Bacterial lactate dehydrogenases.

Garvie, Ellen I.

doi:10.1128/mmbr.44.1.106-139.1980

Cited by 338 publications

(211 citation statements)

References 68 publications

(236 reference statements)

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“…Both Fe-S D-iLDH and glycolate oxidase are membranebound iLDHs are generally membrane-bound proteins (Garvie, 1980). To assess the locations of Fe-S D-iLDH and glycolate oxidase in P. putida KT2440, we measured their activities in cell fractions produced by sonication and differential centrifugation.…”

Section: Comparative Genome Analysis Predicts the Putative D-lactate mentioning

confidence: 99%

Coexistence of two d‐lactate‐utilizing systems in Pseudomonas putida KT2440

Zhang

Jiang

Sheng

et al. 2016

Environ Microbiol Rep

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It is advantageous for rhizosphere-dwelling microorganisms to utilize organic acids such as lactate. Pseudomonas putida KT2440 is one of the most widely studied rhizosphere-dwelling model organisms. The P. putida KT2440 genome contains an NAD-dependent d-lactate dehydrogenase encoding gene, but mutation of this gene does not play a role in d-lactate utilization. Instead, it was found that d-lactate utilization in P. putida KT2440 proceeds via a multidomain NAD-independent d-lactate dehydrogenase with a C-terminal domain containing several Fe-S cluster-binding motifs (Fe-S d-iLDH) and glycolate oxidase, which is widely distributed in various microorganisms. Both Fe-S d-iLDH and glycolate oxidase were identified to be membrane-bound proteins. Neither Fe-S d-iLDH nor glycolate oxidase is constitutively expressed but both of them can be induced by either enantiomer of lactate in P. putida KT2440. This study shows a case in which an environmental microbe contains two types of enzymes specific for d-lactate utilization.

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Section: Comparative Genome Analysis Predicts the Putative D-lactate mentioning

confidence: 99%

Coexistence of two d‐lactate‐utilizing systems in Pseudomonas putida KT2440

Zhang

Jiang

Sheng

et al. 2016

Environ Microbiol Rep

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“…The key enzyme in lactate production from pyruvate is the lactate dehydrogenase (LDH) that quantitatively consumes the electrons (in form of NADH) generated during glycolysis to reduce pyruvate to lactate. These NADH-oxidizing LDHs are classified as nLDHs (Garvie, 1980). Lactate produced by primary fermenters does not accumulate in the environment because it is a good growth substrate for many bacteria (Brockman and Wood, 1975;Balch et al, 1977;Yang et al, 1987;Diez-Gonzalez et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

A novel mode of lactate metabolism in strictly anaerobic bacteria

Weghoff

Bertsch

Müller

2014

Environmental Microbiology

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241

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Lactate is a common substrate for major groups of strictly anaerobic bacteria, but the biochemistry and bioenergetics of lactate oxidation is obscure. The high redox potential of the pyruvate/lactate pair of E0 ' = -190 mV excludes direct NAD(+) reduction (E0 ' = -320 mV). To identify the hitherto unknown electron acceptor, we have purified the lactate dehydrogenase (LDH) from the strictly anaerobic, acetogenic bacterium Acetobacterium woodii. The LDH forms a stable complex with an electron-transferring flavoprotein (Etf) that exhibited NAD(+) reduction only when reduced ferredoxin (Fd(2-) ) was present. Biochemical analyses revealed that the LDH/Etf complex of A. woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD(+) as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin (E0 ' ≈ -500 mV) to NAD(+) according to: lactate + Fd(2-) + 2 NAD(+) → pyruvate + Fd + 2 NADH. The reduced Fd(2-) is regenerated from NADH by a sequence of events that involves conversion of chemical (ATP) to electrochemical ( Δ μ ˜ Na + ) and finally redox energy (Fd(2-) from NADH) via reversed electron transport catalysed by the Rnf complex. Inspection of genomes revealed that this metabolic scenario for lactate oxidation may also apply to many other anaerobes.

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“…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. For this reason,s everal candidate proteins from LAB with the sequence feature of soluble d-iLDHs, together with DLD3 andG OX2071, were selected for furthers creening as possible putative d-lactate oxidases (d-LOXs;F igure 1A).…”

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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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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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Bacterial lactate dehydrogenases.

Abstract: TYPES OF BACTERIAL LACTATE DEHYDROGENASES (LDHs) .107 Nicotinamide Adenine Dinucleotide-Linked LDHs (nT H's) .107 D(-)-flLDH. .109 L((+-)-nH H's .110 Fructose 1,6-diphosphate-activated nlH's .110 Nicotinamide Adenine Dinucleotide-Independent LDHs (iLDH's) .110

Cited by 338 publications

References 68 publications

Coexistence of two d‐lactate‐utilizing systems in Pseudomonas putida KT2440

Coexistence of two d‐lactate‐utilizing systems in Pseudomonas putida KT2440

A novel mode of lactate metabolism in strictly anaerobic bacteria

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

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