Abstract
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.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Cloning, Molecular
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Enzyme Precursors / biosynthesis
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Enzyme Precursors / chemistry
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Genes, Fungal
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Glycoside Hydrolases / biosynthesis*
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Glycoside Hydrolases / chemistry
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Glycoside Hydrolases / genetics*
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Molecular Sequence Data
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Open Reading Frames
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Polysaccharide-Lyases / biosynthesis*
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Polysaccharide-Lyases / chemistry
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Polysaccharide-Lyases / genetics*
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Protein Sorting Signals / biosynthesis
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Protein Sorting Signals / chemistry
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Saccharomyces cerevisiae
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Sequence Alignment
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Sequence Homology, Amino Acid
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Substrate Specificity
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Trichosporon / enzymology*
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Trichosporon / genetics*
Substances
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Enzyme Precursors
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Protein Sorting Signals
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Glycoside Hydrolases
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protopectinase
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Polysaccharide-Lyases
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pectin lyase