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- W4236027633 abstract "The gene encoding endo-β-N-acetylglucosaminidase fromArthrobacter protophormiae(Endo-A) was cloned, and its nucleotide sequence was determined. A single open reading frame consisting of 1935 base pairs and encoding a polypeptide composed of signal peptides of 24 amino acids and a mature protein of 621 amino acids was found. The primary structure of Endo-A exhibited significant homology withF01F.10gene product fromCaenorhabditis elegansand weak homology with peptide-N4-(N-acetyl-β-d-glucosaminyl)asparagine amidase fromFlavobacterium meningosepticumand chitinase fromStreptomyces olivaceoviridis.However, the enzyme had no significant homology with any previously reported endo-β-N-acetylglucosaminidases. TransformedEscherichia colicells carrying the 4.5-kb fragment expressed Endo-A activity. This enzyme activity was detected in the medium as well as in the periplasmic space of cells under the control of the Endo-A gene promoter. The recombinant Endo-A was efficiently isolated from the periplasmic space of the cells. N-terminal sequence analysis revealed that native and recombinant Endo-A have the same N-terminus. Recombinant and native Endo-A also showed very similar optimum pH profiles and transglycosylation activity." @default.
- W4236027633 created "2022-05-12" @default.
- W4236027633 date "1997-03-01" @default.
- W4236027633 modified "2023-09-30" @default.
- W4236027633 title "IN APPRECIATION" @default.
- W4236027633 doi "https://doi.org/10.1006/abbi.1997.9891" @default.
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