Literature summary for 3.4.24.3 extracted from

Spiriti, J.; van der Vaart, A.
Mechanism of the calcium-induced trans-cis isomerization of a non-prolyl peptide bond in Clostridium histolyticum collagenase (2010), Biochemistry, 49, 5314-5320.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
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	Hathewaya histolytica

Organism

Organism	UniProt	Comment	Textmining
Hathewaya histolytica	-	-	-

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Release 2023.1 (January 2023)