Active Site of alpha-Lytic Protease. Enzyme-Substrate Interactions
Open Access
- 1 November 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 120 (2), 289-294
- https://doi.org/10.1111/j.1432-1033.1981.tb05702.x
Abstract
The active site of α-lytic protease has studied with a number of synthetic peptides and compared with similar data published for elastase. The kinetic data indicate that the active site of α-lytic protease extends over at least six subsites (S4-S′2. This extended active site has the effect of increasing kcat/Km by more than 106-fold on going from an N-acetylated amino acid amide to a hexapeptide, due mainly to increases in kcat. There are major differences between α-lytic protease and elastase, both in terms of the kinetic parameters for a number of substrates and in terms of the tertiary structure of the active site. The ability of the S 1 subsite to interact with various P1 amino acid side chains differs markedly between the two enzymes, and can be rationalized in terms of the tertiary structural differences. For α-lytic protease, enzyme-substrate interactions made in subsite S2 appears to be of primary importance, whereas subsite S4 is most important for elastase. The tertiary structural homology of α-lytic protease with another bacterial serine protease, Streptomyces griseus protease A, has allowed detailed model building of a tetrapeptide Ac-Pro-Ala-Pro-Ala-OH at the active site. In this way, the subsites S1-S4 have been examined for α-lytic protease and compared to other serine proteases.This publication has 30 references indexed in Scilit:
- Molecular structure of the α-lytic protease from Myxobacter 495 at 2·8 Å resolutionJournal of Molecular Biology, 1979
- The atomic structure of crystalline porcine pancreatic elastase at 2.5 Å resolution: Comparisons with the structure of α-chymotrypsinJournal of Molecular Biology, 1978
- The active centers of Streptomyces griseus protease 3 and α-chymotrypsinBiochimica et Biophysica Acta (BBA) - Enzymology, 1976
- Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1973
- Primary Structure of α-Lytic Protease: a Bacterial Homologue of the Pancreatic Serine ProteasesNature, 1970
- A comparison of properties of the α-lytic protease of Sorangium sp. and porcine elastaseCanadian Journal of Biochemistry, 1970
- Kinetic properties of the α-lytic protease of Sorangium sp., a bacterial homologue of the pancreatopeptidasesCanadian Journal of Biochemistry, 1969
- CONCERNING THE NATURE OF THE α- AND β-LYTIC PROTEASES OF SORANGIUM SP.Canadian Journal of Biochemistry, 1967
- The nature of the bacteriolytic proteases of SorangiumspBiochemical and Biophysical Research Communications, 1966
- LYTIC ENZYMES OF SORANGIUM SP.: A COMPARISON OF THE PROTEOLYTIC PROPERTIES OF THE α- AND β-LYTIC PROTEASESCanadian Journal of Biochemistry, 1965