Structures of Alcohol Dehydrogenases from Ralstonia and Sphingobium spp. Reveal the Molecular Basis for Their Recognition of ‘Bulky–Bulky’ Ketones

Man, H.; Kędziora, Kinga; Kulig, Justyna; Frank, Albin; Lavandera, Iván; Gotor‐Fernández, Vicente; Rother, Dörte; Hart, Sam; Turkenburg, J.P.; Grogan, Gideon

doi:10.1007/s11244-013-0191-2

Cited by 52 publications

(47 citation statements)

References 39 publications

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“…Nevertheless, the other alcohol dehydrogenases (ADH1-ADH5, and ADH8) in L . reuteri are more likely to play a role in ethanol transformation as reported in other microorganisms [33]. …”

Section: Resultsmentioning

confidence: 97%

Redox Balance in Lactobacillus reuteri DSM20016: Roles of Iron-Dependent Alcohol Dehydrogenases in Glucose/ Glycerol Metabolism

et al. 2016

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Lactobacillus reuteri, a heterofermentative bacterium, metabolizes glycerol via a Pdu (propanediol-utilization) pathway involving dehydration to 3-hydroxypropionaldehyde (3-HPA) followed by reduction to 1,3-propandiol (1,3-PDO) with concomitant generation of an oxidized cofactor, NAD+ that is utilized to maintain cofactor balance required for glucose metabolism and even for oxidation of 3-HPA by a Pdu oxidative branch to 3-hydroxypropionic acid (3-HP). The Pdu pathway is operative inside Pdu microcompartment that encapsulates different enzymes and cofactors involved in metabolizing glycerol or 1,2-propanediol, and protects the cells from the toxic effect of the aldehyde intermediate. Since L. reuteri excretes high amounts of 3-HPA outside the microcompartment, the organism is likely to have alternative alcohol dehydrogenase(s) in the cytoplasm for transformation of the aldehyde. In this study, diversity of alcohol dehydrogenases in Lactobacillus species was investigated with a focus on L. reuteri. Nine ADH enzymes were found in L. reuteri DSM20016, out of which 3 (PduQ, ADH6 and ADH7) belong to the group of iron-dependent enzymes that are known to transform aldehydes/ketones to alcohols. L. reuteri mutants were generated in which the three ADHs were deleted individually. The lagging growth phenotype of these deletion mutants revealed that limited NAD+/NADH recycling could be restricting their growth in the absence of ADHs. Notably, it was demonstrated that PduQ is more active in generating NAD+ during glycerol metabolism within the microcompartment by resting cells, while ADH7 functions to balance NAD+/NADH by converting 3-HPA to 1,3-PDO outside the microcompartment in the growing cells. Moreover, evaluation of ADH6 deletion mutant showed strong decrease in ethanol level, supporting the role of this bifuctional alcohol/aldehyde dehydrogenase in ethanol production. To the best of our knowledge, this is the first report revealing both internal and external recycling for cofactor homeostasis during 3-HPA conversion in L. reuteri.

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“…Nevertheless, the other alcohol dehydrogenases (ADH1-ADH5, and ADH8) in L . reuteri are more likely to play a role in ethanol transformation as reported in other microorganisms [33]. …”

Section: Resultsmentioning

confidence: 97%

Redox Balance in Lactobacillus reuteri DSM20016: Roles of Iron-Dependent Alcohol Dehydrogenases in Glucose/ Glycerol Metabolism

et al. 2016

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“…In comparing the results collected for the two recombinant ADHs it is clear that the ADH from Sphingobium yanoikuyae [20,21] did not accept -oxo ester 2 as a substrate (Table 1, Entry 2). Conversely, the ADH from Ralstonia sp.…”

Section: Resultsmentioning

confidence: 99%

Enantioselective Reduction of Ethyl 3‐Oxo‐5‐phenylpentanoate with Whole‐Cell Biocatalysts

et al. 2016

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“…DSM6428 22 (PDB: 4BMS). It also shared 90% similarity with one predicted protein from Chryseobacterium hispalense (NCBI accession no.…”

Section: Resultsmentioning

confidence: 99%

Synthesis of enantiopure glycidol derivatives via a one-pot two-step enzymatic cascade

Liu

2015

Org. Biomol. Chem.

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Styrene monooxygenase (SMO) can catalyze the kinetic resolution of secondary allylic alcohols to provide enantiopure glycidol derivatives. To overcome the low theoretical yield of kinetic resolution, we designed a one-pot two-step enzymatic cascade using prochiral α,β-unsaturated ketones as the substrates. An S-specific ketoreductase ChKRED03 was screened for the efficient bioreduction of the substrates to provide (S)-allylic alcohols, which underwent SMO-catalyzed epoxidation to achieve glycidol derivatives with contiguous stereogenic centers. Excellent enantioselectivity (ee > 99%) and diastereoselectivity (de > 99%) were achieved for the majority of the substrates, and product yields reached up to >99%.

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Structures of Alcohol Dehydrogenases from Ralstonia and Sphingobium spp. Reveal the Molecular Basis for Their Recognition of ‘Bulky–Bulky’ Ketones

Cited by 52 publications

References 39 publications

Redox Balance in Lactobacillus reuteri DSM20016: Roles of Iron-Dependent Alcohol Dehydrogenases in Glucose/ Glycerol Metabolism

Redox Balance in Lactobacillus reuteri DSM20016: Roles of Iron-Dependent Alcohol Dehydrogenases in Glucose/ Glycerol Metabolism

Enantioselective Reduction of Ethyl 3‐Oxo‐5‐phenylpentanoate with Whole‐Cell Biocatalysts

Synthesis of enantiopure glycidol derivatives via a one-pot two-step enzymatic cascade

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