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carcinine hydrolase/isopenicillin-N N-acyltransferase family protein
Members of this family include hydrolases and N-acyltransferases. Most members of this family have an N-terminal region with an peptidase active site Cys residue, used autocatalytically during enzyme activation in the case of the penicillin biosynthesis enzyme PenDE (AatA) and responsible for classification of many members of this family as C45-family peptidases.
C45 family autoproteolytic acyltransferase/hydolase
Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.
C45 family peptidase
C45 family peptidase similar to Aspergillus nidulans acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase which converts isopenicillin N to penicillin G, and Drosophila pigment protein tan which converts N-beta-alanyl dopamine to dopamine
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