Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1971 Aug;124(1):13–18. doi: 10.1042/bj1240013

Catalytic activity of α-chymotrypsin in which histidine-57 has been methylated

R Henderson 1,*
PMCID: PMC1177107  PMID: 5126468

Abstract

The properties of a derivative of α-chymotrypsin in which histidine-57 has been methylated have been examined. Although the modified enzyme binds substrate with the same affinity as does native α-chymotrypsin, acylation and deacylation occur at much decreased rates. As for native α-chymotrypsin, a basic group of pKa approx. 7 is involved in both acylation and deacylation. The significance of these results is considered in relation to the normal function of histidine-57.

Full text

PDF
13

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BERHARD S. A., TASHJIAN Z. H. ACYL INTERMEDIATES IN THE ALPHA-CHYMOTRYPSIN-CATALYZED HYDROLYSIS OF INDOLEACRYLOYLIMIDAZOLE. J Am Chem Soc. 1965 Apr 20;87:1806–1807. doi: 10.1021/ja01086a042. [DOI] [PubMed] [Google Scholar]
  2. Bernhard S. A., Lee B. F., Tashjian Z. H. On the interaction of the active side of alpha-chymotrypsin with chromophores: proflavin binding and enzyme conformation during catalysis. J Mol Biol. 1966 Jul;18(3):405–420. doi: 10.1016/s0022-2836(66)80033-5. [DOI] [PubMed] [Google Scholar]
  3. Blow D. M., Birktoft J. J., Hartley B. S. Role of a buried acid group in the mechanism of action of chymotrypsin. Nature. 1969 Jan 25;221(5178):337–340. doi: 10.1038/221337a0. [DOI] [PubMed] [Google Scholar]
  4. Charney E., Bernhard S. A. Optical properties and the chemical nature of acyl-chymotrypsin linkages. J Am Chem Soc. 1967 May 24;89(11):2726–2733. doi: 10.1021/ja00987a040. [DOI] [PubMed] [Google Scholar]
  5. GOLD A. M., FAHRNEY D. SULFONYL FLUORIDES AS INHIBITORS OF ESTERASES. II. FORMATION AND REACTIONS OF PHENYLMETHANESULFONYL ALPHA-CHYMOTRYPSIN. Biochemistry. 1964 Jun;3:783–791. doi: 10.1021/bi00894a009. [DOI] [PubMed] [Google Scholar]
  6. KNOWLES J. R. THE ROLE OF METHIONINE IN ALPHA-CHYMOTRYPSIN-CATALYSED REACTIONS. Biochem J. 1965 Apr;95:180–190. doi: 10.1042/bj0950180. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. KOSHLAND D. E., Jr, STRUMEYER D. H., RAY W. J., Jr Amino acids involved in the action of chymotrypsin. Brookhaven Symp Biol. 1962 Dec;15:101–133. [PubMed] [Google Scholar]
  8. Matthews B. W., Sigler P. B., Henderson R., Blow D. M. Three-dimensional structure of tosyl-alpha-chymotrypsin. Nature. 1967 May 13;214(5089):652–656. doi: 10.1038/214652a0. [DOI] [PubMed] [Google Scholar]
  9. Nakagawa Y., Bender M. L. Methylation of histidine-57 in alpha-chymotrypsin by methyl p-nitrobenzenesulfonate. A new approach to enzyme modification. Biochemistry. 1970 Jan 20;9(2):259–267. doi: 10.1021/bi00804a011. [DOI] [PubMed] [Google Scholar]
  10. Nakagawa Y., Bender M. L. Modification of alpha-chymotrypsin by methyl p-nitrobenzenesulfonate. J Am Chem Soc. 1969 Mar 12;91(6):1566–1567. doi: 10.1021/ja01034a068. [DOI] [PubMed] [Google Scholar]
  11. Oppenheimer H. L., Labouesse B., Hess G. P. Implication of an ionizing group in the control of conformation and activity of chymotrypsin. J Biol Chem. 1966 Jun 10;241(11):2720–2730. [PubMed] [Google Scholar]
  12. SCHOELLMANN G., SHAW E. Direct evidence for the presence of histidine in the active center of chymotrypsin. Biochemistry. 1963 Mar-Apr;2:252–255. doi: 10.1021/bi00902a008. [DOI] [PubMed] [Google Scholar]
  13. Sigler P. B., Blow D. M., Matthews B. W., Henderson R. Structure of crystalline -chymotrypsin. II. A preliminary report including a hypothesis for the activation mechanism. J Mol Biol. 1968 Jul 14;35(1):143–164. doi: 10.1016/s0022-2836(68)80043-9. [DOI] [PubMed] [Google Scholar]
  14. Steitz T. A., Henderson R., Blow D. M. Structure of crystalline alpha-chymotrypsin. 3. Crystallographic studies of substrates and inhibitors bound to the active site of alpha-chymotrypsin. J Mol Biol. 1969 Dec 14;46(2):337–348. doi: 10.1016/0022-2836(69)90426-4. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES