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Taxonomic group: plant / Streptophyta (Phylum: Streptophyta)
Organ / tissue: stem

NCBI PubMed ID: 7540902
Journal NLM ID: 8603310
Publisher: Kluwer Academic Publishers
Institutions: Institut für Chemie, Univesität fur Bodenkultur Wien, Austria

The initial velocities of hydrolysis of nineteen glycopeptides by peptide: N-glycosidase F and A were determined. Substrates were prepared from bovine fetuin, hen ovalbumin, pineapple stem bromelain, bovine fibrin and taka-amylase. From these glycopeptides, several variants with regard to peptide and carbohydrate structure were prepared and derivatized with dabsyl chloride, dansyl chloride or activated resorufin. Tyrosine containing glycopeptides were also used without an additional chromophore. Enzymatic hydrolysis of glycopeptides was quantified by narrow bore, reversed phase HPLC with turnaround cycle times of down to 6 min, but usually 15 min. KM values ranging from 30 to 64 microM and from 4 to 36 microM were found for N-glycosidase F and A, respectively. Relative velocities of hydrolysis of the different substrates by each enzyme varied considerably. Little, if any, similarity of the performance of N-glycosidase F and A with the different substrates was observed. The minimal carbohydrate structure released by peptide: N-glycosidase F was a di-N-acetylchitobiose. N-glycosidase A could release even a single N-acetylglucosamine, albeit 3000 times slower than a di-N-acetylchitobiose or larger glycans. In general the structure of the intact glycan had little effect on activity, and with both enzymes the rate of hydrolysis appeared to be primarily governed by peptide structure and length. However, N-glycosidase F did not release glycans α-1,3-fucosylated at the asparagine linked N-acetylglucosamine irrespective of the presence of xylose in the substrate.

Structure type: oligomer
Location inside paper: d-Brl11
Compound class: N-linked glycopeptide
Contained glycoepitopes: IEDB_114085,IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_150900,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_86

Comments, role: Parent molecule: bromelain; Peptide is derivatized with dabsyl chloride, d-Brl10 is same as this structure but without Met

NCBI Taxonomy refs (TaxIDs): 4615
Reference(s) to other database(s): CCSD:40666, CBank-STR:19033
Show glycosyltransferases

There is only one chemically distinct structure:

CSCCC(NC(=O)C(CO)NC(=O)C(CO)NC(=O)C(CCC(=O)O)NC(=O)C(CC(=O)N[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO)[C@@H](O[C@@H]3O[C@H](CO[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O)[C@@H](O)[C@H](O)[C@@H]3O[C@@H]3OC[C@@H](O)[C@H](O)[C@H]3O)[C@H](O)[C@H]2NC(C)=O)[C@H](O[C@@H]2O[C@@H](C)[C@@H](O)[C@@H](O)[C@@H]2O)[C@H]1NC(C)=O)NC(=O)C(CC(N)=O)NC(=O)C(CCCNC(=N)N)NC(=O)C1CCCN1C(=O)C(NC(=O)C(CCCNC(=N)N)NC(=O)C(C)N)C(C)C)C(=O)O

SVG MW SMILES 3D mol Ionize