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J. Biol. Chem., Vol. 259, Issue 12, 7577-7583, Jun, 1984
PW Robbins, RB Trimble, DF Wirth, C Hering, F Maley, GF Maley, R Das, BW Gibson, N Royal and K Biemann
We report the DNA and primary amino acid sequences of the Streptomyces
plicatus enzyme endo-beta-N-acetylglucosaminidase H. Peptide sequence
information was derived from enzyme isolated from Streptomyces culture
medium using a combination of mass spectrometric methods and conventional
techniques, including Edman degradation and carboxypeptidase Y digestion.
The DNA sequence was determined by analysis of the
Endo-beta-N-acetylglucosaminidase H gene cloned into the Escherichia coli
plasmid pBR322 (Robbins, P. W., Wirth , D. F., and Hering , C. (1981) J.
Biol. Chem. 256, 10640-10644). The enzyme from Streptomyces medium is 271
(or 269) amino acids in length and has a ragged NH2-terminal sequence
beginning primarily with Ala-Pro-Val or Ala-Pro-Ala-Pro-Val. DNA resection
experiments as well as the DNA sequence itself suggest that a proenzyme or,
more probably, " prepro " enzyme may be the primary product of translation.
The long 42 (or 44) residue leader sequence of the preproenzyme shows
striking similarities to leader sequences found on proteins secreted by
Bacillus species. The leader sequence is partially removed by E. coli and,
as reported previously, endo-beta-N-acetylglucosaminidase H made in E. coli
appears in both the periplasmic space and in the cell.
Primary structure of the Streptomyces enzyme endo-beta-N- acetylglucosaminidase H
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