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Literature summary for 3.4.24.87 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
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General Stability

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

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the catalytic domain of the enzyme possesses up to three putative Ca2+ binding sites Homo sapiens
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)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
 Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
ADAMTS13
-
 Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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