NADH oxidase from Lactobacillus brevis: a new catalyst for the regeneration of NAD

Geueke, Birgit; Riebel, Bettina R.; Hummel, Werner

doi:10.1016/s0141-0229(02)00290-9

Cited by 130 publications

(77 citation statements)

References 24 publications

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“…1). To this end, we employ a mixture of both an NAD þ -utilizing wild-type (WT) PDH (PDH NADH ), a mutant PDH that utilizes NADP þ (PDH NADPH ), and a water-generating NADH oxidase (NoxE) that specifically oxidizes NADH, but not NADPH 31,32 . By employing this metabolic node, we generate NADPH needed for PHB production from pyruvate, but also dissipate excess reducing equivalents in an autoregulatory manner.…”

Section: Resultsmentioning

confidence: 99%

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A synthetic biochemistry molecular purge valve module that maintains redox balance

2014

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Section: Resultsmentioning

confidence: 99%

“…We chose NoxE from Lactococcus lactis as it is a water-forming NADH oxidase so it does not generate any toxic products such as hydrogen peroxide 31,32,35 . As shown in Table 1, the K cat of NoxE is 248.8 times greater with NADH than NADPH and k cat /K m is 9,900 times greater.…”

Section: Gtx-nadphmentioning

confidence: 99%

A synthetic biochemistry molecular purge valve module that maintains redox balance

2014

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“…Although there is no experimental evidence of O 2 -dependent NADH oxidase activity in L. casei, the inspection of the available genome sequence of L. casei BL23 shows that this organism encodes at least three putative NADH oxidases (data not shown). Furthermore, there is evidence of the involvement of NADH oxidases in NAD ϩ regeneration in other lactobacilli (13,23).…”

Section: Discussionmentioning

confidence: 99%

Identification of a Gene Cluster EnablingLactobacillus caseiBL23 To Utilizemyo-Inositol

Yebra¹,

Zúñiga²,

Beaufils

et al. 2007

Appl Environ Microbiol

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Genome analysis of Lactobacillus casei BL23 revealed that, compared to L. casei ATCC 334, it carries a 12.8-kb DNA insertion containing genes involved in the catabolism of the cyclic polyol myo-inositol (MI). Indeed, L. casei ATCC 334 does not ferment MI, whereas strain BL23 is able to utilize this carbon source. The inserted DNA consists of an iolR gene encoding a DeoR family transcriptional repressor and a divergently transcribed iolTABCDG1G2EJK operon, encoding a complete MI catabolic pathway, in which the iolK gene probably codes for a malonate semialdehyde decarboxylase. The presence of iolK suggests that L. casei has two alternative pathways for the metabolism of malonic semialdehyde: (i) the classical MI catabolic pathway in which IolA (malonate semialdehyde dehydrogenase) catalyzes the formation of acetyl-coenzyme A from malonic semialdehyde and (ii) the conversion of malonic semialdehyde to acetaldehyde catalyzed by the product of iolK. The function of the iol genes was verified by the disruption of iolA, iolT, and iolD, which provided MI-negative strains. By contrast, the disruption of iolK resulted in a strain with no obvious defect in MI utilization. Transcriptional analyses conducted with different mutant strains showed that the iolTABCDG1G2EJK cluster is regulated by substrate-specific induction mediated by the inactivation of the transcriptional repressor IolR and by carbon catabolite repression mediated by the catabolite control protein A (CcpA). This is the first example of an operon for MI utilization in lactic acid bacteria and illustrates the versatility of carbohydrate utilization in L. casei BL23.myo-Inositol (MI) is the most abundant stereoisomer of inositol (1,2,3,4,5,6-cyclohexanehexol). It is common in soils, and it is a constituent of phytic acid (inositol hexaphosphate), which in the form of various salts (phytates) provides a major phosphate storage molecule in plant seeds. Several microorganisms, mostly inhabitants of soil, can utilize MI as a carbon source. For bacteria, the MI catabolic pathway has been elucidated for Enterobacter aerogenes (formerly Aerobacter aerogenes) (3). MI is important for the establishment of symbiosis in legume nodules. The metabolism of MI in Sinorhizobium fredii and Rhizobium leguminosarum is required for efficient nitrogen fixation and nodulation of soybeans (9, 15). MI dehydrogenase genes (e.g., iolG) and inosose dehydratase genes (iolE) have been characterized in S. fredii and Sinorhizobium meliloti (10, 15, 36), and iolA and iolDEB genes have been studied in R. leguminosarum (9). An MI utilization gene cluster has also been described for Clostridium perfringens, which was induced by MI via the IolR regulator (16), and recently, transcriptome analysis permitted the identification of an iol cluster which allowed the rapid growth of Corynebacterium glutamicum on MI (19). However, the first MI catabolic gene cluster was characterized in Bacillus subtilis, and detailed molecular data are available only for this bacterium. The B. subtilis iolRS and iolABC...

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“…No reagents or by-products of the regeneration/substitution step should interfere with product isolation, and they should be compatible with the rest of the reaction system. In the literature, several enzyme-coupled (Geueke et al 2003;Riebel et al 2002Riebel et al , 2003Seelbach et al 1996) and substrate-coupled (Kroutil et al 2004b;Mertens et al 2003;Schumacher et al 2006;Stampfer et al 2002) cofactor regeneration systems are described. There are some disadvantages using an enzyme-coupled regeneration system: costs for a second enzyme and a co-substrate, interferences during product purification caused by secondary products, and reaction conditions have to be optimized for both enzyme reactions.…”

Section: Discussionmentioning

confidence: 99%

Immobilized redox mediators for electrochemical NAD(P)+ regeneration

Kochius

Magnusson

Hollmann

et al. 2012

Appl Microbiol Biotechnol

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The applicability of dissolved redox mediators for NAD(P) + regeneration has been demonstrated several times. Nevertheless, the use of mediators in solutions for sensor applications is not a very convenient strategy since the analysis is not reagentless and long stabilization times occur. The most important drawbacks of dissolved mediators in biocatalytic applications are interferences during product purification, limited reusability of the mediators, and their cost-intensive elimination from wastewater. Therefore, the use of immobilized mediators has both economic and ecological advantages. This work critically reviews the current stateof-art of immobilized redox mediators for electrochemical NAD(P) + regeneration. Various surface modification techniques, such as adsorption polymerization and covalent linkage, as well as the corresponding NAD(P) + regeneration rates and the operational stability of the immobilized mediator films, will be discussed. By comparison with other existing regeneration systems, the technical potential and future perspectives of biocatalytic redox reactions based on electrochemically fed immobilized mediators will be assessed.

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NADH oxidase from Lactobacillus brevis: a new catalyst for the regeneration of NAD

Cited by 130 publications

References 24 publications

A synthetic biochemistry molecular purge valve module that maintains redox balance

A synthetic biochemistry molecular purge valve module that maintains redox balance

Identification of a Gene Cluster EnablingLactobacillus caseiBL23 To Utilizemyo-Inositol

Immobilized redox mediators for electrochemical NAD(P)+ regeneration

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