1993
DOI: 10.1093/oxfordjournals.jbchem.a123991
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Zinc Protease of Bacillus subtilis var. amylosacchariticus: Construction of a Three-Dimensional Model and Comparison with Thermolysin

Abstract: The active site structure of the Zn-containing neutral protease from Bacillus subtilis var. amylosacchariticus (BANP) was predicted by computer-aided modeling on the basis of the three-dimensional structure of thermolysin (TLN). As expected from the high homology in amino acid sequence of the two enzymes, the overall folding of BANP was very similar to that of TLN. Glu144, Tyr158, and His228 of BANP were located near the active site Zn ion, to which three amino acid residues, His143, His147, and Glu167, were c… Show more

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Cited by 7 publications
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“…3), and similar structures have been predicted for the enzymes from Bacillus stearothermophillus (NPrSte), 1 (4) Ba-cillus subtilis (5), and B. subtilis var. amylosacchariticus (6).…”
mentioning
confidence: 99%
“…3), and similar structures have been predicted for the enzymes from Bacillus stearothermophillus (NPrSte), 1 (4) Ba-cillus subtilis (5), and B. subtilis var. amylosacchariticus (6).…”
mentioning
confidence: 99%