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
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu srovnávací studie, časopisecké články
PubMed
3042459
DOI
10.1016/0014-5793(88)81277-8
PII: 0014-5793(88)81277-8
Knihovny.cz E-zdroje
- MeSH
- aspartátové endopeptidasy MeSH
- bromkyan MeSH
- disulfidy metabolismus MeSH
- endopeptidasy metabolismus MeSH
- glykosylace MeSH
- metabolismus sacharidů * MeSH
- molekulární sekvence - údaje MeSH
- Mucor enzymologie MeSH
- peptidové fragmenty MeSH
- sekvence aminokyselin MeSH
- sekvence nukleotidů * MeSH
- sekvenční homologie nukleových kyselin * MeSH
- serinové endopeptidasy MeSH
- trypsin MeSH
- vazebná místa MeSH
- Publikační typ
- časopisecké články MeSH
- srovnávací studie MeSH
- Názvy látek
- aspartátové endopeptidasy MeSH
- bromkyan MeSH
- disulfidy MeSH
- endopeptidasy MeSH
- glutamyl endopeptidase MeSH Prohlížeč
- peptidové fragmenty MeSH
- serinové endopeptidasy 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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