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Isolation and expression of the gene which encodes a novel enzyme with polymethoxygalacturonate‐degrading activity in Trichosporon penicillatum
Author(s) -
Taku Sakai,
Naoki Sirasaka,
Haruka Hirano,
Masao Kishida,
Haruhiko Kawasaki
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01032-6
Subject(s) - open reading frame , gene , amino acid , signal peptide , biochemistry , peptide sequence , enzyme , biology , heterologous expression , nucleic acid sequence , saccharomyces cerevisiae , peptide , microbiology and biotechnology , chemistry , recombinant dna
The novel gene named PSX1 , encoding a new protopectinase with the polymethoxygalacturonase activity, was isolated from Trichosporon penicillatum . Nucleotide sequencing revealed that the PSX1 gene is composed of 1080 bases (360 amino acids, 38 747 Da). The N ‐terminal amino acid sequences of the open reading frame correspond to a signal peptide and propeptide processed by a Kex2‐like proteinase. Mature PPase SX1 was composed of 334 amino acids (36 121 Da). PPase SX1 produced by a S. cerevisiae transformant harboring the PSX1 gene degraded methoxylated polygalacturonic acid as a substrate, but not degraded unmethoxylated polygalacturonic acid.