THE ACTIVE SITE OF AN INDUCIBLE ARYLACYLAMIDASE FROM PSEUDOMONAS ACIDOVORANS
- 12 January 1978
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 11 (1) , 59-64
- https://doi.org/10.1111/j.1399-3011.1978.tb02821.x
Abstract
Though very effectively ibhibited by both SH-group directed reagents and inhibitors typical for serine hydrolases, the inducible arylacylamidase from Pseudomonas acidovorans is a serine enzyme rather than a sulfhydryl enzyme. The amino acid sequence around the reactive serine residue is Gly-Ser-Ile. The sequence of a larger peptide from the active site is described.Keywords
This publication has 21 references indexed in Scilit:
- Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersionBiochemistry, 1972
- Size and shape of bovine serum albumin in acidic water-dioxane mixturesJournal of the American Chemical Society, 1970
- Computed circular dichroism spectra for the evaluation of protein conformationBiochemistry, 1969
- Subunit interactions in the conformational change of horse apohemoglobin on binding of heminJournal of Molecular Biology, 1968
- Evaluation of conformational changes in chemically modified bovine serum albumins on a column of sephadexBiochimica et Biophysica Acta (BBA) - General Subjects, 1966
- Dynamic Viscoelastic Properties of Solutions of Paramyosin and Bovine Serum AlbuminJournal of the American Chemical Society, 1965
- The Ultraviolet Circular Dichroism of Polypeptides1Journal of the American Chemical Society, 1965
- New Cotton Effects in Polypeptides and ProteinsJournal of the American Chemical Society, 1962
- Bovine Serum Albumin in Water-Dioxane MixturesJournal of the American Chemical Society, 1962
- Molecular structural effects produced in proteins by reaction with succinic anhydrideBiochimica et Biophysica Acta, 1958