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
Language English Country Great Britain, England Media print
Document type Comparative Study, Journal Article
PubMed
3042459
DOI
10.1016/0014-5793(88)81277-8
PII: 0014-5793(88)81277-8
Knihovny.cz E-resources
- MeSH
- Aspartic Acid Endopeptidases MeSH
- Cyanogen Bromide MeSH
- Disulfides metabolism MeSH
- Endopeptidases metabolism MeSH
- Glycosylation MeSH
- Carbohydrate Metabolism * MeSH
- Molecular Sequence Data MeSH
- Mucor enzymology MeSH
- Peptide Fragments MeSH
- Amino Acid Sequence MeSH
- Base Sequence * MeSH
- Sequence Homology, Nucleic Acid * MeSH
- Serine Endopeptidases MeSH
- Trypsin MeSH
- Binding Sites MeSH
- Publication type
- Journal Article MeSH
- Comparative Study MeSH
- Names of Substances
- Aspartic Acid Endopeptidases MeSH
- Cyanogen Bromide MeSH
- Disulfides MeSH
- Endopeptidases MeSH
- glutamyl endopeptidase MeSH Browser
- Peptide Fragments MeSH
- Serine Endopeptidases MeSH
- Trypsin MeSH
The amino acid sequence of Mucor pusillus aspartic proteinase was determined by analysis of fragments obtained from cleavage of the enzyme by CNBr and limited tryptic digestion. The proteinase 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 proteinase (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.
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