Amino acid sequence around the reactive serine of cucumisin from melon fruit.
Cucumisin is a diisopropyl fluorophosphate-sensitive enzyme. The inactivation by DFP is accompanied by the formation of 1 mol of labeled serine residue per mol of enzyme. From the soluble portion of the chymotryptic digest of the diisopropyl phosphoryl derivative of cucumisin, two peptides containing phosphorus were isolated; their amino acid sequences were determined to be Gly-Thr-Ser(P)-Met and Asn-Ile-Ile-Ser-Gly-Thr-Ser(P)-Met, respectively. The four residues Gly-Thr-Ser-Met in the above amino acid sequence are identical with those of subtilisin.
D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D010450:Endopeptidases / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000302:isolation & purification; D010944:Plants / Q000201:enzymology*; D012694:Serine / Q000302:isolation & purification*; D012697:Serine Endopeptidases
D010446:Peptide Fragments; D012694:Serine; D010450:Endopeptidases; D012697:Serine Endopeptidases; C041541:cucumisin