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Literature summary for 3.4.24.3 extracted from

  • Ohbayashi, N.; Yamagata, N.; Goto, M.; Watanabe, K.; Yamagata, Y.; Murayama, K.
    Enhancement of the structural stability of full-length clostridial collagenase by calcium ions (2012), Appl. Environ. Microbiol., 78, 5839-5844.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.3

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Hathewaya histolytica

Inhibitors

Inhibitors Comment Organism Structure
EGTA Ca2+ chelation by EGTA induces interdomain conformational changes with an increase in the percent polydispersity as the Ca2+ is chelated, suggesting an increase in protein flexibility. The thermostability is decreased by Ca2+ chelation Hathewaya histolytica

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ interdomain flexibility and the domain arrangement of full-length collagenase H are reversibly regulated by Ca2+ Hathewaya histolytica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
82000
-
 gel filtration Hathewaya histolytica
114000
-
 1 * 114000, calculated Hathewaya histolytica
119000
-
 gel filtration, presence of EGTA Hathewaya histolytica

Organism

Organism UniProt Comment Textmining
Hathewaya histolytica Q46085
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
azokoll + H2O
-
 Hathewaya histolytica ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 114000, calculated Hathewaya histolytica

Synonyms

Synonyms Comment Organism
ColH
-
 Hathewaya histolytica

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
49
-
 melting point, presence of EGTA. Addition of excess Ca2+ restores melting point to 54°C Hathewaya histolytica
54
-
 melting point Hathewaya histolytica