Abstract
It is now quite proper to speak of an "active site" or "center" in (or on) a number of hydrolytic enzymes, chymotrypsin in particular. Such sites have been clearly demonstrated and in some cases they have even been investigated in detail. We are almost persuaded that they are the actual loci of enzyme activity in nature. Whatever we think of them, we do know that they are "some peculiar arrangement of amino acids" (2 a).
Full Text
The Full Text of this article is available as a PDF (615.9 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- BALLS A. K., JANSEN E. F. Stoichiometric inhibition of chymotrypsin. Adv Enzymol Relat Subj Biochem. 1952;13:321–343. doi: 10.1002/9780470122587.ch8. [DOI] [PubMed] [Google Scholar]
- BALLS A. K., MCDONALD C. E. Transesterification reactions catalyzed by chymotrypsin. J Biol Chem. 1956 Aug;221(2):993–1003. [PubMed] [Google Scholar]
- BALLS A. K., WOOD H. N. Acetyl chymotrypsin and its reaction with ethanol. J Biol Chem. 1956 Mar;219(1):245–256. [PubMed] [Google Scholar]
- BOYER P. D. Mechanism of enzyme action. Annu Rev Biochem. 1960;29:15–44. doi: 10.1146/annurev.bi.29.070160.000311. [DOI] [PubMed] [Google Scholar]
- Balls A. K., Aldrich F. L. ACETYL-CHYMOTRYPSIN. Proc Natl Acad Sci U S A. 1955 Apr 15;41(4):190–196. doi: 10.1073/pnas.41.4.190. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DIXON G. H., NEURATH H. Acylation of the enzymatic site of delta-chymotrypsin by esters, acid anhydrides, and acid chlorides. J Biol Chem. 1957 Apr;225(2):1049–1059. [PubMed] [Google Scholar]
- FRAENKEL-CONRAT H., BEAN R. S., LINEWEAVER H. Essential groups for the interaction of ovomucoid, egg white trypsin inhibitor, and trypsin, and for tryptic activity. J Biol Chem. 1949 Jan;177(1):385–403. [PubMed] [Google Scholar]
- HARTLEY B. S., KILBY B. A. The reaction of p-nitrophenyl esters with chymotrypsin and insulin. Biochem J. 1954 Feb;56(2):288–297. doi: 10.1042/bj0560288. [DOI] [PMC free article] [PubMed] [Google Scholar]
- JANSEN E. F., NUTTING F., JANG R., BALLS A. K. Mode of inhibition of chymotrypsin by diisopropyl fluorophosphate. II. Introduction of isopropyl and elimination of fluorine as hydrogen fluoride. J Biol Chem. 1950 Jul;185(1):209–220. [PubMed] [Google Scholar]
- Kunitz M., Northrop J. H. ISOLATION OF A CRYSTALLINE PROTEIN FROM PANCREAS AND ITS CONVERSION INTO A NEW CRYSTALLINE PROTEOLYTIC ENZYME BY TRYPSIN. Science. 1933 Dec 15;78(2033):558–559. doi: 10.1126/science.78.2033.558. [DOI] [PubMed] [Google Scholar]
- McDONALD C. E., BALLS A. K. Analogues of acetyl chymotrypsin. J Biol Chem. 1957 Aug;227(2):727–736. [PubMed] [Google Scholar]
- OOSTERBAAN R. A., KUNST P., COHEN J. A. The nature of the reaction between diisoprophylfluorophosphate and chymotrypsin. Biochim Biophys Acta. 1955 Feb;16(2):299–300. doi: 10.1016/0006-3002(55)90225-0. [DOI] [PubMed] [Google Scholar]
- OOSTERBAAN R. A., VAN ADRICHEM M. E. Isolation of acetyl peptides from acetylchymotrypsin. Biochim Biophys Acta. 1958 Feb;27(2):423–425. doi: 10.1016/0006-3002(58)90359-7. [DOI] [PubMed] [Google Scholar]
- TINOCO I., Jr The alpha-chymotrypsin catalyzed hydrolysis of ethyl lactate. Arch Biochem Biophys. 1958 Jul;76(1):148–160. doi: 10.1016/0003-9861(58)90129-2. [DOI] [PubMed] [Google Scholar]
- WEIL L., JAMES S., BUCHERT A. R. Photo-oxidation of crystalline chymotrypsin in the presence of methylene blue. Arch Biochem Biophys. 1953 Oct;46(2):266–278. doi: 10.1016/0003-9861(53)90200-8. [DOI] [PubMed] [Google Scholar]