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

The Biochemical journal ·Vol. 113 ·No. 2 ·1969-06-00 ·Pages 377-86

Bayliss RS, Knowles JR, Wybrandt GB

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

MeSH Terms

Amino Acid Sequence Aspartic Acid/analysis Binding Sites Chromatography, Gel Chromatography, Paper Electrophoresis Esters Pepsin A/analysis,antagonists & inhibitors Phenylalanine

Chemicals

Esters Aspartic Acid Phenylalanine Pepsin A

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Bayliss R S

Knowles J R

Wybrandt G B

References (19)

19 references, click to expand

On the reaction of diazoacetyl compounds with pepsin.
J Biol Chem. 1969 Jan 10;244(1):154-60 PMID: 4886428
The inhibition of pepsin-catalysed reactions by products and product analogues. Kinetic evidence for ordered release of products.
Biochem J. 1969 Jun;113(2):363-8 PMID: 4897199
[Amino acid determination on paper chromatograms].
Hoppe Seylers Z Physiol Chem. 1957;309(4-6):219-20 PMID: 13513014
Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.
Biochem J. 1966 Oct;101(1):214-28 PMID: 5971783
Stereochemical investigation of the active center of pepsin using a new inactivator.
Biochem Biophys Res Commun. 1967 Jul 21;28(2):203-8 PMID: 5340731
Separation of dansyl-amino acids by polyamide layer chromatography.
Biochim Biophys Acta. 1967 Feb 21;133(2):369-70 PMID: 6029938
[Inactivation of pepsin with diazocarbonyl compounds].
Biokhimiia. 1967 Sep-Oct;32(5):1011-9 PMID: 4878120
The carboxyl-terminal sequence of porcine pepsin.
J Biol Chem. 1967 Apr 25;242(8):1833-7 PMID: 5337592
Specific inactivation of pepsin by benzyloxycarbonyl-L-phenylalanyldiazomethane.
Nature. 1967 Sep 30;215(5109):1492-4 PMID: 4861199
A reactive aspartyl residue of pepsin.
Biochem Biophys Res Commun. 1968 Mar 12;30(5):489-95 PMID: 4870410
The pH-dependence of pepsin-catalysed reactions.
Biochem J. 1969 Jun;113(2):353-62 PMID: 4897198
Specific inactivation of pepsin by a diazo ketone.
Proc Natl Acad Sci U S A. 1966 Dec;56(6):1817-22 PMID: 16591425
The inactivation of pepsin by an equimolar amount of 1-diazo-4-phenylbutanone-2.
Biochem Biophys Res Commun. 1967 Jan 23;26(2):193-8 PMID: 5339943
The pH-dependence of the binding of competitive inhibitors to pepsin.
Biochem J. 1969 Jun;113(2):343-51 PMID: 4897197
Pepsin from pepsinogen. Preparation and properties.
J Biol Chem. 1966 Nov 10;241(21):4940-50 PMID: 5332666
Inactivation of pepsin by diphenyldiazomethane.
Proc Natl Acad Sci U S A. 1965 Oct;54(4):1161-7 PMID: 5327254
Identification of the carboxyl group of pepsin reacting with diazoacetamide derivatives.
Biochem Biophys Res Commun. 1968 Jun 10;31(5):825-30 PMID: 4874970
Studies on the specificity of pepsin.
Biochemistry. 1967 Jun;6(6):1765-77 PMID: 5340947
The inactivation of invertase by tyrosinase. II. The influence of copper and gold on the oxidation of invertase and pepsin.
J Biol Chem. 1951 Jan;188(1):351-9 PMID: 14814145

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1130377

Published

1969-06-00

Pages

377-86

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1184645

Subset

External Links

PubMed source DOI: 10.1042/bj1130377 PMC Full Text View journal details

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

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