3.4.21.66: Thermitase
This is an abbreviated version!
For detailed information about Thermitase, go to the full flat file.
Word Map on EC 3.4.21.66
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3.4.21.66
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subtilisins
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3.4.21.14
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carlsberg
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subtilisin-like
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subtilases
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subtilisin-type
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eglin-c
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biotechnology
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analysis
- 3.4.21.66
- subtilisins
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3.4.21.14
-
carlsberg
-
subtilisin-like
-
subtilases
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subtilisin-type
- eglin-c
- biotechnology
- analysis
Reaction
Hydrolysis of proteins, including collagen =
Synonyms
Alkaline protease, EC 3.4.21.14, EC 3.4.4.16, PLLA-degrading enzyme, PrlA, Proteinase, Thermoactinomyces vulgaris serine, proteolysin, Thermoactinomyces vulgaris serine proteinase, Thermophilic Streptomyces serine proteinase, thermostable serine protease
ECTree
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Metals Ions
Metals Ions on EC 3.4.21.66 - Thermitase
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Ca2+
additional information
required, two calcium sites (Ca1 and Ca2) are present in thermitase are likely to be present in proteolysin as well
Ca2+
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the enzyme binds very strongly one Ca2+, that cannot be removed without denaturation by any known method. A Ca2+ from a second binding site can be removed completely using Ca2+ chelating reagents
Ca2+
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three calcium binding sites, two of these are tight binding sites, and removal of calcium causes unfolding and autolysis to occur. The third calcium is more weakly bound, its removal reduces the activity of the enzyme by 10%, the reduction being reversible
bivalent metal cations increase the activity of proteolysin
additional information
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bivalent metal cations increase the activity of proteolysin