Utilization of
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            -Lactate as an Energy Source Supports the Growth of Gluconobacter oxydans

Sheng, Binbin; Xu, Jun; Zhang, Y.; Jiang, Tianyi; Deng, Sisi; Kong, Jing; Gao, Chao; Ma, Cuiqing; Xu, Ping

doi:10.1128/aem.00527-15

Cited by 20 publications

(23 citation statements)

References 46 publications

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“…The results showed that most proteins contained a membrane‐associated sequence (Figure S1). Actually, only two soluble d ‐iLDHs, DLD3 in Saccharomyces cerevisiae and GOX2071 in Gluconobacter oxydans , have been characterized previously. Other reported soluble d ‐iLDHs have been shown to exist in the crude extracts of lactic acid bacteria (LAB) .…”

Section: Methodsmentioning

confidence: 99%

“…The results showed that most proteins contained am embrane-associated sequence ( Figure S1). Actually,o nly two soluble d-iLDHs, DLD3 in Saccharomyces cerevisiae [20] and GOX2071 in Gluconobactero xydans, [21] have been characterized previously.O ther reported soluble d-iLDHs have been shown to exist in the crude extractso fl actic acid bacteria (LAB). [22] Analysis of these two soluble d-iLDHs in the Pfam database indicatedthat they shared asimilar sequence feature, whichcontained only an FAD-binding domain at the Nt erminus and an FAD-oxidased omain at the Ct erminus.…”

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confidence: 99%

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Enzymatic Resolution by a d‐Lactate Oxidase Catalyzed Reaction for (S)‐2‐Hydroxycarboxylic Acids

Sheng

Zhang

et al. 2016

ChemCatChem

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Oxidase‐catalyzed kinetic resolution is important for the production of enantiopure 2‐hydroxycarboxylic acids (2‐HAs), which are versatile building blocks for the synthesis of many significant compounds. However, in contrast to that of (R)‐2‐HAs, the production of (S)‐2‐HA is challenging because of the lack of related oxidases. Herein, suitable enzymes were screened systematically through the analysis of numerous putative d‐lactate oxidase sequences and identification of several required properties. Finally, a d‐lactate oxidase from Gluconobacter oxydans 621H with advantageous characteristics, such as good solubility, broad substrate spectrum, and high stereoselectivity, was selected to resolve 2‐HAs into (S)‐2‐HAs. A variety of (S)‐2‐HAs was produced successfully using this d‐lactate oxidase with excellent enantiomeric excess values (>99 %). The presented screening criteria and approach for target biocatalysis suggested a guideline for the production of optically active chemicals such as (S)‐2‐HAs.

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

Enzymatic Resolution by a d‐Lactate Oxidase Catalyzed Reaction for (S)‐2‐Hydroxycarboxylic Acids

Sheng

Zhang

et al. 2016

ChemCatChem

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“…Most D-iLDHs belong to the flavin adenine dinucleotide (FAD)-binding oxidoreductase/transferase type 4 family, use FAD instead of FMN as the cofactor, and use quinones or cytochrome c as electron acceptors (7,14,15). However, there have been continual reports of novel types of both L-iLDHs and D-iLDHs in recent years (16)(17)(18)(19). The discovery of these novel enzymes further expands our knowledge of microbial lactate utilization, and detailed characterizations of the enzymes will be helpful in understanding the detailed mechanisms underlying these processes.…”

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confidence: 99%

A Bacterial Multidomain NAD-Independent d -Lactate Dehydrogenase Utilizes Flavin Adenine Dinucleotide and Fe-S Clusters as Cofactors and Quinone as an Electron Acceptor for d -Lactate Oxidization

et al. 2017

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Bacterial membrane-associated NAD-independent d-lactate dehydrogenase (Fe-S d-iLDH) oxidizes d-lactate into pyruvate. A sequence analysis of the enzyme reveals that it contains an Fe-S oxidoreductase domain in addition to a flavin adenine dinucleotide (FAD)-containing dehydrogenase domain, which differs from other typical d-iLDHs. Fe-S d-iLDH from KT2440 was purified as a His-tagged protein and characterized in detail. This monomeric enzyme exhibited activities with l-lactate and several d-2-hydroxyacids. Quinone was shown to be the preferred electron acceptor of the enzyme. The two domains of the enzyme were then heterologously expressed and purified separately. The Fe-S cluster-binding motifs predicted by sequence alignment were preliminarily verified by site-directed mutagenesis of the Fe-S oxidoreductase domain. The FAD-containing dehydrogenase domain retained 2-hydroxyacid-oxidizing activity, although it decreased compared to the full Fe-S d-iLDH. Compared to the intact enzyme, the FAD-containing dehydrogenase domain showed increased catalytic efficiency with cytochrome as the electron acceptor, but it completely lost the ability to use coenzyme Q Additionally, the FAD-containing dehydrogenase domain was no longer associated with the cell membrane, and it could not support the utilization of d-lactate as a carbon source. Based on the results obtained, we conclude that the Fe-S oxidoreductase domain functions as an electron transfer component to facilitate the utilization of quinone as an electron acceptor by Fe-S d-iLDH, and it helps the enzyme associate with the cell membrane. These functions make the Fe-S oxidoreductase domain crucial for the d-lactate utilization function of Fe-S d-iLDH. Lactate metabolism plays versatile roles in most domains of life. Lactate utilization processes depend on certain enzymes to oxidize lactate to pyruvate. In recent years, novel bacterial lactate-oxidizing enzymes have been continually reported, including the unique NAD-independent d-lactate dehydrogenase that contains an Fe-S oxidoreductase domain besides the typical flavin-containing domain (Fe-S d-iLDH). Although Fe-S d-iLDH is widely distributed among bacterial species, the investigation of it is insufficient. Fe-S d-iLDH from KT2440, which is the major d-lactate-oxidizing enzyme for the strain, might be a representative of this type of enzyme. A study of it will be helpful in understanding the detailed mechanisms underlying the lactate utilization processes.

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“…The common NADH-oxidation pathway in Gluconobacter oxydans involves pyruvate oxidation to acetyl-coenzyme A (CoA), followed by: 1) CoA entry into the TCA cycle, which provides carbon and energy resources for bacterial growth; or 2) accumulated pyruvate entry into a non-energy-generating pathway, with acetate as the final product23. It was also suggested that accumulation of intracellular NADH might enhance hydrogen production by a putative membrane-bound hydrogenase in Enterobacter aerogenes 19.…”

Section: Discussionmentioning

confidence: 99%

Contributory roles of two l-lactate dehydrogenases for l-lactic acid production in thermotolerant Bacillus coagulans

Sun

Zhang

Lyu

et al. 2016

Sci Rep

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Thermotolerant Bacillus coagulans is considered to be a more promising producer for bio-chemicals, due to its capacity to withstand harsh conditions. Two L-lactate dehydrogenase (LDH) encoding genes (ldhL1 and ldhL2) and one D-LDH encoding gene (ldhD) were annotated from the B. coagulans DSM1 genome. Transcriptional analysis revealed that the expression of ldhL2 was undetectable while the ldhL1 transcription level was much higher than that of ldhD at all growth phases. Deletion of the ldhL2 gene revealed no difference in fermentation profile compared to the wild-type strain, while ldhL1 single deletion or ldhL1ldhL2 double deletion completely blocked L-lactic acid production. Complementation of ldhL1 in the above knockout strains restored fermentation profiles to those observed in the wild-type strain. This study demonstrates ldhL1 is crucial for L-lactic acid production and NADH balance in B. coagulans DSM1 and lays the fundamental for engineering the thermotolerant B. coagulans strain as a platform chemicals producer.

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Utilization of d -Lactate as an Energy Source Supports the Growth of Gluconobacter oxydans

Cited by 20 publications

References 46 publications

Enzymatic Resolution by a d‐Lactate Oxidase Catalyzed Reaction for (S)‐2‐Hydroxycarboxylic Acids

Enzymatic Resolution by a d‐Lactate Oxidase Catalyzed Reaction for (S)‐2‐Hydroxycarboxylic Acids

A Bacterial Multidomain NAD-Independent d -Lactate Dehydrogenase Utilizes Flavin Adenine Dinucleotide and Fe-S Clusters as Cofactors and Quinone as an Electron Acceptor for d -Lactate Oxidization

Contributory roles of two l-lactate dehydrogenases for l-lactic acid production in thermotolerant Bacillus coagulans

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