Cloning, expression, and characterization of an (R)-specific alcohol dehydrogenase fromLactobacillus kefir

Cloning and Overexpression of an NADH-Dependent Alcohol Dehydrogenase Gene fromCandida marisInvolved in (R)-Selective Reduction of 5-Acetylfuro[2,3-c]pyridine

“…The two enzymes have similar biochemical properties, (R)-specificity, and NAD-dependency for their reactions. The similarities of the deduced amino acid sequences of bacterial (R)-specific alcohol dehydrogenases isolated from Leifsonia sp., 8,12) Lactobacillus kefir, 6,11) and Lactobacillus brevis 5) were about 41.3%, 42.2%, and 38.9% respectively. The substrate specificities of the enzymes resembled those of AFPDH, even though they are tetrameric enzymes.…”

“…4) On the other hand, only a few enzymes follow the antiPrelog rule. 5) Several NADH-or NADPH-dependent (R)-specific alcohol dehydrogenases, from bacteria and NADPH-dependent ones from yeast have been purified, [5][6][7][8][9][10] and the genes of these enzymes have been cloned and sequenced, 5,11,12) but there have been no reports on the DNA sequence of an NADH-dependent highly enantioselective (R)-specific alcohol dehydrogenase from yeast.…”

Identification of ketone reductase ChKRED20 from the genome of Chryseobacterium sp. CA49 for highly efficient anti-Prelog reduction of 3,5-bis(trifluoromethyl)acetophenone

“…ChKRED20, predicted ketone reductase in this work, KC342020; LSADH, alcohol dehydrogenase from Leifsonia sp. S749, BAD99642 [31]; LK-ADH, R-specific alcohol dehydrogenase from Lactobacillus kefir, AAP94029 [28]; LB-RADH, R-specific alcohol dehydrogenase from Lactobacillus brevis, AJ544275 [32]; TtADH, alcohol dehydrogenase from Thermus thermophilus, 2D1Y [36]; CPADH, (S)-1-phenyl-1,2-ethanediol dehydrogenase from Candida parapsilosis, DQ675534 [29]. Gray shading indicates residues highly conserved in the SDR family.…”

“…Thus far, a few ketoreductases have been shown to catalyze asymmetric reductions that take place following the anti-Prelog's rule [25][26][27][28][29] and most of them were of bacterial origin. We evaluated a library of yeast strains preserved in the lab, and several were found to catalyze the bioreduction of 1a.…”

Characterization of a robust anti-Prelog short-chain dehydrogenase/reductase ChKRED20 from Chryseobacterium sp. CA49

“…The results indicated excellent adaptability of ChKRED20 under varied reaction conditions. The high tolerance against thermal treatment and pH variation compared well with the majority of SDRs from mesophilic microorganisms [30][31][32][33][34][35][36][37][38][39][40], which would be beneficial for large-scale application of this enzyme.…”