3.4.24.3: microbial collagenase

This is an abbreviated version!
For detailed information about microbial collagenase, go to the full flat file.

Word Map on EC 3.4.24.3

Reaction

Digestion of native collagen in the triple helical region at -/-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' =

Synonyms

More, collagenase, aspergillopeptidase C, azocollase, clostridiopeptidase A, clostridiopeptidase I, clostridiopeptidase II, collagen peptidase, collagenase A, collagenase MMP-1, EC 3.4.4.19, EC 3.4.99.5, kollaza, matrix metalloproteinase-1, metallocollagenase, metalloproteinase-1, MMP-1, nucleolysin, peptidase, clostridio-, A, proteinase, Clostridium histolyticum, A, soycollagestin, collagen protease, matirx metalloproteinase-18, collagenase I, Clostridium histolyticum collagenase, Achromobacter iophagus collagenase, 120 kDa collagenase, ColG, ChC, bacterial collagenase, thermophilic collagenolytic protease, collagenase G, clostridial collagenase A, CCA, collagenase H, ColH, collagenase T, ColT, microbial collagenase, M9-peptidase, class II collagenase, bacterial collagenase V, ColA, class III collagenase, VMC peptidase, BC_2466, class I collagenase, clostridial collagenase, type I collagenase, Dupuytren collagenase, Dupuytren clostridium histolyticum, collagenase clostridium histolyticum, type II collagenase, metalloproteinase ColB, Clostridium histolyticum class II collagenase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.3 microbial collagenase

Metals Ions

Metals Ions on EC 3.4.24.3 - microbial collagenase

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Calcium
-
binding of calcium ions triggers the formation of a cis peptide bond in the collagen-binding domain. The calcium ions not only stabilize the cis peptide bond thermodynamically but also catalyze its formation. The free energy barrier to the formation of the cis peptide bond decreases from 21.4 kcal/mol in the absence of calciumions to 10.3 kcal/mol in their presence. The calcium ions electrostatically stabilize the lone pair on the nitrogen atom that forms during the isomerization. Their attraction to acidic amino acid side chains and formation of a hydrogen bond network constrain the peptide backbone in a way that makes it easier for the nitrogen to pyramidalize
Co2+
-
activates at low concentration, inhibits at high concentration
Li+
-
activates