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sedolisin

 
National Institutes of Health

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Broader (1)

Carboxypeptidase

Papers overview

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2014
2014
Computer Simulations Of Enzymes
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2013
2013
Chapter 735 – Sedolisin
 
2011
2011
Clarification of the mechanism of acylation reaction and origin of substrate specificity of the serine-carboxyl peptidase sedolisin through QM/MM free energy simulations.
Quantum mechanical/molecular mechanical (QM/MM) free energy simulations are applied for understanding the mechanism of the… Expand
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2008
2008
Prosegment of Tripeptidyl Peptidase I Is a Potent, Slow-binding Inhibitor of Its Cognate Enzyme*
Tripeptidyl peptidase I (TPP I) is the first mammalian representative of a family of pepstatin-insensitive serine-carboxyl… Expand
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2006
2006
Molecular Modeling the Reaction Mechanism of Serine-Carboxyl Peptidases.
We performed molecular modeling on the mechanism of serine-carboxyl peptidases, a novel class of enzymes active at acidic pH and… Expand
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Highly Cited
2006
Highly Cited
2006
Sedolisins, a New Class of Secreted Proteases from Aspergillus fumigatus with Endoprotease or Tripeptidyl-Peptidase Activity at Acidic pHs
ABSTRACT The secreted proteolytic activity of Aspergillus fumigatus is of potential importance as a virulence factor and in the… Expand
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2005
2005
Grifolisin, a member of the sedolisin family produced by the fungus Grifola frondosa.
The pepstatin-insensitive carboxyl proteinase grifolisin was purified from fruiting bodies of the fungus Grifola frondosa, a… Expand
2004
2004
Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate.
High-resolution crystallographic analysis of a complex of the serine-carboxyl proteinase sedolisin with pseudo-iodotyrostatin… Expand
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Review
2003
Review
2003
Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.
Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they are… Expand
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2003
2003
A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases
BackgroundTripeptidyl-peptidase I, also known as CLN2, is a member of the family of sedolisins (serine-carboxyl peptidases). In… Expand
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