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Literature summary for 3.4.24.87 extracted from

  • Banno, F.; Chauhan, A.; Kokame, K.; Yang, J.; Miyata, S.; Wagner, D.; Miyata, T.
    The distal carboxyl-terminal domains of ADAMTS13 are required for regulation of in vivo thrombus formation (2009), Blood, 113, 5323-5329.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene Adamts13, DNA and amino acid sequence determination and analysis, expression of truncated ADAMTS13 in 129/Sv transgenic mice Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information generation of a congenic mouse model expressing the C-terminally truncated form of ADAMTS13 on 129/Sv genetic background, presence of IAP insertion in the Adamts13 gene of the congenic Adamts13S/S mice by PCR, and detection an IAP chimeric transcript by Northern blotting of RNA from liver, overview. The distal C-terminally truncated form of mouseADAMTS13 does not completely lose the activity. In vivo thrombus growth is accelerated in Adamts13S/S mice, overview Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular secreted enzyme Mus musculus
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-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
von Willebrand factor + H2O Mus musculus
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?
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
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129/Sv mice
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Source Tissue

Source Tissue Comment Organism Textmining
liver primary site of ADAMTS13 synthesis, the enzyme is secreted Mus musculus
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plasma
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Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FRET-VWF73 + H2O fluorogenic von Willebrand factor-derived peptide substrate. The distal C-terminal domains of ADAMTS13 are not necessary for the cleavage of the VWF73-based peptide substrate Mus musculus ?
-
?
GST-VWF73 + H2O labeled von Willebrand factor-derived peptide substrate. The distal C-terminal domains of ADAMTS13 are not necessary for the cleavage of the VWF73-based peptide substrate Mus musculus ?
-
?
von Willebrand factor + H2O
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Mus musculus ?
-
?
von Willebrand factor + H2O specific cleavage of ultra-large von Willebrand factor multimers Mus musculus ?
-
?

Synonyms

Synonyms Comment Organism
ADAMTS13
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Mus musculus

General Information

General Information Comment Organism
physiological function ADAMTS13 is a multidomain protease that limits platelet thrombogenesis through the cleavage of von Willebrand factor and contributes to inhibition of platelet aggregation. Accelerated thrombus growth occurs in truncated mutant Adamts13S/S mice compared with wild-type full-length Adamts13L/L mice, indicating that the distal C-terminally truncated form of mouse ADAMTS13 has significantly reduced activity in vivo Mus musculus