Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.24.87: ADAMTS13 endopeptidase

This is an abbreviated version!
For detailed information about ADAMTS13 endopeptidase, go to the full flat file.

Word Map on EC 3.4.24.87

Reaction

The enzyme cleaves the von Willebrand factor at bond Tyr842-/-Met843 within the A2 domain =

Synonyms

a disintegrin and metalloprotease with thrombospondin motifs 13, a disintegrin and metalloprotease with thrombospondin type 1 repeats 13, a disintegrin and metalloprotease with thrombospondin-13, a disintegrin and metalloproteinase with a thrombonspondin type 1 motif member 13, a disintegrin and metalloproteinase with a thrombospondin motif repeats 13, a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13, a disintegrin-like and metalloprotease with thrombospondin type I repeats – 13, a disintegrin-like and metalloprotease with thrombospondin type-1 motifs 13, a disintegrin-like and metalloproteinase domain with thrombospondin type I motifs 13, a disintegrin-like and metalloproteinase with thrombospondin type-1 motifs 13, a disintegrin-like domain and metalloprotease with thrombospondin type I motif, a thrombospondin type 1 motif, member 13, ADAMTS 13, ADAMTS VWF cleaving metalloprotease, ADAMTS-13, ADAMTS13, ADAMTS13 metalloprotease, M12.241, metalloprotease ADAMTS-13, More, plasma metalloprotease ADAMTS13, plasma von Willebrand factor cleaving activity, Upshaw factor, van Willebrand factor processing activity, von Willebrand cleavage protease, von Willebrand cleavaging protease, von Willebrand factor cleaving protease, von Willebrand factor specific cleaving protease, von Willebrand factor-cleaving metalloprotease, von Willebrand factor-cleaving protease, von Willebrand factor-cleaving proteinase, von-Willebrand factor cleaving protease, von-Willebrand factor degrading protease, von-Willebrand-factor-cleaving protease, VWF cleaving metalloprotease, VWF cleaving protease, vWF protease, VWF-cleaving metalloprotease, vWF-cleaving protease, VWF-CP, vWF-degrading protease, VWFCP, xWF-CP

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.87 ADAMTS13 endopeptidase

Crystallization

Crystallization on EC 3.4.24.87 - ADAMTS13 endopeptidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in electron microscopy, wild-type ADAMTS13 adopts a closed conformation, gain-of-function mutant R568K/F592Y/R660K/Y661F/Y665F shows a more open conformation
purified recombinant detagged ADAMTS13-DTCS, residues 287-685, an non-catalytic von Willebrand factor-exosite-containing ADAMTS13 fragment, sitting drop vapor diffusion method, mixing of 500 nl of protein solution and 500 nl reservoir solution containing 26% w/v PEG1500, 100 mM MES, pH 6.0, supplemented with 200 nl of 40% w/w pentaerythritol ethoxylate, equilibration for several days at 20°C. Os-derivative crystals by soaking native crystals in reservoir solution supplemented with 1 mM OsCl3 and 20% glycerol for several hours, X-ray diffraction structure determination and analysis at 2.6 A and 2.8 A resolution resulting in two crystal structures
-
recombinant His-tagged ADAMTS13 ancillary domains, residues 287-685, sitting-drop vapour-diffusion method, mixing of 100 nl protein solution, containing about 20 mg/ml protein, with an equal amount of reservoir solution, containing 26% w/v PEG 1500, 100 mM MES, pH 6.0, equilibration against 0.1 ml of reservoir solution, at 20°C, for 24 h, crystals are soaked in a solution containing 20% glycerol, 26% PEG 1500, 100 mM MES, pH 6.0, for cryoprotection, X-ray diffraction structure determination and analysis at 2.6-2.8 A resolution, labeling with heavy-atom derivatives