Conversion of the Cleavage Specificity of Subtilisin YaB on Oxidized Insulin Chains to an Elastase-like Specificity by Replacement of Gly124 with Ala | Zendy

HuiChing Mei | Zendy; Ywan-Feng Li | Zendy; Chi-Cheng Hsu | Zendy; Ying-Chieh Tsai | Zendy; Hiroshi Takagi | Zendy

Open Access

Conversion of the Cleavage Specificity of Subtilisin YaB on Oxidized Insulin Chains to an Elastase-like Specificity by Replacement of Gly124 with Ala

Author(s) -

HuiChing Mei,

Ywan-Feng Li,

Chi-Cheng Hsu,

Ying-Chieh Tsai,

Hiroshi Takagi

Publication year - 2003

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.67.1601

Subject(s) - subtilisin , cleavage (geology) , chemistry , mutant , elastase , hydrolysis , pancreatic elastase , biochemistry , stereochemistry , enzyme , biology , gene , paleontology , fracture (geology)

Replacement of Gly124 on the S1 pocket of subtilisin YaB with Ala changed the cleavage pattern on oxidized insulin B-chain from the subtilisin type to the elastase type. The initial cleavage site in the B-chain shifted from L15-Y16 for wild-type YaB to A14-L15 for the G124A mutant. Upon complete hydrolysis with the G124A mutant, four of the six major cleavage sites on the B-chain were identical to porcine pancreatic elastase cleavage sites.

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