Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes | Synapse
May 8, 2026Open Access
Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes
Key Points
This research aims to investigate the role of the loop in the wild-type conformation of coproheme decarboxylase in substrate transfer regulation.
Analyzing the structural conformation of coproheme decarboxylase from Listeria monocytogenes
Examining the interaction between active site and cosubstrates
The loop in wild-type conformation significantly regulates cosubstrate transfer toward coproheme.
Evidence of the loop's critical role suggests implications for enzymatic function and substrate specificity.
Abstract
, suggesting the loop in its wild-type conformation plays a key biological role in regulating the transfer of cosubstrates towards the main substrate coproheme.