Trivalent metal complex geometry of the substrate governs cathepsin B enzymatic cleavage rate

2020 ◽  
Vol 56 (53) ◽  
pp. 7289-7292 ◽  
Author(s):  
Shin Hye Ahn ◽  
James N. Iuliano ◽  
Eszter Boros

The identity of the trivalent metal ion controls the rate of the enzymatic cleavage of a series of metal-complexed cathepsin B substrates. Increasing the distance between the metal complex and the enzyme cleavage site diminishes this effect.

2010 ◽  
Vol 25 (1) ◽  
pp. 89-95 ◽  
Author(s):  
Syed Ali Raza Naqvi ◽  
Torkjel Matzow ◽  
Ciara Finucane ◽  
Saeed A. Nagra ◽  
Malik M. Ishfaq ◽  
...  

2019 ◽  
Vol 8 (41) ◽  
Author(s):  
Hend Altaib ◽  
Yuka Ozaki ◽  
Tomoya Kozakai ◽  
Yassien Badr ◽  
Izumi Nomura ◽  
...  

A series of new Escherichia coli entry vectors (pIIS18-SapI, pIIS18-BsmBI, pIIS18-BsaI, pIIS18-BfuAI-1, and pIIS18-BfuAI-2) was constructed based on a modified pUC18 backbone, which carried newly designed multiple cloning sites, consisting of two facing type IIS enzyme cleavage sites and one blunt-end enzyme cleavage site. These vectors are useful for seamless gene cloning.


1998 ◽  
Vol 336 (1) ◽  
pp. 207-212 ◽  
Author(s):  
Caron J. BILLINGTON ◽  
Ian M. CLARK ◽  
Tim E. CAWSTON

The breakdown of aggrecan in cartilage is, in part, mediated by an enzyme named aggrecanase that cleaves within the interglobular domain of the molecule between a glutamic residue and an alanine residue. Although the enzyme cleavage site has been identified, the identity, characteristics and localization of this enzyme remain unclear. We have demonstrated that membranes isolated from stimulated chondrocytes are able to generate aggrecan fragments that are labelled by an antibody that recognizes the new N-terminus formed by aggrecanase activity. It was further shown that the membrane activity was a metalloproteinase but was not inhibited by the naturally occurring matrix metalloproteinase (MMP) inhibitors, TIMPs 1 and 2. These results show that an aggrecanase activity is associated with the membranes of the chondrocytes and is a metalloproteinase, but might not be a member of the MMP family.


Biomedicines ◽  
2021 ◽  
Vol 9 (8) ◽  
pp. 1044
Author(s):  
Qingxin Li ◽  
Congbao Kang

Zika virus (ZIKV)—a member of the Flaviviridae family—is an important human pathogen. Its genome encodes a polyprotein that can be further processed into structural and non-structural proteins. ZIKV protease is an important target for antiviral development due to its role in cleaving the polyprotein to release functional viral proteins. The viral protease is a two-component protein complex formed by NS2B and NS3. Structural studies using different approaches demonstrate that conformational changes exist in the protease. The structures and dynamics of this protease in the absence and presence of inhibitors were explored to provide insights into the inhibitor design. The dynamic nature of residues binding to the enzyme cleavage site might be important for the function of the protease. Due to the charges at the protease cleavage site, it is challenging to develop small-molecule compounds acting as substrate competitors. Developing small-molecule compounds to inhibit protease activity through an allosteric mechanism is a feasible strategy because conformational changes are observed in the protease. Herein, structures and dynamics of ZIKV protease are summarized. The conformational changes of ZIKV protease and other proteases in the same family are discussed. The progress in developing allosteric inhibitors is also described. Understanding the structures and dynamics of the proteases are important for designing potent inhibitors.


2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Robert Christie ◽  
Adrian Abel

Abstract There are several commercially significant metal complex organic pigments that are based on first row transition metals. The most important of these are the copper phthalocyanine blue and green pigments which find virtually universal use in paints, printing inks, and plastics. These pigments are of such prime importance that they are dealt with separately in three other chapters in this series. This paper describes a group of pigments that are complexes of iron, copper, nickel, and cobalt with polydentate colored ligands of azo, azomethine, oxime, and isoindoline chemical types. The oldest metal complex organic pigment that still finds some use is CI Pigment Green 8, an octahedral oxime iron complex. In the 1970s and 1980s, there was considerable industrial research effort aimed at developing metal complex pigments based on azomethine and isoindoline structures, many of which were found to offer excellent lightfastness, good solvent resistance and thermal stability, although they exhibited rather dull colors. However, several products provide brilliant effects when used in combination with metallic and pearlescent pigments in automotive paints. Many of the pigments introduced have since been withdrawn by the original manufacturers, but a few remain on the market. The synthesis of metal complex pigments generally involves the preparation of the colored ligand, which is then complexed with the transition metal ion


Sign in / Sign up

Export Citation Format

Share Document