Found 2 records.
Displayed records from 1 to 2
Expand all records
Collapse all records
Show all as text (SweetDB notation)
Show all graphically (SNFG notation)
Bar-Peled M, Griffith CL, Doering TL
Functional cloning and characterization of a UDP-glucuronic acid decarboxylase: the pathogenic fungus Cryptococcus neoformans elucidates UDP-xylose synthesis
Proceedings of the National Academy of Sciences of the USA 21 (2001)
12003-12008
b-Xyl-(1-2)-+
|
b-GlcA-(1-2)-+ |
| |
b-Xyl-(1-2)-+ | |
| | |
-3)-a-Man-(1-3)-a-Man-(1-3)-a-Man-(1-
|
b-Xyl-(1-4)-+ |
Show graphically |
Cryptococcus neoformans B
(later renamed to: Cryptococcus gattii VGI)
(NCBI TaxID 37769,
species name lookup)
Taxonomic group: fungi / Basidiomycota
(Phylum: Basidiomycota)
Associated disease: infection due to Cryptococcus neoformans [ICD11:
XN3EH 
];
infection due to Cryptococcus gattii [ICD11:
XN0LE 
]
Publication DOI: 10.1073/pnas.211229198Journal NLM ID: 7505876Publisher: National Academy of Sciences
Correspondence: peled

ccrc.uga.edu
Institutions: Complex Carbohydrate Research Center and Department of Botany, University of Georgia, Athens, GA 30602, USA, Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110, USA
UDP-xylose is a sugar donor required for the synthesis of diverse and important glycan structures in animals, plants, fungi, and bacteria. Xylose-containing glycans are particularly abundant in plants and in the polysaccharide capsule that is the major virulence factor of the pathogenic fungus Cryptococcus neoformans. Biosynthesis of UDP-xylose is mediated by UDP-glucuronic acid decarboxylase, which converts UDP-glucuronic acid to UDP-xylose. Although this enzymatic activity was described over 40 years ago it has never been fully purified, and the gene encoding it has not been identified. We used homology to a bacterial gene, hypothesized to encode a related function, to identify a cryptococcal sequence as putatively encoding a UDP-glucuronic acid decarboxylase. A soluble 47-kDa protein derived from bacteria expressing the C. neoformans gene catalyzed conversion of UDP-glucuronic acid to UDP-xylose, as confirmed by NMR analysis. NADH, UDP, and UDP-xylose inhibit the activity. Close homologs of the cryptococcal gene, which we termed UXS1, appear in genome sequence data from organisms ranging from bacteria to humans.
Structure type: suggested polymer biological repeating unit
Location inside paper: fig. 1, GXM
Contained glycoepitopes: IEDB_114701,IEDB_115136,IEDB_115576,IEDB_130701,IEDB_1394182,IEDB_140116,IEDB_140630,IEDB_144983,IEDB_145668,IEDB_152206,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_423153,IEDB_76933,IEDB_983930,SB_197,SB_44,SB_67,SB_72
Methods: 1H NMR, SDS-PAGE, HPLC, cloning, protein expression, UDP-GlcA decarboxylase assay
Related record ID(s): 40794
NCBI Taxonomy refs (TaxIDs): 37769Reference(s) to other database(s): GTC:G28901JS
Show glycosyltransferases
There are too many chemically distinct structures (~16384), so only one is shown:
-3)[bDXylp(1-2)]aDManp(1-3)[bDXylp(1-4),bDGlcpA(1-2)]aDManp(1-3)[bDXylp(1-2)]aDManp(1-
Expand this record
Collapse this record
Bar-Peled M, Griffith CL, Doering TL
Functional cloning and characterization of a UDP-glucuronic acid decarboxylase: the pathogenic fungus Cryptococcus neoformans elucidates UDP-xylose synthesis
Proceedings of the National Academy of Sciences of the USA 21 (2001)
12003-12008
a-Man-(1-3)-a-Man-(1-4)-b-Gal-(1-3)-+
|
b-Xyl-(1-3)-+ |
| |
b-Xyl-(1-2)-+ | |
| | |
b-Xyl-(1-3)-a-Man-(1-3)-a-Man-(1-4)-b-Gal-(1-3)-+ |
| |
-6)-a-Gal-(1-6)-a-Gal-(1-6)-a-Gal-(1-6)-a-Gal-(1- |
Show graphically |
Cryptococcus neoformans
(NCBI TaxID 5207,
species name lookup)
Taxonomic group: fungi / Basidiomycota
(Phylum: Basidiomycota)
Associated disease: infection due to Cryptococcus neoformans [ICD11:
XN3EH 
]
Publication DOI: 10.1073/pnas.211229198Journal NLM ID: 7505876Publisher: National Academy of Sciences
Correspondence: peled

ccrc.uga.edu
Institutions: Complex Carbohydrate Research Center and Department of Botany, University of Georgia, Athens, GA 30602, USA, Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110, USA
UDP-xylose is a sugar donor required for the synthesis of diverse and important glycan structures in animals, plants, fungi, and bacteria. Xylose-containing glycans are particularly abundant in plants and in the polysaccharide capsule that is the major virulence factor of the pathogenic fungus Cryptococcus neoformans. Biosynthesis of UDP-xylose is mediated by UDP-glucuronic acid decarboxylase, which converts UDP-glucuronic acid to UDP-xylose. Although this enzymatic activity was described over 40 years ago it has never been fully purified, and the gene encoding it has not been identified. We used homology to a bacterial gene, hypothesized to encode a related function, to identify a cryptococcal sequence as putatively encoding a UDP-glucuronic acid decarboxylase. A soluble 47-kDa protein derived from bacteria expressing the C. neoformans gene catalyzed conversion of UDP-glucuronic acid to UDP-xylose, as confirmed by NMR analysis. NADH, UDP, and UDP-xylose inhibit the activity. Close homologs of the cryptococcal gene, which we termed UXS1, appear in genome sequence data from organisms ranging from bacteria to humans.
Structure type: polymer chemical repeating unit
Location inside paper: fig. 1, GalXM
Contained glycoepitopes: IEDB_114701,IEDB_130701,IEDB_134624,IEDB_136044,IEDB_136095,IEDB_136906,IEDB_137472,IEDB_1394182,IEDB_141794,IEDB_144983,IEDB_145668,IEDB_151528,IEDB_152206,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_190606,IEDB_983930,SB_163,SB_165,SB_166,SB_187,SB_195,SB_197,SB_44,SB_67,SB_7,SB_72,SB_88
Methods: 1H NMR, SDS-PAGE, HPLC, cloning, protein expression, UDP-GlcA decarboxylase assay
Related record ID(s): 40538
NCBI Taxonomy refs (TaxIDs): 5207Reference(s) to other database(s): GTC:G36303MW
Show glycosyltransferases
There are too many chemically distinct structures (~67108864), so only one is shown:
-6)aDGalp(1-6)[bDXylp(1-3)[bDXylp(1-2)[bDXylp(1-3)aDManp(1-3)]aDManp(1-4)]bDGalp(1-3)]aDGalp(1-6)aDGalp(1-6)[aDManp(1-3)aDManp(1-4)bDGalp(1-3)]aDGalp(1-
Expand this record
Collapse this record
Total list of record IDs on all result pages of the current query:
Execution: 5 sec