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  2. Serine protease - Wikipedia

    en.wikipedia.org/wiki/Serine_protease

    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 ...

  3. Serpin - Wikipedia

    en.wikipedia.org/wiki/Serpin

    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).

  4. Subtilase - Wikipedia

    en.wikipedia.org/wiki/Subtilase

    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.

  5. Maspin - Wikipedia

    en.wikipedia.org/wiki/Maspin

    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 ...

  6. Kallikrein - Wikipedia

    en.wikipedia.org/wiki/Kallikrein

    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.

  7. Subtilisin - Wikipedia

    en.wikipedia.org/wiki/Subtilisin

    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.

  8. Clp protease family - Wikipedia

    en.wikipedia.org/wiki/CLP_protease_family

    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 ]

  9. Fibroblast activation protein, alpha - Wikipedia

    en.wikipedia.org/wiki/Fibroblast_activation...

    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 ...