FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1968394703> ?p ?o ?g. }

• W1968394703 endingPage "15418" @default.
• W1968394703 startingPage "15411" @default.
• W1968394703 abstract "The collagenases are members of the matrix metalloproteinase family (MMP) that degrade native triple-helical type I collagen. To understand the mechanism by which these enzymes recognize and cleave this substrate, we studied the substrate specificity of a modified form of MMP-1 (FC) in which its active site region (amino acids 212−254) had been replaced with that of MMP-9 (amino acids 395−437). Although this substitution increased the activity of the enzyme toward gelatin and the peptide substrate Mca-PLGL(Dpa)AR-NH2 by ∼3- and ∼11-fold, respectively, it decreased the type I collagenolytic activity of the enzyme to 0.13%. The replacement of Gly233, the only amino acid in this region of FC that is conserved in all collagenase family members, with the corresponding Glu residue in MMP-9 resulted in a substantial decrease in the type I collagenolytic activity of the enzyme without affecting its general proteolytic activities. The kinetic parameters of the FC/G233E mutant for the collagen substrate were similar to those of the chimeric enzyme. In addition, substituting Gly233 for Glu in the chimera increased the collagenolytic activity of the enzyme by 12-fold. Interestingly, replacing Glu415 in MMP-9 with Gly, its corresponding residue in FC, endowed the enzyme with type I collagenolytic activity. The catalytic activity of the MMP-9 mutant toward triple-helical type I collagen was 2-fold higher than that of the collagenase chimera. These data in conjunction with the X-ray crystal structure of FC indicate that Gly233 provides the flexibility necessary for the enzyme active site to change conformation upon substrate binding. The flexibility provided by the Gly residue is essential for type I collagenolytic activity." @default.
• W1968394703 created "2016-06-24" @default.
• W1968394703 creator A5044803964 @default.
• W1968394703 creator A5067270215 @default.
• W1968394703 creator A5082174745 @default.
• W1968394703 creator A5089996469 @default.
• W1968394703 date "2006-12-01" @default.
• W1968394703 modified "2023-09-23" @default.
• W1968394703 title "Matrix Metalloproteinase-1 Takes Advantage of the Induced Fit Mechanism To Cleave the Triple-Helical Type I Collagen Molecule" @default.
• W1968394703 cites W1586161363 @default.
• W1968394703 cites W1593295279 @default.
• W1968394703 cites W1611167266 @default.
• W1968394703 cites W1806896498 @default.
• W1968394703 cites W1894541755 @default.
• W1968394703 cites W1935587632 @default.
• W1968394703 cites W1951248594 @default.
• W1968394703 cites W1974618539 @default.
• W1968394703 cites W1995249913 @default.
• W1968394703 cites W2007849177 @default.
• W1968394703 cites W2022289649 @default.
• W1968394703 cites W2023285074 @default.
• W1968394703 cites W2030334284 @default.
• W1968394703 cites W2030744682 @default.
• W1968394703 cites W2043703193 @default.
• W1968394703 cites W2045255814 @default.
• W1968394703 cites W2057055923 @default.
• W1968394703 cites W2072438573 @default.
• W1968394703 cites W2089719502 @default.
• W1968394703 cites W2115426314 @default.
• W1968394703 cites W2117960153 @default.
• W1968394703 cites W2147145439 @default.
• W1968394703 cites W2157114285 @default.
• W1968394703 cites W238469003 @default.
• W1968394703 cites W4250908540 @default.
• W1968394703 doi "https://doi.org/10.1021/bi060849d" @default.
• W1968394703 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17176063" @default.
• W1968394703 hasPublicationYear "2006" @default.
• W1968394703 type Work @default.
• W1968394703 sameAs 1968394703 @default.
• W1968394703 citedByCount "25" @default.
• W1968394703 countsByYear W19683947032012 @default.
• W1968394703 countsByYear W19683947032013 @default.
• W1968394703 countsByYear W19683947032014 @default.
• W1968394703 countsByYear W19683947032015 @default.
• W1968394703 countsByYear W19683947032017 @default.
• W1968394703 countsByYear W19683947032018 @default.
• W1968394703 countsByYear W19683947032019 @default.
• W1968394703 countsByYear W19683947032022 @default.
• W1968394703 crossrefType "journal-article" @default.
• W1968394703 hasAuthorship W1968394703A5044803964 @default.
• W1968394703 hasAuthorship W1968394703A5067270215 @default.
• W1968394703 hasAuthorship W1968394703A5082174745 @default.
• W1968394703 hasAuthorship W1968394703A5089996469 @default.
• W1968394703 hasConcept C109523444 @default.
• W1968394703 hasConcept C125209161 @default.
• W1968394703 hasConcept C134018914 @default.
• W1968394703 hasConcept C181199279 @default.
• W1968394703 hasConcept C185592680 @default.
• W1968394703 hasConcept C19014433 @default.
• W1968394703 hasConcept C2778394429 @default.
• W1968394703 hasConcept C2779281246 @default.
• W1968394703 hasConcept C2780644872 @default.
• W1968394703 hasConcept C41183919 @default.
• W1968394703 hasConcept C515207424 @default.
• W1968394703 hasConcept C55493867 @default.
• W1968394703 hasConcept C55728118 @default.
• W1968394703 hasConcept C71240020 @default.
• W1968394703 hasConcept C86803240 @default.
• W1968394703 hasConceptScore W1968394703C109523444 @default.
• W1968394703 hasConceptScore W1968394703C125209161 @default.
• W1968394703 hasConceptScore W1968394703C134018914 @default.
• W1968394703 hasConceptScore W1968394703C181199279 @default.
• W1968394703 hasConceptScore W1968394703C185592680 @default.
• W1968394703 hasConceptScore W1968394703C19014433 @default.
• W1968394703 hasConceptScore W1968394703C2778394429 @default.
• W1968394703 hasConceptScore W1968394703C2779281246 @default.
• W1968394703 hasConceptScore W1968394703C2780644872 @default.
• W1968394703 hasConceptScore W1968394703C41183919 @default.
• W1968394703 hasConceptScore W1968394703C515207424 @default.
• W1968394703 hasConceptScore W1968394703C55493867 @default.
• W1968394703 hasConceptScore W1968394703C55728118 @default.
• W1968394703 hasConceptScore W1968394703C71240020 @default.
• W1968394703 hasConceptScore W1968394703C86803240 @default.
• W1968394703 hasIssue "51" @default.
• W1968394703 hasLocation W19683947031 @default.
• W1968394703 hasLocation W19683947032 @default.
• W1968394703 hasOpenAccess W1968394703 @default.
• W1968394703 hasPrimaryLocation W19683947031 @default.
• W1968394703 hasRelatedWork W1872082610 @default.
• W1968394703 hasRelatedWork W1968394703 @default.
• W1968394703 hasRelatedWork W1993618555 @default.
• W1968394703 hasRelatedWork W2030982529 @default.
• W1968394703 hasRelatedWork W2083457571 @default.
• W1968394703 hasRelatedWork W2101041156 @default.
• W1968394703 hasRelatedWork W2328992017 @default.
• W1968394703 hasRelatedWork W260430480 @default.
• W1968394703 hasRelatedWork W4256403470 @default.
• W1968394703 hasRelatedWork W1970430898 @default.

• next