Selected article for: "active enzyme and cleavage site"
Title: Isolation, characterization, and expression of cDNAs encoding murine alpha-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans
  • Document date: 1991_12_2
    • ID: qrg1rtzi_31
    Snippet: In addition to the NHZ-terminal peptide sequence, the mouse equivalent of the six remaining rat Man II polypeptide sequences determined previously (30) were all found in the Man II open reading frame confirming the predicted peptide sequence map (Ref. 30, Fig . 8 ) . Chymotrypsin has been used to cleave Man II in vitro generating a soluble catalytically active form of the enzyme (28, 30) . The cleavage site is at residue 107 in the open reading f.....
    Document: In addition to the NHZ-terminal peptide sequence, the mouse equivalent of the six remaining rat Man II polypeptide sequences determined previously (30) were all found in the Man II open reading frame confirming the predicted peptide sequence map (Ref. 30, Fig . 8 ) . Chymotrypsin has been used to cleave Man II in vitro generating a soluble catalytically active form of the enzyme (28, 30) . The cleavage site is at residue 107 in the open reading frame and predicts that the cytoplasmic tail, transmembrane domain, and 80 residues of Moremen and Robbins cDNA Cloning and Expression of Golgi a-Mannosidase 11 1527 lumenally oriented polypeptide are not essential for enzyme activity.

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