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

Kawano, Shohei; Yano, Miho; Hasegawa, Junzo; Yasohara, Yoshihiko

doi:10.1271/bbb.110453

Cited by 6 publications

(2 citation statements)

References 25 publications

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“…The third step in alkane degradation involves the conversion of the primary alcohol to its corresponding aldehyde then followed by conversion of the aldehyde to fatty acid, which are carried out by alcohol dehydrogenases (ADHs) and aldehyde dehydrogenases (ALDHs), respectively (Ludwig et al ., 1995; Ishige et al ., 2000; Peng et al ., 2006; Palma‐Gutierrez et al ., 2008; Liu et al ., 2009; Kawano et al ., 2011). We identified eight ADHs homologues and five ALDHs homologues in DQ12‐45‐1b genome through multiple sequence alignment or phylogenetic analysis of ADH or ALDH related homologues from alkane‐degrading bacteria (Supporting Information Figs.…”

Section: Resultsmentioning

confidence: 99%

Comparative transcriptome analysis reveals different adaptation mechanisms for degradation of very long‐chain and normal long‐chain alkanes in Dietzia sp. DQ12‐45‐1b

Tang

Nie

et al. 2022

Environmental Microbiology

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Hydrocarbon-degrading bacteria typically metabolize a broad range of alkane substrates, but global metabolic characteristics of strains growing on alkane substrates in different chain lengths remain unclear. In this study, we analysed the transcriptional profiles of a hydrocarbon degrading bacterium, Dietzia sp. DQ12-45-1b, during growth on octacosane (C28), hexadecane (C16) and glucose as the sole carbon sources. Our results highlight that C16 and C28 induced common genes of core alkane degradation pathways in DQ12-45-1b, whereas transcriptional patterns of genes related to lipid metabolism, energy metabolism, biomass synthesis, and metal ion transportation were distinct. In addition, the transcriptional differences of genes related to glyoxylate shunt (GS) as well as growth phenotypes of mutant strain with defects in GS demonstrated that GS is essential for C16 degradation, though it is dispensable for C28 degradation in DQ12-45-1b. These results demonstrate that DQ12-45-1b cells exhibited considerable metabolic flexibility by using various mechanisms during growth on alkane substrates in different chain lengths. This study advances our knowledge of microbial hydrocarbon degradation and provides valuable information for the application of alkanedegrading bacteria in bioremediation and microbial enhanced oil recovery.

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Section: Resultsmentioning

confidence: 99%

Comparative transcriptome analysis reveals different adaptation mechanisms for degradation of very long‐chain and normal long‐chain alkanes in Dietzia sp. DQ12‐45‐1b

Tang

Nie

et al. 2022

Environmental Microbiology

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“…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.…”

Section: Isolation Of Chryseobacterium Sp Ca49 and Its Characteristicsmentioning

confidence: 99%

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

Liu

Tang

Pei

et al. 2014

Journal of Molecular Catalysis B: Enzymatic

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Stairway to Stereoisomers: Engineering Short‐ and Medium‐Chain Ketoreductases To Produce Chiral Alcohols

Shanbhag

2023

ChemBioChem

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The short-and medium-chain dehydrogenase/reductase superfamilies are responsible for most chiral alcohol production in laboratories and industries. In nature, they participate in diverse roles such as detoxification, housekeeping, secondary metabolite production, and catalysis of several chemicals with commercial and environmental significance. As a result, they are used in industries to create biopolymers, active pharmaceutical intermediates (APIs), and are also used as components of modular enzymes like polyketide synthases for fabricating bioactive molecules. Consequently, random, semi-rational and rational engineering have helped transform these enzymes into product-oriented efficient catalysts. The rise of newer synthetic chemicals and their enantiopure counterparts has proved challenging, and engineering them has been the subject of numerous studies. However, they are frequently limited to the synthesis of a single chiral alcohol. The study attempts to defragment and describe hotspots of engineering short-and medium-chain dehydrogenases/reductases for the production of chiral synthons.

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

Cited by 6 publications

References 25 publications

Comparative transcriptome analysis reveals different adaptation mechanisms for degradation of very long‐chain and normal long‐chain alkanes in Dietzia sp. DQ12‐45‐1b

Comparative transcriptome analysis reveals different adaptation mechanisms for degradation of very long‐chain and normal long‐chain alkanes in Dietzia sp. DQ12‐45‐1b

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

Stairway to Stereoisomers: Engineering Short‐ and Medium‐Chain Ketoreductases To Produce Chiral Alcohols

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