Isolation and Primary Structural Analysis of Two Conjugated Polyketone Reductases from Candida parapsilosis
Author(s) -
Aklani-Rose G.D. HIDALGO,
Muhammad Ali Akond,
Keiko Kita,
Michihiko Kataoka,
Sakayu Shimizu
Publication year - 2001
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.65.2785
Subject(s) - candida parapsilosis , conjugated system , amino acid residue , biochemistry , enzyme , amino acid , structural similarity , chemistry , active site , protein primary structure , isolation (microbiology) , antifungal , biology , peptide sequence , gene , microbiology and biotechnology , organic chemistry , polymer
Two conjugated polyketone reductases (CPRs) were isolated from Candida parapsilosis IFO 0708. The primary structures of CPRs (C1 and C2) were analyzed by amino acid sequencing. The amino acid sequences of both enzymes had high similarity to those of several proteins of the aldo-keto-reductase (AKR) superfamily. However, several amino acid residues in the putative active sites of AKRs were not conserved in CPRs-C1 and -C2.
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