Isolation and expression of the gene which encodes a novel enzyme with polymethoxygalacturonate-degrading activity in Trichosporon penicillatum

FEBS Lett. 1997 Sep 8;414(2):439-43. doi: 10.1016/s0014-5793(97)01032-6.

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.

Publication types

  • Comparative Study

MeSH terms

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

Substances

  • Enzyme Precursors
  • Protein Sorting Signals
  • Glycoside Hydrolases
  • protopectinase
  • Polysaccharide-Lyases
  • pectin lyase