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Matches in DBpedia 2014 for { <http://dbpedia.org/resource/Subtilase> ?p ?o. }

• Subtilase abstract "Subtilases are a family of subtilisin-like serine proteases. 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. Over 200 subtilases are presently known, more than 170 of which with their complete amino acid sequence. Subtilase is widespread, being found in eubacteria, archaebacteria, eukaryotes and viruses. The vast majority of the family are endopeptidases, although there is an exopeptidase, tripeptidyl peptidase. Structures have been determined for several members of the subtilisin family showing that subtilisins exploit the same catalytic triad as the chymotrypsins although the residues occur in a different order (His/Asp/Ser in chymotrypsin and Asp/His/Ser in subtilisin); otherwise the structures show similarity to no other proteins. Some subtilisins are mosaic proteins, whereas others contain N- and C-terminal extensions that show no sequence similarity to any other known protein. Based on sequence homology, a subdivision into six families has been proposed.The proprotein-processing endopeptidases kexin, furin and related enzymes form a distinct subfamily known as the kexin subfamily (S8B). These preferentially cleave C-terminally to paired basic amino acids. Members of this subfamily can be identified by subtly different motifs around the active site. Members of the kexin family, along with endopeptidases R, T and K from the yeast Tritirachium and cuticle-degrading peptidase from Metarhizium, require thiol activation. This can be attributed to the presence of Cys-173 near to the active histidine. Only 1 viral member of the subtilisin family is known, a 56-kDa protease from herpes virus 1, which infects the channel catfish.Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features of these enzymes are a unique catalytic triad, Ser/Glu/Asp, as well as the presence of an aspartic acid residue in the oxyanion hole. High-resolution crystal structures have now been solved for sedolisin from Pseudomonas sp. 101, as well as for kumamolisin from a thermophilic bacterium, Bacillus novo sp. MN-32. Mutations in the human gene leads to a fatal neurodegenerative disease.".
• Subtilase symbol "Peptidase_S8".
• Subtilase thumbnail PDB_1cse_EBI.jpg?width=300.
• Subtilase wikiPageID "24009802".
• Subtilase wikiPageRevisionID "593104889".
• Subtilase caption "Structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis.".
• Subtilase cdd "cd00306".
• Subtilase hasPhotoCollection Subtilase.
• Subtilase interpro "IPR000209".
• Subtilase merops "S8".
• Subtilase name "Subtilase family".
• Subtilase pdb "A:134-391 E:13-269 E:13-269 E:13-269 :13-269 :113-373 E:113-373 E:113-373 E:113-373 A:113-373 :113-373 E:113-373 E:113-373 E:113-373 A:113-373 E:113-373 E:113-373 E:113-373 E:113-373 E:113-373 :113-373 :113-373 :113-373 E:113-373 :113-373 E:113-373 E:113-373 :113-373 A:113-373 E:113-373 :113-373 E:113-373 :113-373 :113-373 E:113-373 E:113-373 E:113-373 :113-373 :113-373 E:113-373 :113-373 E:113-373 E:113-373 A:113-373 :113-373 :113-373 E:113-373 A:113-373 :113-373 :113-373 :113-373 A:113-373 :113-373 E:113-373 :113-373 E:113-373 A:112-372 A:6-266 E:111-370 :111-370 :111-370 B:111-370 A:111-370 :111-370 :111-370 A:111-370 E:111-370 E:111-370 :111-370 E:111-370 :111-370 :111-370 :111-370 :111-370 :111-370 :111-370 :111-370 A:111-370 :111-370 A:6-265 A:117-371 A:117-371 :117-371 A:6-260 A:6-260 A:6-260 A:6-260 :6-260 A:6-260 A:6-260 :6-260 :6-260 A:6-260 A:6-260 :6-260 A:164-457 B:150-561 A:129-414 A:117-372 E:117-372 A:117-372 A:117-372 E:117-372 :117-372 A:117-372 :117-372 E:117-372 A:117-372 A:117-372 A:117-372 A:117-372 :117-372 A:117-372 A:150-410 B:150-410 A:211-514 A:211-514 A:211-514 B:107-573 D:127-427 A:149-445 B:149-445 A:195-521 A:195-521 A:195-521 1:194-515 1:194-515 A:194-515 1:194-515 2:194-515 A:194-515 A:194-515 A:227-552 A:227-552 A:227-552 A:227-552 A:227-552 A:227-552 A:227-552 A:227-552 A:227-552".
• Subtilase pfam "PF00082".
• Subtilase prosite "PDOC00125".
• Subtilase scop "1".
• Subtilase symbol "Peptidase_S8".
• Subtilase subject Category:Peptidase.
• Subtilase subject Category:Protein_domains.
• Subtilase subject Category:Single-pass_transmembrane_proteins.
• Subtilase type Abstraction100002137.
• Subtilase type Attribute100024264.
• Subtilase type Chemical114806838.
• Subtilase type Compound114818238.
• Subtilase type Environment113934596.
• Subtilase type Macromolecule114944888.
• Subtilase type Material114580897.
• Subtilase type Matter100020827.
• Subtilase type Molecule114682133.
• Subtilase type OrganicCompound114727670.
• Subtilase type Part113809207.
• Subtilase type PhysicalEntity100001930.
• Subtilase type Protein114728724.
• Subtilase type ProteinDomains.
• Subtilase type Relation100031921.
• Subtilase type Single-passTransmembraneProteins.
• Subtilase type Situation113927383.
• Subtilase type Sphere114514039.
• Subtilase type State100024720.
• Subtilase type Substance100019613.
• Subtilase type Thing100002452.
• Subtilase type Unit109465459.
• Subtilase type Biomolecule.
• Subtilase type Protein.
• Subtilase type BiologicalObject.
• Subtilase comment "Subtilases are a family of subtilisin-like serine proteases. 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.".
• Subtilase label "Subtilase".
• Subtilase sameAs m.07kd77k.
• Subtilase sameAs Q7632227.
• Subtilase sameAs Q7632227.
• Subtilase sameAs Subtilase.
• Subtilase wasDerivedFrom Subtilase?oldid=593104889.
• Subtilase depiction PDB_1cse_EBI.jpg.
• Subtilase isPrimaryTopicOf Subtilase.