Skip to search formSkip to main content
You are currently offline. Some features of the site may not work correctly.

rhizopuspepsin

Known as: Rhizopus carboxyl proteinase, rhizopepsin, Rhizopus chinensis aspartic protease 
 
National Institutes of Health

Related topics

Related topics

1 relation

Broader (1)

Aspartic Acid Endopeptidases

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2009
2009
Recombinant immobilized rhizopuspepsin as a new tool for protein digestion in hydrogen/deuterium exchange mass spectrometry.
Hydrogen/deuterium (H/D) exchange coupled to mass spectrometry is nowadays routinely used to probe protein interactions or… Expand
  • figure 1
  • figure 2
  • figure 3
  • table 1
  • table 1
Is this relevant?
2009
2009
Purification and characterization of a new Rhizopuspepsin from Rhizopus oryzae NBRC 4749.
A secretory aspartic protease (also termed as rhizopuspepsin) was purified from Rhizopus oryzae NBRC 4749 by ion exchange… Expand
  • table 1
  • figure 2
  • figure 1
  • figure 3
  • figure 5
Is this relevant?
1995
1995
Engineering the substrate specificity of rhizopuspepsin: the role of Asp 77 of fungal aspartic proteinases in facilitating the cleavage of oligopeptide substrates with lysine in P1.
Rhizopuspepsin and other fungal aspartic proteinases are distinct from the mammalian enzymes in that they are able to cleave… Expand
Is this relevant?
Highly Cited
1993
Highly Cited
1993
Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design.
Cathepsin D (EC 3.4.23.5) is a lysosomal protease suspected to play important roles in protein catabolism, antigen processing… Expand
  • figure 1
  • figure 2
  • table 1
Is this relevant?
1992
1992
pH dependence of kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants.
The pH dependence of the kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants has been… Expand
  • table 11
  • figure 1
  • table I
  • table I
  • figure 2
Is this relevant?
1990
1990
X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
The molecular structure of endothiapepsin (EC 3.4.23.6), the aspartic proteinase from Endothia parasitica, has been refined to a… Expand
Is this relevant?
1989
1989
Construction of side-chains in homology modelling. Application to the C-terminal lobe of rhizopuspepsin.
A detailed and rule-based side-chain modelling procedure for globular proteins is presented. It uses the conformational… Expand
Is this relevant?
1988
1988
Isolation and sequencing of a genomic clone encoding aspartic proteinase of Rhizopus niveus.
A gene encoding Rhizopus niveus aspartic proteinase was isolated from an R. niveus genomic library by using oligonucleotides… Expand
Is this relevant?
1987
1987
Amino acid sequence of rhizopuspepsin isozyme pI 5.
The complete amino acid sequence of an aspartic protease from Rhizopus chinensis, rhizopuspepsin isozyme pI 5, has been… Expand
Is this relevant?
1982
1982
Purification and characterization of rhizopuspepsin isozymes from a liquid culture of Rhizopus chinensis.
1. Rhizopuspepsin has been purified from liquid cultures of Rhizopus chinensis. 2. Purification by ammonium sulfate precipitation… Expand
Is this relevant?
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy, Terms of Service, and Dataset License
ACCEPT & CONTINUE