Novel Leu-Lys-specific peptidase (Leulysin) produced by gel-entrapped yeast cells.
Saccharomyces cerevisiae cells entrapped with a neutral hydrophilic photo-crosslinkable resin prepolymers specifically excreted into a cultured medium a new type of a peptidase, which cleaved Leu-Lys bond of alpha-mating factor. The enzyme was purified by membrane filtration followed by ion exchange chromatography and gel filtration chromatography. The purified enzyme showed a strict substrate specificity on internal Leu-Lys bond. Leu-Lys bond near terminus of a molecule and Leu-X and X-Lys bonds examined so far were not hydrolyzed by the enzyme.
D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D007930:Leucine; D008239:Lysine; D000072235:Mating Factor; D008970:Molecular Weight; D010455:Peptides / Q000378:metabolism; D011092:Polyethylene Glycols; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
C052689:ENT 2000 resin; D010455:Peptides; D011092:Polyethylene Glycols; D000072235:Mating Factor; D010450:Endopeptidases; C052688:leulysin; D007930:Leucine; D008239:Lysine