Drentin et al., 2015 - Google Patents
Investigation of the mechanism of interaction between Mannose-binding lectin-associated serine protease-2 and complement C4Drentin et al., 2015
- Document ID
- 8689775896099607281
- Author
- Drentin N
- Conroy P
- Gunzburg M
- Pike R
- Wijeyewickrema L
- Publication year
- Publication venue
- Molecular Immunology
External Links
Snippet
The interaction between mannose-binding lectin [MBL]-associated serine protease-2 (MASP- 2) and its first substrate, C4 is crucial to the lectin pathway of complement, which is vital for innate host immunity, but also involved in a number of inflammatory diseases. Recent data …
- 230000003993 interaction 0 title abstract description 27
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6427—Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6489—Metalloendopeptidases (3.4.24)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6402—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals
- C12N9/6405—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals not being snakes
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
- G01N2333/95—Proteinases, i.e. endopeptidases (3.4.21-3.4.99)
- G01N2333/964—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue
- G01N2333/96425—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals
- G01N2333/96427—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals in general
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
- C12N9/18—Carboxylic ester hydrolases (3.1.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
- C12Q1/37—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving hydrolase involving peptidase or proteinase
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Odintsov et al. | Latent LytM at 1.3 Å resolution | |
| Ambrus et al. | Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and-2: a study on recombinant catalytic fragments | |
| Huntington et al. | Mechanism of heparin activation of antithrombin. Evidence for reactive center loop preinsertion with expulsion upon heparin binding | |
| King et al. | Molecular basis of substrate recognition and degradation by human presequence protease | |
| Perona et al. | Crystal structure of an Ecotin− Collagenase complex suggests a model for recognition and cleavage of the collagen triple helix | |
| Agarwal et al. | Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212→ Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway | |
| Houston et al. | Activation and proteolytic activity of the Treponema pallidum metalloprotease, pallilysin | |
| Weng et al. | Improving the activity of the subtilisin nattokinase by site-directed mutagenesis and molecular dynamics simulation | |
| Drentin et al. | Investigation of the mechanism of interaction between Mannose-binding lectin-associated serine protease-2 and complement C4 | |
| Toma et al. | Grafting of a calcium-binding loop of thermolysin to Bacillus subtilis neutral protease | |
| Vath et al. | The crystal structure of exfoliative toxin B: a superantigen with enzymatic activity | |
| Jacobsen et al. | Catalytic properties of ADAM12 and its domain deletion mutants | |
| Fitzpatrick et al. | Regulation of plasmin activity by annexin II tetramer | |
| Loy et al. | Domain interactions between streptokinase and human plasminogen | |
| Peters et al. | Pro region C-terminus: protease active site interactions are critical in catalyzing the folding of α-lytic protease | |
| Komiyama et al. | Engineered eglin c variants inhibit yeast and human proprotein processing proteases, Kex2 and furin | |
| Szabó et al. | Mesotrypsin signature mutation in a chymotrypsin C (CTRC) variant associated with chronic pancreatitis | |
| Jin et al. | Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity | |
| Radisky et al. | Binding, proteolytic, and crystallographic analyses of mutations at the protease− inhibitor interface of the subtilisin BPN ‘/chymotrypsin inhibitor 2 complex | |
| Lu et al. | Staphylococcus aureus sortase A exists as a dimeric protein in vitro | |
| Chaillan-Huntington et al. | The P6− P2 Region of Serpins Is Critical for Proteinase Inhibition and Complex Stability | |
| KRAMER et al. | Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding | |
| Tsiftsoglou et al. | The catalytically active serine protease domain of human complement factor I | |
| Ally et al. | Characterization of the specificity of arginine-specific gingipains from Porphyromonas gingivalis reveals active site differences between different forms of the enzymes | |
| Duncan et al. | Multiple domains of MASP-2, an initiating complement protease, are required for interaction with its substrate C4 |