Protein chemical characterization of Mucor pusillus aspartic proteinase Amino acid sequence homology with the other aspartic proteinases, disulfide bond arrangement and site of carbohydrate attachment
- 1 August 1988
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 235 (1-2) , 271-274
- https://doi.org/10.1016/0014-5793(88)81277-8
Abstract
The amino acid sequence of Mucor pusillus aspartic protenaise was determined by analysis of fragments obtained from cleavage of the enzyme by CNBr and limited tryptic digestion. The protenaise is a single polypeptide chain protein containing 361 amino acid residues, cross‐linked by two disulfide bonds. A sugar moiety composed of two GlcNAc residues and four neutral sugar residues is asparagine‐linked to the chain. The sequence of M. pusillus proteinase is highly homologous with the M. miehei protonaise (83% identity). The homology with other aspartic proteinases is low (22–24%) and indicates that the Mucor proteinases diverged at an early evolutionary phase. The most conservative regions of the molecule are those involved in catalysis and forming the binding cleft and the core region of the molecule.Keywords
This publication has 24 references indexed in Scilit:
- On the rational design of renin inhibitors: x-ray studies of aspartic proteinases complexed with transition-state analogsBiochemistry, 1987
- Structure and refinement at 1.8 Å resolution of the aspartic proteinase from Rhizopus chinensisJournal of Molecular Biology, 1987
- Primary structure of Mucor miehei aspartyl protease: evidence for a zymogen intermediateGene, 1985
- Modification of serine residues during sequential degradation of proteins and peptides by the phenylisothiocyanate methodAnalytical Biochemistry, 1985
- Peptide mapping of bovine pancreatic ribonuclease A by reverse-phase high-performance liquid chromatographyAnalytical Biochemistry, 1985
- Characterization of the sulfated glycopeptide of chicken pepsinogenCollection of Czechoslovak Chemical Communications, 1982
- Milk-clotting enzyme from microorganisms. XII. Physicochemical and immunochemical studies on similarities of acid proteases Mucor pusillus rennin and Mucor miehei rennin.Agricultural and Biological Chemistry, 1979
- Micro‐sequence analysis of peptides and proteins using 4‐NN‐dimethylaminoazobenzene 4′‐isothiocyanate/phenylisothiocyanate double coupling methodFEBS Letters, 1978
- Structural and functional determinants of Mucor miehei protease VI. Inactivation of the enzyme by diazoacetyl norleucine methyl ester, pepstatin andBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- Milk Clotting Enzyme from MicroorganismsAgricultural and Biological Chemistry, 1967