Description

IPR025661 is a Cysteine peptidase, asparagine active site.

<p>Thiol (cysteine) proteases (EC 3.4.22.-) [[cite:PUB00000685]] are a family of proteolytic enzymes which contain an active site cysteine. Catalysis proceeds through a thioester intermediate and is facilitated by a nearby histidine side chain; an asparagine completes the essential catalytic triad.</p> <p>Cysteine peptidases have characteristic molecular topologies, which can be seen not only in their three-dimensional structures, but commonly also in the two-dimensional structures. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins which are evolutionary related), and further sub-divided into families, on the basis of the architecture of their catalytic dyad (cysteine-histidene) or triad [[cite:PUB00011704]].</p> <p>Modification of the catalytic triad, especially of its first amino acid (cysteine), has been postulated as a suitable target for a chemical modulation of enzyme function. This is the case for silicateins, where the cysteine residue has been replaced by a serine [[cite:PUB00057831]]. Silicateins represent a group of enzymes possessing bi-functional activity; in addition to the silica-condensing activity, they possess a proteolytic (cathepsin-like) activity [[cite:PUB00057832]].</p> <p>The sequences around the three active site residues are well conserved. This entry represents the asparagine active site. The catalytic triad consists of this entry, [interpro:IPR000169] and [interpro:IPR025660]. This catalytic triad detects mainly proteases of the C1 family, including papain and several cathepsins.</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 55

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: