Characterization and mutational analysis of two UDP-galactose 4-epimerases in Streptococcus pneumoniae TIGR4
Current clinical treatments for pneumococcal infections have many limitations and are faced with many challenges. New capsular polysaccharide structures must be explored to cope with diseases caused by different serotypes of Streptococcus pneumoniae . UDP-galactose 4-epimerase (GalE) is an essential...
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| Published in: | Biochemistry (Moscow) Vol. 83; no. 1; pp. 37 - 44 |
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| Main Authors: | , , , , , |
| Format: | Journal Article |
| Language: | English |
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| Abstract | Current clinical treatments for pneumococcal infections have many limitations and are faced with many challenges. New capsular polysaccharide structures must be explored to cope with diseases caused by different serotypes of
Streptococcus pneumoniae
. UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. It is an important virulence factor in many bacterial pathogens. In this study, we found that two genes (
galE
sp1
and
galE
sp2
) are responsible for galactose metabolism in pathogenic S.
pneumoniae
TIGR4. Both GalE
Sp1
and Gal
ESp2
were shown to catalyze the epimerization of UDP-glucose (UDP-Glc)/UDP-galactose (UDP-Gal), but only GalE
Sp2
was shown to catalyze the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc)/UDP-N-acetylgalactosamine (UDP-GalNAc). Interestingly, GalE
Sp2
had 3-fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalE
Sp1
. The biochemical properties of GalE
Sp2
were studied. GalE
Sp2
was stable over a wide range of temperatures, between 30 and 70°C, at pH 8.0. The K86G substitution caused GalE
Sp2
to lose its epimerase activity toward UDP-Glc and UDP-Gal; however, substitution C300Y in GalE
Sp2
resulted in only decreased activity toward UDP-GlcNAc and UDP-GalNAc. These results indicate that the Lys86 residue plays a critical role in the activity and substrate specificity of GalE
Sp2
. |
|---|---|
| AbstractList | Current clinical treatments for pneumococcal infections have many limitations and are faced with many challenges. New capsular polysaccharide structures must be explored to cope with diseases caused by different serotypes of Streptococcus pneumoniae. UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. It is an important virulence factor in many bacterial pathogens. In this study, we found that two genes (galEsp1 and galEsp2) are responsible for galactose metabolism in pathogenic S. pneumoniae TIGR4. Both GalESp1 and GalESp2 were shown to catalyze the epimerization of UDP-glucose (UDP-Glc)/UDP-galactose (UDP-Gal), but only GalESp2 was shown to catalyze the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc)/UDP-N-acetylgalactosamine (UDP-GalNAc). Interestingly, GalESp2 had 3-fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. The biochemical properties of GalESp2 were studied. GalESp2 was stable over a wide range of temperatures, between 30 and 70°C, at pH 8.0. The K86G substitution caused GalESp2 to lose its epimerase activity toward UDP-Glc and UDP-Gal; however, substitution C300Y in GalESp2 resulted in only decreased activity toward UDP-GlcNAc and UDP-GalNAc. These results indicate that the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2. Current clinical treatments for pneumococcal infections have many limitations and are faced with many challenges. New capsular polysaccharide structures must be explored to cope with diseases caused by different serotypes of Streptococcus pneumoniae. UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. It is an important virulence factor in many bacterial pathogens. In this study, we found that two genes ([galE.sub.sp1] and [galE.sub.sp2]) are responsible for galactose metabolism in pathogenic S. pneumoniae TIGR4. Both [GalE.sub.Sp1] and [GalE.sub.Sp2] were shown to catalyze the epimerization of UDP-glucose (UDP-Glc)/UDP-galactose (UDP-Gal), but only [GalE.sub.Sp2] was shown to catalyze the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc)/UDP-N-acetylgalactosamine (UDP-GalNAc). Interestingly, [GalE.sub.Sp2] had 3-fold higher epimerase activity toward UDP-Glc/UDP-Gal than [GalE.sub.Sp1]. The biochemical properties of [GalE.sub.Sp2] were studied. [GalE.sub.Sp2] was stable over a wide range of temperatures, between 30 and 70[degrees]C, at pH 8.0. The K86G substitution caused [GalE.sub.Sp2] to lose its epimerase activity toward UDP-Glc and UDP-Gal; however, substitution C300Y in [GalE.sub.Sp2] resulted in only decreased activity toward UDP-GlcNAc and UDP-GalNAc. These results indicate that the Lys86 residue plays a critical role in the activity and substrate specificity of [GalE.sub.Sp2]. DOI: 10.1134/S0006297918010054 Keywords: UDP-galactose 4-epimerase (GalE), Streptococcus pneumoniae TIGR4, mutation, substrate specificity Current clinical treatments for pneumococcal infections have many limitations and are faced with many challenges. New capsular polysaccharide structures must be explored to cope with diseases caused by different serotypes of Streptococcus pneumoniae. UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. It is an important virulence factor in many bacterial pathogens. In this study, we found that two genes ([galE.sub.sp1] and [galE.sub.sp2]) are responsible for galactose metabolism in pathogenic S. pneumoniae TIGR4. Both [GalE.sub.Sp1] and [GalE.sub.Sp2] were shown to catalyze the epimerization of UDP-glucose (UDP-Glc)/UDP-galactose (UDP-Gal), but only [GalE.sub.Sp2] was shown to catalyze the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc)/UDP-N-acetylgalactosamine (UDP-GalNAc). Interestingly, [GalE.sub.Sp2] had 3-fold higher epimerase activity toward UDP-Glc/UDP-Gal than [GalE.sub.Sp1]. The biochemical properties of [GalE.sub.Sp2] were studied. [GalE.sub.Sp2] was stable over a wide range of temperatures, between 30 and 70[degrees]C, at pH 8.0. The K86G substitution caused [GalE.sub.Sp2] to lose its epimerase activity toward UDP-Glc and UDP-Gal; however, substitution C300Y in [GalE.sub.Sp2] resulted in only decreased activity toward UDP-GlcNAc and UDP-GalNAc. These results indicate that the Lys86 residue plays a critical role in the activity and substrate specificity of [GalE.sub.Sp2]. Current clinical treatments for pneumococcal infections have many limitations and are faced with many challenges. New capsular polysaccharide structures must be explored to cope with diseases caused by different serotypes of Streptococcus pneumoniae. UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. It is an important virulence factor in many bacterial pathogens. In this study, we found that two genes (galEsp1 and galEsp2) are responsible for galactose metabolism in pathogenic S. pneumoniae TIGR4. Both GalESp1 and GalESp2 were shown to catalyze the epimerization of UDP-glucose (UDP-Glc)/UDP-galactose (UDP-Gal), but only GalESp2 was shown to catalyze the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc)/UDP-N-acetylgalactosamine (UDP-GalNAc). Interestingly, GalESp2 had 3-fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. The biochemical properties of GalESp2 were studied. GalESp2 was stable over a wide range of temperatures, between 30 and 70°C, at pH 8.0. The K86G substitution caused GalESp2 to lose its epimerase activity toward UDP-Glc and UDP-Gal; however, substitution C300Y in GalESp2 resulted in only decreased activity toward UDP-GlcNAc and UDP-GalNAc. These results indicate that the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2. Current clinical treatments for pneumococcal infections have many limitations and are faced with many challenges. New capsular polysaccharide structures must be explored to cope with diseases caused by different serotypes of Streptococcus pneumoniae . UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. It is an important virulence factor in many bacterial pathogens. In this study, we found that two genes ( galE sp1 and galE sp2 ) are responsible for galactose metabolism in pathogenic S. pneumoniae TIGR4. Both GalE Sp1 and Gal ESp2 were shown to catalyze the epimerization of UDP-glucose (UDP-Glc)/UDP-galactose (UDP-Gal), but only GalE Sp2 was shown to catalyze the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc)/UDP-N-acetylgalactosamine (UDP-GalNAc). Interestingly, GalE Sp2 had 3-fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalE Sp1 . The biochemical properties of GalE Sp2 were studied. GalE Sp2 was stable over a wide range of temperatures, between 30 and 70°C, at pH 8.0. The K86G substitution caused GalE Sp2 to lose its epimerase activity toward UDP-Glc and UDP-Gal; however, substitution C300Y in GalE Sp2 resulted in only decreased activity toward UDP-GlcNAc and UDP-GalNAc. These results indicate that the Lys86 residue plays a critical role in the activity and substrate specificity of GalE Sp2 . Current clinical treatments for pneumococcal infections have many limitations and are faced with many challenges. New capsular polysaccharide structures must be explored to cope with diseases caused by different serotypes of Streptococcus pneumoniae. UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. It is an important virulence factor in many bacterial pathogens. In this study, we found that two genes (galE.sub.sp1 and galE.sub.sp2) are responsible for galactose metabolism in pathogenic S. pneumoniae TIGR4. Both GalE.sub.Sp1 and Gal.sub.ESp2 were shown to catalyze the epimerization of UDP-glucose (UDP-Glc)/UDP-galactose (UDP-Gal), but only GalE.sup.Sp2 was shown to catalyze the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc)/UDP-N-acetylgalactosamine (UDP-GalNAc). Interestingly, GalE.sub.Sp2 had 3-fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalE.sub.Sp1. The biochemical properties of GalE.sub.Sp2 were studied. GalE.sub.Sp2 was stable over a wide range of temperatures, between 30 and 70°C, at pH 8.0. The K86G substitution caused GalE.sub.Sp2 to lose its epimerase activity toward UDP-Glc and UDP-Gal; however, substitution C300Y in GalE.sub.Sp2 resulted in only decreased activity toward UDP-GlcNAc and UDP-GalNAc. These results indicate that the Lys86 residue plays a critical role in the activity and substrate specificity of GalE.sub.Sp2. |
| Audience | Academic |
| Author | Chen, M. Wang, J. H. Wang, Y. F. Chen, L. L. Zhai, Y. F. Han, D. L. |
| Author_xml | – sequence: 1 givenname: L. L. surname: Chen fullname: Chen, L. L. organization: State Key Laboratory of Microbial Technology, School of Life Sciences, Shandong University, Institute of Agro-Food Science and Technology, Shandong Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing Technology of Shandong Province/Key Laboratory of Novel Food Resources Processing, Ministry of Agriculture – sequence: 2 givenname: D. L. surname: Han fullname: Han, D. L. organization: State Key Laboratory of Microbial Technology, School of Life Sciences, Shandong University – sequence: 3 givenname: Y. F. surname: Zhai fullname: Zhai, Y. F. organization: State Key Laboratory of Microbial Technology, School of Life Sciences, Shandong University – sequence: 4 givenname: J. H. surname: Wang fullname: Wang, J. H. organization: Institute of Agro-Food Science and Technology, Shandong Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing Technology of Shandong Province/Key Laboratory of Novel Food Resources Processing, Ministry of Agriculture – sequence: 5 givenname: Y. F. surname: Wang fullname: Wang, Y. F. organization: Institute of Agro-Food Science and Technology, Shandong Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing Technology of Shandong Province/Key Laboratory of Novel Food Resources Processing, Ministry of Agriculture – sequence: 6 givenname: M. surname: Chen fullname: Chen, M. email: chenmin@sdu.edu.cn organization: State Key Laboratory of Microbial Technology, School of Life Sciences, Shandong University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29534667$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1016_j_vaccine_2021_06_017 crossref_primary_10_3389_fmicb_2019_01996 crossref_primary_10_3390_pathogens10101322 |
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| SubjectTerms | Analysis Bacteria Bacterial pneumonia Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Cellulose Chemical properties Dextrose Enzymes Epimerase Galactose Gene mutation Genetic aspects Glucose Health aspects Identification and classification Life Sciences Metabolism Microbiology N-Acetylgalactosamine N-Acetylglucosamine Observations Physiological aspects Pneumonia Serotypes Streptococcus infections Streptococcus pneumoniae Substitutes Substrate specificity Substrates Vaccines Virulence Virulence (Microbiology) Virulence factors |
| Title | Characterization and mutational analysis of two UDP-galactose 4-epimerases in Streptococcus pneumoniae TIGR4 |
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