Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis.

Vos, Willem M. de; Boerrigter, I.J.; Rooyen, R J van; Reiche, B; Hengstenberg, Wolfgang

doi:10.1016/s0021-9258(18)45741-9

Cited by 123 publications

(21 citation statements)

References 42 publications

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“…This cavity is lined with hydrophobic residues including Leu88, Leu89 and Val92 and is separated from the actual C terminus by two hydrophobic layers, comprising the sidechains of Leu96 and Leu99 and their counterparts in the other subunits. The volume of the cavity is 230 Å 3 . The electron-density map does not show any evidence for the presence of structurally ordered water molecules or other compounds in the cavity.…”

Section: Hydrophobic Cavitymentioning

confidence: 99%

“…Enzyme IIA lac was cloned into E. coli, overexpressed and purified according to the procedure previously described [3]. The crystallization of this protein has been reported previously [17].…”

Section: Protein Purification and Crystallizationmentioning

confidence: 99%

“…The IIA lac component was first isolated from Staphylococcus and later from milk fermenting bacteria [2]. The corresponding genes have been cloned and overexpressed in Escherichia coli [3].…”

Section: Introductionmentioning

confidence: 99%

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The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system

et al. 1997

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Enzyme IIAlactose is the first representative of the family of lactose/cellobiose-specific enzymes IIA for which a three-dimensional structure has been determined. Some of its structural features, like the presence of two histidine residues at the active site, seem to be common to all enzymes no overall structural homology is observed to any PTS proteins or to any other proteins in the Protein Data Bank. Enzyme IIAlactose shows surface complementarity to the phosphorylated form of HPr and several energetically favourable interactions between the two molecules can be predicted.

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Section: Hydrophobic Cavitymentioning

confidence: 99%

Section: Protein Purification and Crystallizationmentioning

confidence: 99%

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The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system

et al. 1997

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“…The gene model indicated the lacABCDFEGX genes as indicators of higher acidification rate (Fig 6). The lac genes of L. lactis are responsible for the tagatose 6-phosphate pathway (lacABCD), the phosphotransferase system (lacF and lacE), the phospho-beta-galactosidase (lacG), and one unknown function (lacX) [22,23]. These genes were split into two features in PLOS ONE the gene model, since the lacABCDF genes were missing in strain354 and the lac genes therefore did not co-occur in all strains.…”

Section: Genes For Lactose Metabolism Were Identified As Predictors Omentioning

confidence: 99%

Machine learning predicts and provides insights into milk acidification rates of Lactococcus lactis

et al. 2021

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Lactococcus lactis strains are important components in industrial starter cultures for cheese manufacturing. They have many strain-dependent properties, which affect the final product. Here, we explored the use of machine learning to create systematic, high-throughput screening methods for these properties. Fast acidification of milk is such a strain-dependent property. To predict the maximum hourly acidification rate (Vmax), we trained Random Forest (RF) models on four different genomic representations: Presence/absence of gene families, counts of Pfam domains, the 8 nucleotide long subsequences of their DNA (8-mers), and the 9 nucleotide long subsequences of their DNA (9-mers). Vmax was measured at different temperatures, volumes, and in the presence or absence of yeast extract. These conditions were added as features in each RF model. The four models were trained on 257 strains, and the correlation between the measured Vmax and the predicted Vmax was evaluated with Pearson Correlation Coefficients (PC) on a separate dataset of 85 strains. The models all had high PC scores: 0.83 (gene presence/absence model), 0.84 (Pfam domain model), 0.76 (8-mer model), and 0.85 (9-mer model). The models all based their predictions on relevant genetic features and showed consensus on systems for lactose metabolism, degradation of casein, and pH stress response. Each model also predicted a set of features not found by the other models.

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“…As indicated above, in many lactococcal strains lactose utilisation genes are plasmid encoded and a well-characterised example is present on the lactose mini-plasmid pMG820. The lac-operon on this plasmid encodes a lactose PTS import system (lacEF), a phospho-βgalactosidase (lacG) and the tagatose pathway (lacABCD) (de Vos et al 1990;van Rooijen, van Schalkwijk and de Vos 1991), and its expression is controlled by the divergently transcribed repressor LacR, which relieves repression upon binding to the tagatose pathway intermediate tagatose-6-phosphate (van Rooijen, Gasson and de Vos 1992).…”

Section: The Foundation Of Acidification Carbon Metabolism In L Lactismentioning

confidence: 99%

Lifestyle, metabolism and environmental adaptation inLactococcus lactis

Kleerebezem

Bachmann

Pelt-KleinJan

et al. 2020

FEMS Microbiology Reviews

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Lactococcus lactis serves as a paradigm organism for the lactic acid bacteria (LAB). Extensive research into the molecular biology, metabolism and physiology of several model strains of this species has been fundamental for our understanding of the LAB. Genomic studies have provided new insights in the species L. lactis, including the resolution of the genetic basis of its subspecies division, as well as the control mechanisms involved in the fine-tuning of growth-rate and energy metabolism. In addition, it has enabled novel approaches to study lactococcal lifestyle adaptations to the dairy application environment, including its adjustment to near-zero growth rates that are particularly relevant in the context of cheese ripening. This review highlights various insights in these areas and exemplifies the strength of combining experimental evolution with functional genomics and bacterial physiology research to expand our fundamental understanding of the L. lactis lifestyle under different environmental conditions.

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Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis.

Cited by 123 publications

References 42 publications

The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system

The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system

Machine learning predicts and provides insights into milk acidification rates of Lactococcus lactis

Lifestyle, metabolism and environmental adaptation inLactococcus lactis

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