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Literature DB >> 5529715

The susceptibility of N-acetyl-S-alkyl- and N-acetyl-S-aryl-cysteine ethyl esters to chymotryptic hydrolysis.

Abstract

1. The preparation of the ethyl esters of some N-acetyl-S-alkyl- and N-acetyl-S-aryl-cysteine derivatives is described. 2. Kinetic parameters for the hydrolysis of these esters by chymotrypsin are reported. 3. The results are discussed in terms of the mechanism of action of chymotrypsin and also with reference to the possible application to sequence studies of cysteine-containing proteins.

Entities: Chemical

Mesh：

Substances：

Year: 1970 PMID： 5529715 PMCID： PMC1179250 DOI： 10.1042/bj1180553

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

10 in total

1. SPECIFICITY OF PEPTIDASES. HYDROLYSIS BY TRYPSIN, PAPAIN AND CATHEPSIN B OF SUBSTRATES CONTAINING LYSINE, 4-THIALYSINE OR 4-OXALYSINE.

Authors: G I TESSER; R J NIVARD; M GRUBER
Journal: Biochim Biophys Acta Date: 1964-08-26

2. THE PRIMARY SPECIFICITY OF ALPHA-CHYMOTRYPSIN. ACYLATED AMINO ACID ESTERS WITH NORMAL ALKYL SIDE CHAINS.

Authors: J B JONES; T KUNITAKE; C NIEMANN; G E HEIN
Journal: J Am Chem Soc Date: 1965-04-20 Impact factor: 15.419

3. The structure of ribonuclease. II. The preparation, separation, and relative alignment of large enzymatically produced fragments.

Authors: R R REDFIELD; C B ANFINSEN
Journal: J Biol Chem Date: 1956-07 Impact factor: 5.157

4. A new synthetic substrate for trypsin and its application to the determination of the amino-acid sequence of proteins.

Authors: H LINDLEY
Journal: Nature Date: 1956-09-22 Impact factor: 49.962

2 in total

Review 1. Theories of enzyme specificity and their application to proteases and aminoacyl-transfer RNA synthetases.

Authors: H R Bosshard
Journal: Experientia Date: 1976-08-15

2. The hydrolysis by thermolysin of dipeptide derivatives that conatin substituted cysteine.

Authors: A P Damoglou; H Lindley; I W Stapleton
Journal: Biochem J Date: 1971-07 Impact factor: 3.857

2 in total

The susceptibility of N-acetyl-S-alkyl- and N-acetyl-S-aryl-cysteine ethyl esters to chymotryptic hydrolysis.

1. SPECIFICITY OF PEPTIDASES. HYDROLYSIS BY TRYPSIN, PAPAIN AND CATHEPSIN B OF SUBSTRATES CONTAINING LYSINE, 4-THIALYSINE OR 4-OXALYSINE.

2. THE PRIMARY SPECIFICITY OF ALPHA-CHYMOTRYPSIN. ACYLATED AMINO ACID ESTERS WITH NORMAL ALKYL SIDE CHAINS.

3. The structure of ribonuclease. II. The preparation, separation, and relative alignment of large enzymatically produced fragments.

4. A new synthetic substrate for trypsin and its application to the determination of the amino-acid sequence of proteins.

5. A method for the specific proteolytic cleavage of protein chains.

6. The synthesis of cysteine-(cystine-) tyrosine peptides and the action thereon of crystalline pepsin.

7. Role of a buried acid group in the mechanism of action of chymotrypsin.

8. The study of alpha-chymotrypsin by x-ray diffraction. The Third CIBA Medal Lecture.

9. Enzyme specificity: alpha-chymotrypsin.

10. KINETICS OF NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENATION BY HUMAN PLACENTA.

Review 1. Theories of enzyme specificity and their application to proteases and aminoacyl-transfer RNA synthetases.

2. The hydrolysis by thermolysin of dipeptide derivatives that conatin substituted cysteine.