Studies on the distribution and regulation of microbial keto ester reductases

Peters, Jörg; Zelinski, Thomas; Kula, Maria‐Regina

doi:10.1007/bf00170082

Cited by 37 publications

(3 citation statements)

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“…Further biochemical assay demonstrated that Fusarium KivRFp could utilize NADPH and NADH as coenzyme, while the NADPH is preferred (Figure 5 B). In accordance to our results, bacterial chiral enzymes belonging to the D-ketoacid reductases superfamily also could utilize NADH as coenzyme, and also feature a conserved Arg-(Asp/Glu)-His active site triad [ 20 , 37 ]. Based on the phylogenetic, molecular, and biochemical analysis results, we propose that KivRFp is a new member of family ketonate oxidoreductases.…”

Section: Discussionsupporting

confidence: 86%

Cloning and characterization of a novel 2-ketoisovalerate reductase from the beauvericin producer Fusarium proliferatum LF061

et al. 2012

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BackgroundThe ketoisovalerate reductase (EC 1.2.7.7 ) is required for the formation of beauvericin via the nonribosomal peptide synthetase biosynthetic pathway. It catalyzes the NADPH-specific reduction of ketoisovaleric acid to hydroxyisovalerate. However, little is known about the bioinformatics’ data about the 2-Kiv reductase in Fusarium. To date, heterologous production of the gene KivRFp from Fusarium has not been achieved.ResultsThe KivRFp gene was subcloned and expressed in Escherichia coli BL21 using the pET expression system. The gene KivRFp contained a 1,359 bp open reading frame (ORF) encoding a polypeptide of 452 amino acids with a molecular mass of 52 kDa. Sequence analysis indicated that it showed 61% and 52% amino acid identities to ketoisovalerate reductase from Beauveria bassiana ATCC 7159 (ACI30654) and Metarhizium acridum CQMa 102 (EFY89891), respectively; and several conserved regions were identified, including the putative nucleotide-binding signature site, GXGXXG, a catalytic triad (Glu405, Asn184, and Lys285). The KivRFp exhibited the highest activity at 35°C and pH 7.5 respectively, by reduction of ketoisovalerate. It also exhibited the high level of stability over wide temperature and pH spectra and in the presence of metal ions or detergents.ConclusionsA new ketoisovalerate reductase KivRFp was identified and characterized from the depsipeptide-producing fungus F. proliferatum. KivRFp has been shown to have useful properties, such as moderate thermal stability and broad pH optima, and may serve as the starting points for future protein engineering and directed evolution, towards the goal of developing efficient enzyme for downstream biotechnological applications.

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Section: Discussionsupporting

confidence: 86%

Cloning and characterization of a novel 2-ketoisovalerate reductase from the beauvericin producer Fusarium proliferatum LF061

et al. 2012

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“…The FDH catalyzes the oxidation of formate into carbon dioxide, while reducing the oxidized form of the cofactor into its reduced form, NAD(P)H. The most widely applied FDH is probably the FDH from C. boidinii and optimized mutants thereof [191] developed in the Kula group who are --jointly with the Hummel and Wandrey groups --pioneers in the fi eld of FDH -based applications [192,193] in addition to the Whitesides group [194] . The Kula group also carried out preparative transformations based on these enzymes by coupling the ADH reduction reactions with FDH regeneration [198,199] . In addition, downstream processing is simplifi ed since (ideally) no organic by -product remains in the reaction mixture.…”

Section: Reduction Of Ketonesmentioning

confidence: 99%

Enzyme‐Catalyzed Asymmetric Synthesis

Gröger

2010

Catalytic Asymmetric Synthesis

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INTRODUCTIONBiocatalysis has been recognized over the past decades as a highly valuable tool for organic chemists to prepare enantiomerically pure molecules, so -called chiral building blocks, in a highly effi cient way. Besides a multitude of academic work, it is noteworthy that enzyme catalysis belongs to the standard repertoire in industry when facing challenging enantioselective synthetic routes. A broad range of biocatalytic methods is already in use in particular for large -scale manufacture of drug intermediates [1] .The research in the fi eld of enzyme catalysis has already been comprehensively reviewed some years ago [2] . Thus, the focus of the current review is on a selection of (particularly recently developed) enantioselective enzymatic reactions, which turned out to be highly useful and applicable in organic synthesis, fulfi lling criteria such as high productivity, substrate concentrations, conversions, and enantioselectivities. The presented methods are an interesting complementary tool to existing " classic organic " or " chemocatalytic asymmetric " methodologies. Among biocatalytic reactions, both resolution of racemates and asymmetric synthesis starting from prochiral substrates are attractive routes already applied, in part, in industry. A third type of biotechnological approach, which is not a subject of this review, are fermentation processes. A graphical summary of these three types of so -called " white biotechnology " methodologies is given in Scheme 6.1 .Hydrolases are the enzyme class most commonly applied as biocatalysts in organic chemistry. This is mainly due to the accessibility of these enzymes (used, e.g., in the textile and detergents industry), their suitability for transformations in organic media Catalytic Asymmetric Synthesis, Third Edition, Edited by Iwao Ojima 269 270 ENZYME-CATALYZED ASYMMETRIC SYNTHESIS (in particular when using lipases), and the lack of a need for cofactors. However, in recent years, we have also seen an increasing tendency to apply redox enzymes in organic syntheses as well as lyases in C -C bond formations and transferases. Isomerases also turned out to be very useful in particular in combination with hydrolases for dynamic kinetic resolutions. Thus, a broad range of biotransformations is available for organic chemists. A challenge, however, is the use of ATP cofactor -dependent enzymes, which contribute to only a negligible number of typical organic biotransformations (e.g., due to the high price of ATP).The fi eld of biocatalysis benefi ted signifi cantly from the tremendous progress in molecular biology. Highly effi cient methods for screening and optimization of biocatalysts (by, e.g., directed evolution in the latter case) have been developed, which allows access to tailor -made enzymes. Furthermore, the design of recombinant microorganisms gives access to highly productive whole -cell catalysts, which contain only the desired enzymes in large amount, thus signifi cantly reducing the required biomass for biotransformations compared with the use of...

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“…NAD-dependent coniferyl alcohol dehydrogenase (Jaeger et al, 1981 ;Jaeger, 1988), NAD\mycothiol-dependent for-maldehyde dehydrogenase (Eggeling & Sahm, 1984van Ophem et al, 1992 ;van Ophem & Duine, 1994 ;Misset-Smits et al, 1997) and methanol : N,Ndimethyl-4-nitrosoaniline (NDMA) oxidoreductase (MNO) from R. erythropolis DSM 1069 (van Ophem et al, 1993) ; MNO from R. rhodochrous LMD 89.129 (van Ophem et al, 1993) and from Rhodococcus sp. NI86\21 (Nagy et al, 1995), which has since been identified as R. erythropolis (de Schrijver et al, 1997) ; NAD-dependent propan-2-ol dehydrogenase from R. rhodochrous PNKb1 (Ashraf & Murrell, 1990, 1992 ; NADH-dependent carbonyl reductase from R. erythropolis DSM 743 (Peters et al, 1992(Peters et al, , 1993Zelinski et al, 1994) ; NAD-dependent long-chain secondary alcohol dehydrogenase from R. erythropolis ATCC 4277 (Ludwig et al, 1995) ; NAD-dependent secondary alcohol dehydrogenase from Rhodococcus sp. GK1 (Krier et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes The EMBL accession number for the sequence reported in this paper is P81747.

Schenkels

Duine

2000

Microbiology

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Extracts from benzyl-alcohol-grown Rhodococcus erythropolis DSM 1069 showed NAD(P)-independent, N,N-dimethyl-4-nitrosoaniline (NDMA)-dependent alcohol dehydrogenase activity. The enzyme exhibiting this activity was purified to homogeneity and characterized. It appears to be a typical nicotinoprotein as it contains tightly bound NADH acting as cofactor instead of coenzyme. Other characteristics indicate that it is highly similar to the known nicotinoprotein alcohol dehydrogenase (np-ADH) from Amycolatopsis methanolica : it is a homotetramer of 150 kDa ; N-terminal amino acid sequencing (22 residues) showed that 77 % of these amino acids are identical in the two enzymes ; it has optimal activity at pH 70 ; it lacks NAD(P)Hdependent aldehyde reductase activity ; it catalyses the oxidation of a broad range of (preferably) primary and secondary alcohols, either aliphatic or aromatic, and formaldehyde, with the concomitant reduction of the artificial electron acceptor NDMA. NDMA could be replaced by an aldehyde, but not formaldehyde, the substrate specificity of the enzyme for the aldehydes reflecting that for the corresponding alcohols. The latter also applied to the low aldehyde dismutase activity displayed by the enzyme. From this, together with the results of the induction studies, it is concluded that np-ADH functions as the main alcohol-oxidizing enzyme in the dissimilation of many, but not all, alcohols by R. erythropolis and may also catalyse coenzyme-independent interconversion of alcohols and aldehydes under certain circumstances. It is anticipated that the enzyme may be of even wider significance since structural data indicate that np-ADH is also present in other (nocardioform) actinomycetes.

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Studies on the distribution and regulation of microbial keto ester reductases

Cited by 37 publications

References 42 publications

Cloning and characterization of a novel 2-ketoisovalerate reductase from the beauvericin producer Fusarium proliferatum LF061

Cloning and characterization of a novel 2-ketoisovalerate reductase from the beauvericin producer Fusarium proliferatum LF061

Enzyme‐Catalyzed Asymmetric Synthesis

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