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Literature summary extracted from

  • Watanabe-Nakayama, T.; Itami, M.; Kodera, N.; Ando, T.; Konno, H.
    High-speed atomic force microscopy reveals strongly polarized movement of clostridial collagenase along collagen fibrils (2016), Sci. Rep., 6, 28975 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.3 recombinant expression of ColG fused to a Strep-tag II and a His6-tag at the N- and C-termini, respectively, in Escherichia coli strain BL21(DE3) Hathewaya histolytica

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.3 Zn2+ catalytic zinc ion, dependent on Hathewaya histolytica

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.3 Collagen type I + H2O Hathewaya histolytica
-
 ?
-
 ?
3.4.24.3 additional information Hathewaya histolytica ColG moves about 14.5 nm toward the collagen N-terminus in 3.8 s in a manner dependent on a catalytic zinc ion. While ColG is engaged, the collagen molecules are not only degraded but also occasionally rearranged to thicken neighboring collagen fibrils, relationship between collagen structure and collagenase movement, detailed overview. Collagen molecules form self-assembled thin sheets characterized by D-bands, also known as collagen microribbons, on a mica surface in the presence of 0.2 M potassium. ColG clears the collagen microribbon from the lateral edge, rather than from the middle. Strongly polarized movement of ColG on collagen fibrils ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.3 Hathewaya histolytica Q9X721
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.3 recombinant STrep- and His6-tagged ColG from Escherichia coli strain BL21(DE3) by Strep-Tactin affinity and nickel affinity chromatography, cleavage of the Strept-tag, and gel filtration Hathewaya histolytica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.3 Collagen type I + H2O
-
 Hathewaya histolytica ?
-
 ?
3.4.24.3 Collagen type I + H2O from rat tail Hathewaya histolytica ?
-
 ?
3.4.24.3 additional information ColG moves about 14.5 nm toward the collagen N-terminus in 3.8 s in a manner dependent on a catalytic zinc ion. While ColG is engaged, the collagen molecules are not only degraded but also occasionally rearranged to thicken neighboring collagen fibrils, relationship between collagen structure and collagenase movement, detailed overview. Collagen molecules form self-assembled thin sheets characterized by D-bands, also known as collagen microribbons, on a mica surface in the presence of 0.2 M potassium. ColG clears the collagen microribbon from the lateral edge, rather than from the middle. Strongly polarized movement of ColG on collagen fibrils Hathewaya histolytica ?
-
 ?
3.4.24.3 additional information the N-terminal His-tag alters the N-(3-[2-furyl]-acryloyl)-Leu-Gly-Pro-Ala (FALGPA) peptide digestion activity of ColG Hathewaya histolytica ?
-
 ?
3.4.24.3 N-(3-[2-furyl]-acryloyl)-Leu-Gly-Pro-Ala + H2O
-
 Hathewaya histolytica ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.3 bacterial collagenase
-
 Hathewaya histolytica
3.4.24.3 clostridial collagenase
-
 Hathewaya histolytica
3.4.24.3 ColG
-
 Hathewaya histolytica
3.4.24.3 type I collagenase
-
 Hathewaya histolytica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.3 25
-
 assay at Hathewaya histolytica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.3 7.5
-
 assay at Hathewaya histolytica