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3.4.24.86: ADAM 17 endopeptidase

This is an abbreviated version!
For detailed information about ADAM 17 endopeptidase, go to the full flat file.

Word Map on EC 3.4.24.86

Reaction

Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln-Ala-/-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNFalpha). Similarly cleaves other membrane-anchored, cell-surface proteins to "shed" the extracellular domains =

Synonyms

(TACE/ADAM17/CD156q), (TACE:ADAM17), a disintegrin and metallo protease domain 17, a disintegrin and metalloprotease 17, a disintegrin and metalloprotease-17, a disintegrin and metalloproteinase 17, a disintegrin and metalloproteinase-17, ADAM-17, ADAM17, ADAM17 proteinase, ADAM17/tumor necrosis factor-alpha (TNF-A)converting enzyme, ADAMTS-2, CD156, H-TACE, human TACE B, metalloprotease TACE, metalloprotease-disintegrin tumour necrosis factor alpha convertase, metalloproteinase ADAM17, pro tumor necrosis factor cleavage enzyme, pro-tumor necrosis factor-alpha-processing enzyme, proteinase, pro-tumor necrosis factor (9CI), sheddase, TACE, TACE proteinase, TACE/ADAM17, TNF converting enzyme, TNF-alpha convertase, TNF-alpha converting enzyme, TNF-alpha processing protease, TNFalpha converting enzyme, tumor necrosis factor alpha convertase, tumor necrosis factor alpha converting enzyme, tumor necrosis factor alpha-converting enzyme, tumor necrosis factor-alpha converting enzyme, tumor necrosis factor-alpha-converting enzyme, tumour necrosis factor alpha-converting enzyme, tumour necrosis factor-alpha converting enzyme

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.86 ADAM 17 endopeptidase

Crystallization

Crystallization on EC 3.4.24.86 - ADAM 17 endopeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
docking of nine-residue peptide PLAQA-VRSS from proTNF-alpha. The peptide adopts an anti-parallel beta-sheet conformation against a nearby beta-sheet of the protein. In the complexmodel, the side-chains of residues P2 and P2' are largely exposed,and do not form highly favorable interactions
hanging drop vapour diffusion method with 15% polyethylene glycol 4000, 10% 2-propanol, 100 mM sodium citrate (pH 5.6)
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molecular docking studies of inhibitor 2-(N-benzoxycarbonyl)aminoethyl-N-(4-hydroxyamino-4-oxo-2-(isopropylthio)butanoyl)-L-3-phenylalanyl-L-alanyl amide
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TACE mutant V353G is crystallized with the respective inhibitors with a resolution of 1.7 A using the hanging drop method
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X-ray crystal structure of the catalytic domain of TACE
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