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Multiple endoglycosidase (endo) F activities expressed by Flavobacterium meningosepticum . Endo F sub(1): Molecular cloning, primary sequence, and structural relationship to endo H

A full-length insert for the endo- beta -N-acetylglucosaminidase (Endo) F sub(1) gene was located on a 2,200-base pair EcoRI fragment of genomic DNA and cloned into the plasmid vector Bluescript. Transformed Escherichia coli) cells expressed Endo F sub(1) activity very well, but the enzyme apparentl...

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Bibliographic Details
Published in:The Journal of biological chemistry 1992-01, Vol.267 (6), p.3868-3872
Main Authors: Tarentino, AL, Quinones, G, Schrader, W P, Changchien, L-M, Plummer, TH Jr
Format: Article
Language:English
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Summary:A full-length insert for the endo- beta -N-acetylglucosaminidase (Endo) F sub(1) gene was located on a 2,200-base pair EcoRI fragment of genomic DNA and cloned into the plasmid vector Bluescript. Transformed Escherichia coli) cells expressed Endo F sub(1) activity very well, but the enzyme apparently was not processed and secreted into the medium as it normally is in Flavobacterium meningosepticum). DNA sequencing revealed an open reading frame of 1,017 nucleotides encoding a putative 50-amino acid signal sequence, and a mature protein (31,667 Da) of 289 amino acids. Potential catalytic domains identified in other proteins that hydrolyze the beta 1,4 glycosidic linkage between N-acetylglucosamine residues are also conserved for amino acid identity and relative spacing in Endo F sub(1).
ISSN:0021-9258