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Literature summary extracted from

  • Rottensteiner, H.; Kaufmann, S.; Rathgeb, A.; Kink, B.; Plaimauer, B.; Matthiessen, P.; Hann, S.; Scheiflinger, F.
    Temperature-dependent irreversible conformational change of recombinant ADAMTS13 upon metal ion chelation (2019), J. Thromb. Haemost., 17, 995-1002 .
    View publication on PubMedView publication on EuropePMC

General Stability

EC Number General Stability Organism
3.4.24.87 no enzyme activity decrease is seen in heparinized plasma, but the addition of citrate causes enzyme instability at 37°C Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.87 Ca2+ the catalytic domain of the enzyme possesses up to three putative Ca2+ binding sites Homo sapiens
3.4.24.87 Zn2+ the catalytic domain of the enzyme possesses one Zn2+ binding site. Zn2+ is required to stabilize enzyme structure at physiologic temperature Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.87 von Willebrand factor + H2O Homo sapiens
-
?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.87 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.87 blood plasma
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.87 FRETS-von Willebrand factor 73 + H2O
-
Homo sapiens ?
-
?
3.4.24.87 von Willebrand factor + H2O
-
Homo sapiens ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.87 ADAMTS13
-
Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.24.87 25 37 the enzyme is stable at room temperature for up to 24 h irrespective of the presence of citrate (0.38% (w/v)). However, at 37°C, citrate causes a time-dependent activity decrease Homo sapiens