Literature DB >> 6427203

Amino acid sequence around the reactive serine of cucumisin from melon fruit.

M Kaneda, H Ohmine, H Yonezawa, N Tominaga.   

Abstract

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.

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Year:  1984        PMID: 6427203     DOI: 10.1093/oxfordjournals.jbchem.a134674

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  3 in total

1.  Milk-clotting activity of cucumisin, a plant serine protease from melon fruit.

Authors:  T Uchikoba; M Kaneda
Journal:  Appl Biochem Biotechnol       Date:  1996-03       Impact factor: 2.926

2.  Macluralisin--a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid.

Authors:  G N Rudenskaya; E A Bogdanova; L P Revina; B N Golovkin; V M Stepanov
Journal:  Planta       Date:  1995       Impact factor: 4.116

3.  A serine proteinase of an archaebacterium, Halobacterium mediterranei. A homologue of eubacterial subtilisins.

Authors:  V M Stepanov; G N Rudenskaya; L P Revina; Y B Gryaznova; E N Lysogorskaya; I I Ivanova
Journal:  Biochem J       Date:  1992-07-01       Impact factor: 3.857

  3 in total

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