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Literature summary extracted from

  • Matsushita, O.; Koide, T.; Kobayashi, R.; Nagata, K.; Okabe, A.
    Substrate recognition by the collagen-binding domain of Clostridium histolyticum class I collagenase (2001), J. Biol. Chem., 276, 8761-8770.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.3 E414Q mutant enzyme with a with a lower level of hydrolytic activity against insoluble collagen compared to wild-type enzyme Hathewaya histolytica

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.3 additional information
-
 MW of various C-terminal segments Hathewaya histolytica
3.4.24.3 114200
-
 mutant enzyme E414Q, MALDI-TOF mass spectrometry Hathewaya histolytica
3.4.24.3 114200
-
 wild-type enzyme, MALDI-TOF mass spectrometry Hathewaya histolytica

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.3 Hathewaya histolytica
-
 type I collagenase ColG
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.3 full-length type I collagenase and C-terminal fragments Hathewaya histolytica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.3 Collagen + H2O a collagen-binding domain specifically recognizes the triple-helical conformation made by three chains in the collagenous region Hathewaya histolytica ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.3 ColG
-
 Hathewaya histolytica