aspartic proteinase

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'aspartic proteinase' can also refer to...

aspartic proteinase

Aspartic Proteinase Phylogeny and the Origin of Pregnancy-Associated Glycoproteins

Altered adherence in strains of Candida albicans harbouring null mutations in secreted aspartic proteinase genes

Effect of N-linked glycosylation on the aspartic proteinase porcine pepsin expressed from Pichia pastoris

Pepstatin A, an Aspartic Proteinase Inhibitor, Suppresses RANKL-Induced Osteoclast Differentiation

Cloning and characterization of Sapp2p, the second aspartic proteinase isoenzyme from Candida parapsilosis

Temperature-related expression of the vacuolar aspartic proteinase (APR1) gene and β-N-acetylglucosaminidase (HEX1) gene during Candida albicans morphogenesis

Replacements of Amino Acid Residues at Subsites and Their Effects on the Catalytic Properties of Rhizomucor pusillus Pepsin, an Aspartic Proteinase from Rhizomucor pusillus

Comparative modelling and analysis of amino acid substitutions suggests that the family of pregnancy-associated glycoproteins includes both active and inactive aspartic proteinases

Protein engineering loops in aspartic proteinases: site-directed mutagenesis, biochemical characterization and X-ray analysis of chymosin with a replaced loop from rhizopuspepsin

Purification and molecular cloning of aspartic proteinases from the stomach of adult Japanese fire belly newts, Cynops pyrrhogaster

Extensive Expansion of A1 Family Aspartic Proteinases in Fungi Revealed by Evolutionary Analyses of 107 Complete Eukaryotic Proteomes

Molecular cloning of an extracellular aspartic proteinase from Rhizopus microsporus and evidence for its expression during infection

Virulence of an aspergillopepsin-deficient mutant of Aspergillus fumigatus and evidence for another aspartic proteinase linked to the fungal cell wall

Involvement of a residue at position 75 in the catalytic mechanism of a fungal aspartic proteinase, Rhizomucor pusilus pepsin. Replacement of tyrosine 75 on the flap by asparagine enhances catalytic efficiency


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Quick Reference

Any endopeptidase that contains an aspartyl residue that is essential for catalytic activity. Examples include pepsin, renin, rennin, and HIV protease.

Subjects: Chemistry.

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