The  ywad  gene from  Bacillus subtilis  encodes a double‐zinc aminopeptidase | Zendy

FundoianoHershcovitz Yifat | Zendy; Rabinovitch Larisa | Zendy; Shulami Smadar | Zendy; Reiland Vera | Zendy; Shoham Gil | Zendy; Shoham Yuval | Zendy

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The ywad gene from Bacillus subtilis encodes a double‐zinc aminopeptidase

Author(s) -

FundoianoHershcovitz Yifat,

Rabinovitch Larisa,

Shulami Smadar,

Reiland Vera,

Shoham Gil,

Shoham Yuval

Publication year - 2005

Publication title -

fems microbiology letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.899

H-Index - 151

eISSN - 1574-6968

pISSN - 0378-1097

DOI - 10.1016/j.femsle.2004.12.001

Subject(s) - bacillus subtilis , aminopeptidase , serine protease , enzyme , escherichia coli , zinc , biochemistry , protease , biology , enzyme kinetics , serine , gene , bacillales , chemistry , microbiology and biotechnology , amino acid , leucine , bacteria , active site , genetics , organic chemistry

The yet uncharacterized ywad gene from Bacillus subtilis has been cloned and overexpressed in Escherichia coli . The gene product (BSAP) was purified and shown to be an aminopeptidase. The activity of BSAP was optimal at pH 8.4, the enzyme was stable for 20 min at 80 °C and its activity was not affected by serine protease and aspartic protease inhibitors, but was completely diminished by the Zn‐chelator 1,10‐phenanthroline. ZnCl 2 was able to restore activity, and the binding stochiometry of zinc to apo‐BSAP indicated two Zn ions per protein molecule. BSAP exhibited high preference toward p ‐nitroanilide derived Arg, Lys, and Leu synthetic substrates resulting in k cat / K m values of 1–5 × 10 1 s −1 mM −1 .

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