0.8 80.4 ± 0.8 S
2 ADH-R2 Ralstonia sp. SDR 92.4 ± 2.5 1.9 ± 0.9 99.9 ± 0.1 S
3 ADH-R3 Lactobacillus kefiri SDR 47.7 ± 0.3 1.6 ± 0.3 70.1 ± 0.7 S
4 ADH-R4 Oenococcus alcoholitolerans SDR 87.5 ± 0.7 11.4 ± 1.8 99.4 ± 0.2 S
5 ADH-R5 Zymomonas mobilis MDR 87.9 ± 1.8 2.9 ± 0.4 88.3 ± 0.0 R
6 ADH-R6 Parageobacillus thermoglucosidasius MDR 90.6 ± 1.8 2.6 ± 0.4 92.5 ± 1.5 R
7 ADH-R7 Thermus thermophilus SDR 95.4 ± 0.3 3.7 ± 0.3 99.9 ± 0.1 R
8 ADH-R8 Rhodopseudomonas palustris MDR 93.5 ± 1.4 2.9 ± 0.6 95.5 ± 5.4 R
9 ADH-R9 Rhizobium etli MDR 96.7 ± 1.2 2.9 ± 1.0 99.4 ± 0.1 R
10 ADH-R10 Pseudomonas meliae MDR 95.5 ± 0.9 4.3 ± 0.9 99.9 ± 0.1 R
a

Reaction conditions: 1a (10 mM), NADP+ (1 mM), glucose (20 mM), glutamate dehydrogenase (GDH) (2.5 mg mL–1), ADHs (0.1 g mL–1 of whole cell with 6 units mL–1 of DNaseI and 1 mg mL–1 of lysozyme), DMSO (5% v/v) in NaPi buffer (pH 7.4, 50 mM), at 30 °C, 800 rpm. Total volume: 1 mL.