T. Sakai et al., ISOLATION AND EXPRESSION OF THE GENE WHICH ENCODES A NOVEL ENZYME WITH POLYMETHOXYGALACTURONATE-DEGRADING ACTIVITY IN TRICHOSPORON PENICILLATUM, FEBS letters, 414(2), 1997, pp. 439-443
The novel gene named PSX1, encoding a new protopectinase with the poly
methoxygalacturonase activity, was isolated from Trichosporon penicill
atum. Nucleotide sequencing revealed that the PSX1 gene is composed of
1080 bases (360 amino acids, 38 747 Da). The N-terminal amino acid se
quences of the open reading frame correspond to a signal peptide and p
ropeptide processed by a Kex2-like proteinase. Mature PPase SX1 was co
mposed of 334 amino acids (36121 Da). PPase SX1 produced by a S. cerev
isiae transformant harbouring the PSX1 gene degraded methoxylated poly
galacturonic acid as a substrate, but not degraded unmethoxylated poly
galacturonic acid. (C) 1997 Federation of European Biochemical Societi
es.