CATH Classification

Domain Context

CATH Clusters

Superfamily Immunoglobulins
Functional Family Cell surface protein

Enzyme Information

3.4.24.3
Microbial collagenase.
based on mapping to UniProt Q9X721
Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.
-!- Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. -!- Class I has forms alpha (68 kDa), beta (115 kDa) and gamma (79 kDa); class II has delta (100 kDa), epsilon (110 kDa) and zeta (125 kDa). -!- The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. -!- The enzymes also act as peptidyl-tripeptidases. -!- Variants of the enzyme have been purified from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio, Vibrio B-30 (ATCC 21250) and V.alginolyticus (previously Achromobacter iophagus). -!- Also known from Streptomyces sp. -!- Belongs to peptidase family M9. -!- Formerly EC 3.4.4.19, EC 3.4.24.8 and EC 3.4.99.5.

UniProtKB Entries (1)

Q9X721
COLG_HATHI
Hathewaya histolytica
Collagenase ColG

PDB Structure

PDB 4TN9
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structures of three polycystic kidney disease-like domains from Clostridium histolyticum collagenases ColG and ColH.
Bauer, R., Janowska, K., Taylor, K., Jordan, B., Gann, S., Janowski, T., Latimer, E.C., Matsushita, O., Sakon, J.
Acta Crystallogr.,Sect.D