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Literature DB >> 4897201

An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide.

Abstract

Pepsin reacts stoicheiometrically with the active-site-directed irreversible inhibitor N-diazoacetyl-l-phenylalanine methyl ester, with concomitant loss of all proteolytic and peptidolytic activity. The reagent esterifies a unique aspartic acid residue in pepsin, which is in the sequence:Ile-Val-Asp-Thr-Gly-Thr-Ser

Entities: Chemical Gene

Mesh：

Substances：

Year: 1969 PMID： 4897201 PMCID： PMC1184645 DOI： 10.1042/bj1130377

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

19 in total

1. [Amino acid determination on paper chromatograms].

Authors: J HEILMANN; J BARROLLIER; E WATZKE
Journal: Hoppe Seylers Z Physiol Chem Date: 1957

2. On the reaction of diazoacetyl compounds with pepsin.

Authors: R L Lundblad; W H Stein
Journal: J Biol Chem Date: 1969-01-10 Impact factor: 5.157

3. A reactive aspartyl residue of pepsin.

Authors: K T Fry; O K Kim; C F Kettering; J Spona; G A Hamilton
Journal: Biochem Biophys Res Commun Date: 1968-03-12 Impact factor: 3.575

4. [Inactivation of pepsin with diazocarbonyl compounds].

Authors: L V Kozlov; L M Ginodman; V N Orekhovich
Journal: Biokhimiia Date: 1967 Sep-Oct

5. Specific inactivation of pepsin by benzyloxycarbonyl-L-phenylalanyldiazomethane.

Authors: E B Ong; G E Perlmann
Journal: Nature Date: 1967-09-30 Impact factor: 49.962

6. Stereochemical investigation of the active center of pepsin using a new inactivator.

Authors: B F Erlanger; S M Vratsanos; N Wassermann; A G Cooper
Journal: Biochem Biophys Res Commun Date: 1967-07-21 Impact factor: 3.575

7. The carboxyl-terminal sequence of porcine pepsin.

Authors: T A Dopheide; S Moore; W H Stein
Journal: J Biol Chem Date: 1967-04-25 Impact factor: 5.157

8. Separation of dansyl-amino acids by polyamide layer chromatography.

Authors: K R Woods; K T Wang
Journal: Biochim Biophys Acta Date: 1967-02-21

9. The inhibition of pepsin-catalysed reactions by products and product analogues. Kinetic evidence for ordered release of products.

Authors: P Greenwell; J R Knowles; H Sharp
Journal: Biochem J Date: 1969-06 Impact factor: 3.857

10. Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.

Authors: J R Brown; B S Hartley
Journal: Biochem J Date: 1966-10 Impact factor: 3.857

19 in total

10. Inhibition of cathepsin D-type proteinase of macrophages by pepstatin, a specific pepsin inhibitor, and other substances.

Authors: M H McAdoo; A M Dannenberg; C J Hayes; S P James; J H Sanner
Journal: Infect Immun Date: 1973-04 Impact factor: 3.441

An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide.

1. [Amino acid determination on paper chromatograms].

2. On the reaction of diazoacetyl compounds with pepsin.

3. A reactive aspartyl residue of pepsin.

4. [Inactivation of pepsin with diazocarbonyl compounds].

5. Specific inactivation of pepsin by benzyloxycarbonyl-L-phenylalanyldiazomethane.

6. Stereochemical investigation of the active center of pepsin using a new inactivator.

7. The carboxyl-terminal sequence of porcine pepsin.

8. Separation of dansyl-amino acids by polyamide layer chromatography.

9. The inhibition of pepsin-catalysed reactions by products and product analogues. Kinetic evidence for ordered release of products.

10. Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.

Review 1. Diazo Compounds: Versatile Tools for Chemical Biology.

2. Digestive enzymes secreted by the carnivorous plant Nepenthes macferlanei L.

3. The effect of acid proteinase inhibitors on chicken pepsin.

4. Chemical modification of cellulase from Aspergillus niger.

5. Amino-acid sequence of porcine pepsin.

Review 6. Strategy and tactics in protein chemistry.

7. The comparative specificity of acid proteinases.

8. Bovine pepsinogens and pepsins. The sequence around a reactive aspartyl residue.

9. Bifunctional inhibitors of pepsin.

10. Inhibition of cathepsin D-type proteinase of macrophages by pepstatin, a specific pepsin inhibitor, and other substances.