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Riegert AS, Narindovshvili T, Coricello A, Richards NGJ, Raushel FM
Functional Characterization of Two PLP-Dependent Enzymes Involved in Capsular Polysaccharide Biosynthesis from Campylobacter jejuni
Biochemistry 60(37) (2021)
2836-2843
Subst-(1-4)-D-gro-a-L-glcHepp6Me-(1-3)-+
|
Subst-(1-3)-+ |
| |
-2)-b-D-Ribf-(1-5)-b-D-GalfNAc-(1-4)-a-D-GlcpA-(1-
|
EtN-(2-6)-+
Subst = O-methyl phosphamide (OHPO(NH2)OMe) = SMILES {1}OP(OC)(N)=O |
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Campylobacter jejuni HS:2 NCTC 11168
(Ancestor NCBI TaxID 197,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11:
XN4Q5 
]
NCBI PubMed ID: 34505775Publication DOI: 10.1021/acs.biochem.1c00439Journal NLM ID: 0370623Publisher: American Chemical Society
Correspondence: raushel

tamu.edu
Institutions: Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States, Department of Biochemistry & Biophysics, Texas A&M University, College Station, Texas 77843, United States, Dipartimento di Scienze della Salute, Universita 'Magna Gracia' di Catanzaro, 88100 Catanzaro, Italiy, School of Chemistry, Cardiff University, Cardiff CF10 3AT, United Kingdom
Campylobacter jejuni is a Gram-negative, pathogenic bacterium that causes campylobacteriosis, a form of gastroenteritis. C. jejuni is the most frequent cause of food-borne illness in the world, surpassing Salmonella and E. coli. Coating the surface of C. jejuni is a layer of sugar molecules known as the capsular polysaccharide that, in C. jejuni NCTC 11168, is composed of a repeating unit of d-glycero-l-gluco-heptose, d-glucuronic acid, d-N-acetyl-galactosamine, and d-ribose. The d-glucuronic acid moiety is further amidated with either serinol or ethanolamine. It is unknown how these modifications are synthesized and attached to the polysaccharide. Here, we report the catalytic activities of two previously uncharacterized, pyridoxal phosphate (PLP)-dependent enzymes, Cj1436 and Cj1437, from C. jejuni NCTC 11168. Using a combination of mass spectrometry and nuclear magnetic resonance, we determined that Cj1436 catalyzes the decarboxylation of l-serine phosphate to ethanolamine phosphate. Cj1437 was shown to catalyze the transamination of dihydroxyacetone phosphate to (S)-serinol phosphate in the presence of l-glutamate. The probable routes to the ultimate formation of the glucuronamide substructures in the capsular polysaccharides of C. jejuni are discussed.
NMR, biosynthesis, structure, capsular polysaccharide, Campylobacter jejuni, mass spectrometry, decarboxylase, L-serine phosphate
Structure type: polymer chemical repeating unit
Location inside paper: p. 2837, Fig. 1, (2)
Compound class: CPS
Contained glycoepitopes: IEDB_115136,IEDB_120354,IEDB_137473,IEDB_140630,IEDB_149136
Methods: 13C NMR, 1H NMR, PCR, kinetics assays, 31P NMR, chemical synthesis, MS, genetic methods, cloning, bioinformatic analysis, enzymatic synthesis, membrane inlet MS
Related record ID(s): 9754, 10931
NCBI Taxonomy refs (TaxIDs): 197
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Riegert AS, Narindovshvili T, Coricello A, Richards NGJ, Raushel FM
Functional Characterization of Two PLP-Dependent Enzymes Involved in Capsular Polysaccharide Biosynthesis from Campylobacter jejuni
Biochemistry 60(37) (2021)
2836-2843
GroN-(2-6)-+ Subst-(1-4)-+
| |
-4)-b-D-GlcpA-(1-3)-b-D-GlcpNAc-(1-
Subst = O-methyl phosphamide (OHPO(NH2)OMe) = SMILES {1}OP(OC)(N)=O |
Show graphically |
Campylobacter jejuni HS:19 RM 1285
(Ancestor NCBI TaxID 197,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11:
XN4Q5 
]
NCBI PubMed ID: 34505775Publication DOI: 10.1021/acs.biochem.1c00439Journal NLM ID: 0370623Publisher: American Chemical Society
Correspondence: raushel

tamu.edu
Institutions: Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States, Department of Biochemistry & Biophysics, Texas A&M University, College Station, Texas 77843, United States, Dipartimento di Scienze della Salute, Universita 'Magna Gracia' di Catanzaro, 88100 Catanzaro, Italiy, School of Chemistry, Cardiff University, Cardiff CF10 3AT, United Kingdom
Campylobacter jejuni is a Gram-negative, pathogenic bacterium that causes campylobacteriosis, a form of gastroenteritis. C. jejuni is the most frequent cause of food-borne illness in the world, surpassing Salmonella and E. coli. Coating the surface of C. jejuni is a layer of sugar molecules known as the capsular polysaccharide that, in C. jejuni NCTC 11168, is composed of a repeating unit of d-glycero-l-gluco-heptose, d-glucuronic acid, d-N-acetyl-galactosamine, and d-ribose. The d-glucuronic acid moiety is further amidated with either serinol or ethanolamine. It is unknown how these modifications are synthesized and attached to the polysaccharide. Here, we report the catalytic activities of two previously uncharacterized, pyridoxal phosphate (PLP)-dependent enzymes, Cj1436 and Cj1437, from C. jejuni NCTC 11168. Using a combination of mass spectrometry and nuclear magnetic resonance, we determined that Cj1436 catalyzes the decarboxylation of l-serine phosphate to ethanolamine phosphate. Cj1437 was shown to catalyze the transamination of dihydroxyacetone phosphate to (S)-serinol phosphate in the presence of l-glutamate. The probable routes to the ultimate formation of the glucuronamide substructures in the capsular polysaccharides of C. jejuni are discussed.
NMR, biosynthesis, structure, capsular polysaccharide, Campylobacter jejuni, mass spectrometry, decarboxylase, L-serine phosphate
Structure type: polymer chemical repeating unit
Location inside paper: p. 2837, Fig. 1, (3)
Compound class: CPS
Contained glycoepitopes: IEDB_115136,IEDB_135813,IEDB_137340,IEDB_140630,IEDB_141807,IEDB_151527,IEDB_151531,IEDB_231709,IEDB_423153
Methods: 13C NMR, 1H NMR, PCR, kinetics assays, 31P NMR, chemical synthesis, MS, genetic methods, cloning, bioinformatic analysis, enzymatic synthesis, membrane inlet MS
Related record ID(s): 9753, 10931
NCBI Taxonomy refs (TaxIDs): 197
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There is only one chemically distinct structure:
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Riegert AS, Narindovshvili T, Coricello A, Richards NGJ, Raushel FM
Functional Characterization of Two PLP-Dependent Enzymes Involved in Capsular Polysaccharide Biosynthesis from Campylobacter jejuni
Biochemistry 60(37) (2021)
2836-2843
Subst-(1-4)-D-gro-a-L-glcHepp6Me-(1-3)-+
|
Subst-(1-3)-+ |
| |
-2)-b-D-Ribf-(1-5)-b-D-GalfNAc-(1-4)-a-D-GlcpA-(1-
|
GroN-(2-6)-+
Subst = O-methyl phosphamide (OHPO(NH2)OMe) = SMILES {1}OP(OC)(N)=O |
Show graphically |
Campylobacter jejuni HS:2 NCTC 11168
(Ancestor NCBI TaxID 197,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11:
XN4Q5 
]
NCBI PubMed ID: 34505775Publication DOI: 10.1021/acs.biochem.1c00439Journal NLM ID: 0370623Publisher: American Chemical Society
Correspondence: raushel

tamu.edu
Institutions: Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States, Department of Biochemistry & Biophysics, Texas A&M University, College Station, Texas 77843, United States, Dipartimento di Scienze della Salute, Universita 'Magna Gracia' di Catanzaro, 88100 Catanzaro, Italiy, School of Chemistry, Cardiff University, Cardiff CF10 3AT, United Kingdom
Campylobacter jejuni is a Gram-negative, pathogenic bacterium that causes campylobacteriosis, a form of gastroenteritis. C. jejuni is the most frequent cause of food-borne illness in the world, surpassing Salmonella and E. coli. Coating the surface of C. jejuni is a layer of sugar molecules known as the capsular polysaccharide that, in C. jejuni NCTC 11168, is composed of a repeating unit of d-glycero-l-gluco-heptose, d-glucuronic acid, d-N-acetyl-galactosamine, and d-ribose. The d-glucuronic acid moiety is further amidated with either serinol or ethanolamine. It is unknown how these modifications are synthesized and attached to the polysaccharide. Here, we report the catalytic activities of two previously uncharacterized, pyridoxal phosphate (PLP)-dependent enzymes, Cj1436 and Cj1437, from C. jejuni NCTC 11168. Using a combination of mass spectrometry and nuclear magnetic resonance, we determined that Cj1436 catalyzes the decarboxylation of l-serine phosphate to ethanolamine phosphate. Cj1437 was shown to catalyze the transamination of dihydroxyacetone phosphate to (S)-serinol phosphate in the presence of l-glutamate. The probable routes to the ultimate formation of the glucuronamide substructures in the capsular polysaccharides of C. jejuni are discussed.
NMR, biosynthesis, structure, capsular polysaccharide, Campylobacter jejuni, mass spectrometry, decarboxylase, L-serine phosphate
Structure type: polymer chemical repeating unit
Location inside paper: p. 2837, Fig. 1, (1)
Compound class: CPS
Contained glycoepitopes: IEDB_115136,IEDB_137473,IEDB_140630,IEDB_149136
Methods: 13C NMR, 1H NMR, PCR, kinetics assays, 31P NMR, chemical synthesis, MS, genetic methods, cloning, bioinformatic analysis, enzymatic synthesis, membrane inlet MS
Related record ID(s): 9753, 9754
NCBI Taxonomy refs (TaxIDs): 197
Show glycosyltransferases
There is only one chemically distinct structure:
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