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Molecular Characterization of the Poly(3‐hydroxybutyrate) Depolymerase Gene from Penicillium funiculosum
Author(s) -
Kasuya Kenichi,
Tezuka Yoko,
Ishii Nariaki,
Yamagata Yoko,
Shiraki Mari,
Saito Terumi,
Hisano Tamao,
Iwata Tadahisa,
Doi Yoshiharu
Publication year - 2007
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.200750433
Subject(s) - edman degradation , complementary dna , linker , open reading frame , cdna library , amino acid , microbiology and biotechnology , peptide sequence , biology , gene , peptide , homology (biology) , chemistry , biochemistry , computer science , operating system
A cDNA encoding Penicillium funiculosum P(3HB) depolymerase (PhaZ Pfu ) was cloned from a cDNA library. This cDNA contained a 1,020‐bp open reading frame (ORF) that encoded 339 amino acids. Edman degradation of PhaZ Pfu indicated that 20 amino acids from the N terminus function as a signal peptide. Homology analysis revealed that PhaZ Pfu lacks linker and substrate‐binding domains, both of which are observed in bacterial P(3HB) depolymerases. This may account for a weak binding affinity of PhaZ Pfu to the P(3HB) surface.