Ad
related to: serine protease family structure
Search results
Results From The WOW.Com Content Network
Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. [1] They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like ...
Serpins are a superfamily of proteins with similar structures that were first identified for their protease inhibition activity and are found in all kingdoms of life. [1] [2] The acronym serpin was originally coined because the first serpins to be identified act on chymotrypsin-like serine proteases (serine protease inhibitors).
They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like in the trypsin serine proteases. The structure of proteins in this family shows that they have an alpha/beta fold containing a 7-stranded parallel beta sheet. The subtilisin family is the second largest serine protease family characterised to date.
Serpins have a complex structure, a key component of which is the reactive site loop, RSL. [10] Inhibitory serpins transition between a stress and relaxed stage. The catalytic serine residue in the protease target attacks the stressed conformation of the RSL loop to form an acyl intermediate. The loop then undergoes a conformational change to ...
Kallikreins are a subgroup of serine proteases, enzymes capable of cleaving peptide bonds in proteins. In humans, plasma kallikrein (encoded by KLKB1 gene) has no known paralogue, while tissue kallikrein-related peptidases (KLKs) encode a family of fifteen closely related serine proteases.
The structure of subtilisin has been determined by X-ray crystallography. The mature form is a 275-residue globular protein with several alpha-helices , and a large beta-sheet . The N-terminal contains an I9 propeptide domain ( InterPro : IPR010259 ) that assists the folding of subtilisin.
In molecular biology, the CLP protease family is a family of serine peptidases belong to the MEROPS peptidase family S14 (ClpP endopeptidase family, clan SK). ClpP is an ATP -dependent protease that cleaves a number of proteins , such as casein and albumin . [ 1 ]
14089 Ensembl ENSG00000078098 ENSMUSG00000000392 UniProt Q12884 P97321 RefSeq (mRNA) NM_001291807 NM_004460 NM_007986 RefSeq (protein) NP_001278736 NP_004451 NP_032012 Location (UCSC) Chr 2: 162.17 – 162.25 Mb Chr 2: 62.33 – 62.4 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Fibroblast activation protein alpha (FAP-alpha) also known as prolyl endopeptidase FAP is an enzyme that ...