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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

Purification

Purification on EC 3.4.24.87 - ADAMTS13 endopeptidase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
A10-agarose column chromatography, HiTrap DEAE column chromatography, and Superdex 200 gel filtration
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about 10000fold
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from commercial factor VIII/vWF concentrate
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HiLoad Superdex 200 gel filtration
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Ni-NTA agarose column chromatography
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Ni-NTA column chromatography
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recombinant ADAMTS-13 from HEK293 cells by Zn2+-agarose affinity and anion exchange chromatography to homogeneity
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recombinant His-tagged ADAMTS13 ancillary domains, ADAMTS13-DTCS, consisting of residues 287-685, from CHO Lec cells by nickel affinity and cation exchange chromatography
recombinant His-tagged ADAMTS13 by nickel affinity chromatography
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recombinant His-tagged ADAMTS13 from HEK-293 cells by anion exchange chromatography, Ni affinity chromatography, and gel filtration
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recombinant structure-based mutants of ADAMTS13-MDTCS residues 75-685 fragment with a C-terminal tobacco etch virus proteinase cleavage site followed by tandem His-tag sequences from CHO Lec 3.2.8.1 cells by nickel affinity chromatography and gel filtration
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recombinant tagged deletion mutants
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recombinant wild-type ADAMTS13 with a C-terminal Myc/His tag from HEK293 cells, and recombinant His-tagged truncated DAMTS13 mutants MP-Dis and MP by nickel affinity chromatography and gel filtration
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recombinant wild-type and mutant ADAMTS13 from HEK-293 cells by nickel affinity chromatography
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recombinant wild-type and mutant ADAMTS13s with a C-terminal Myc/His tag expressed from HEK-293 cells by nickel affinity chromatography
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Sephadex 26/10 gel filtration
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to homogeneity
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