Properties and Function of Fumarate Reductase (NADH) in Streptococcus Lactis

Hillier, A J; Jericho, RE; Green, SM; Jago, G. R.

doi:10.1071/bi9790625

Cited by 11 publications

(9 citation statements)

References 16 publications

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“…In fact, fumarase activity has been reported for some LAB that colonize grape must and wines (Pilone 1975). Reduction of fumarate to succinate can be utilized by some LAB to regenerate the intracellular NAD + pool and therefore allow for a more efficient degradation of sugars (Hillier et al 1979;Ryu et al 2001). Nevertheless, the relevance of Asp as a source of fumarate has not been evaluated.…”

Section: Aspartasementioning

confidence: 98%

Amino Acid Catabolic Pathways of Lactic Acid Bacteria

Fernández

Zúñiga

2006

Critical Reviews in Microbiology

341

229

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Lactic acid bacteria (LAB) constitute a diverse group of Gram positive obligately fermentative microorganisms which include both beneficial and pathogenic strains. LAB generally have complex nutritional requirements and therefore they are usually associated with nutrient-rich environments such as animal bodies, plants and foodstuffs. Amino acids represent an important resource for LAB and their utilization serves a number of physiological roles such as intracellular pH control, generation of metabolic energy or redox power, and resistance to stress. As a consequence, the regulation of amino acid catabolism involves a wide set of both general and specific regulators and shows significant differences among LAB. Moreover, due to their fermentative metabolism, LAB amino acid catabolic pathways in some cases differ significantly from those described in best studied prokaryotic model organisms such as Escherichia coli or Bacillus subtilis. Thus, LAB amino acid catabolism constitutes an interesting case for the study of metabolic pathways. Furthermore, LAB are involved in the production of a great variety of fermented products so that the products of amino acid catabolism are also relevant for the safety and the quality of fermented products.

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Section: Aspartasementioning

confidence: 98%

Amino Acid Catabolic Pathways of Lactic Acid Bacteria

Fernández

Zúñiga

2006

Critical Reviews in Microbiology

341

229

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“…The NSLAB subsequently grow to high cell densities ( ca 10 7 –10 8 CFU g −1 ) during the ageing process. The production of succinate was described for L. lactis (Harper 1965; Hillier and Jago 1978a,b; Hillier et al. 1979; Lapujade et al.…”

Section: Introductionmentioning

confidence: 99%

Succinate production and citrate catabolism by Cheddar cheese nonstarter lactobacilli

Dudley¹,

Steele

2005

J Appl Microbiol

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Aims: To identify strains of Cheddar cheese nonstarter lactobacilli that synthesize succinate from common precursors and characterize the biochemical pathways utilized. Methods and Results: Whole cell incubations of Lactobacillus plantarum, Lactobacillus casei, Lactobacillus zeae and Lactobacillus rhamnosus, were used to identify strains that accumulated succinate from citrate, L L-lactate, aspartic acid or isocitrate. In vivo 13 C-nuclear magnetic resonance spectroscopy ( 13 C-NMR) identified the biochemical pathway involved at pH 7AE0, and under conditions more representative of the cheese ripening environment (pH 5AE1/4% NaCl/13°C). Enzyme assays on cell-free extracts were used to support the pathway suggested by 13 C-NMR. Conclusions: The Lact. plantarum strains studied synthesize succinate from citrate by the reductive tricarboxylic acid (TCA) cycle at either pH 7AE0 or pH 5AE1/4% NaCl/13°C. Lactobacillus casei, Lact. zeae and Lact. rhamnosus strains lack one or more enzymatic activities present in this pathway, and do not accumulate succinate from any of the four precursors studied. Significance and Impact of the Study: The addition of Lact. plantarum strains to milk during cheese manufacture may increase the accumulation of the flavour enhancer succinate.

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“…Since both the Oye2p‐acrylate binding and the reduction of α,β‐carbon double bonds are inefficient, rational engineering of OYE for higher propionic acid yield would have to 1) enhance substrate binding by making the ligand binding pocket more electropositive, and 2) introduce amino acid residues in the active site that can coordinate acrylic acid, such that the necessary electron withdrawing groups would stabilize the transition state. The fumarate reductase (1.3.1.6) from Lactococcus lactis has been shown to have low reactivity against acrylate, but we were unable to reproduce this result (with 1 µM enzyme and 2 mM acrylate). Ambiguity in the particular strain of L. lactis may explain this discrepancy.…”

Section: Discussionmentioning

confidence: 79%

“…The final reaction is the reduction of acrylic acid to propionic acid. There is a report that this activity can be catalyzed by fumarate reductase in Lactococcus lactis , though the activity was low . The reduction of acrylic acid to propionic acid will be common across many predicted pathways and will subsequently be discussed in more detail.…”

Section: Resultsmentioning

confidence: 98%

“…The enoate reductase Enr from Clostridium tyrobutyricum (CAA71086.1) was selected because it has been recombinantly expressed under T 5 promoter in E. coli M15(pREP4) . The L. lactis fumarate reductase FrdC was included to reproduce the acrylate reduction assay conducted by Hillier, et al FrdC (BAL51025.1) is the only gene annotated as a fumarate reductase in the Lactococcus lactis genome (AP012281.1). Fre is an E. coli enzyme used in the FrdC assay to reduce FAD to FADH 2 , which FrdC uses as a cofactor.…”

Section: Resultsmentioning

confidence: 99%

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Exploring De Novo metabolic pathways from pyruvate to propionic acid

Stine

Zhang

et al. 2016

Biotechnology Progress

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Industrial biotechnology provides an efficient, sustainable solution for chemical production. However, designing biochemical pathways based solely on known reactions does not exploit its full potential. Enzymes are known to accept non-native substrates, which may allow novel, advantageous reactions. We have previously developed a computational program named Biological Network Integrated Computational Explorer (BNICE) to predict promiscuous enzyme activities and design synthetic pathways, using generalized reaction rules curated from biochemical reaction databases. Here, we use BNICE to design pathways synthesizing propionic acid from pyruvate. The currently known natural pathways produce undesirable by-products lactic acid and succinic acid, reducing their economic viability. BNICE predicted seven pathways containing four reaction steps or less, five of which avoid these by-products. Among the 16 biochemical reactions comprising these pathways, 44% were validated by literature references. More than 28% of these known reactions were not in the BNICE training dataset, showing that BNICE was able to predict novel enzyme substrates. Most of the pathways included the intermediate acrylic acid. As acrylic acid bioproduction has been well advanced, we focused on the critical step of reducing acrylic acid to propionic acid. We experimentally validated that Oye2p from Saccharomyces cerevisiae can catalyze this reaction at a slow turnover rate (10(-3) s(-1) ), which was unknown to occur with this enzyme, and is an important finding for further propionic acid metabolic engineering. These results validate BNICE as a pathway-searching tool that can predict previously unknown promiscuous enzyme activities and show that computational methods can elucidate novel biochemical pathways for industrial applications. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:303-311, 2016.

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Properties and Function of Fumarate Reductase (NADH) in Streptococcus Lactis

Cited by 11 publications

References 16 publications

Amino Acid Catabolic Pathways of Lactic Acid Bacteria

Amino Acid Catabolic Pathways of Lactic Acid Bacteria

Succinate production and citrate catabolism by Cheddar cheese nonstarter lactobacilli

Exploring De Novo metabolic pathways from pyruvate to propionic acid

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