6.3.2.26	malfunction	RNAi-mediated silencing of penV gene, encoding protein Pc22g22150, UniProt-ID B6HTR9, provokes a drastic reduction of the production of the delta-(L-alpha-aminoadipyl-L-cysteinyl-D-valine) and isopenicillin N intermediates and the final product of the pathway	
6.3.2.26	additional information	the ACVS is able to catalyse multiple activities including substrate amino acids adenylation, peptide-bond formation, epimerization and tripeptide release by an integrated thioesterase, since it contains three different modules each of approximately 1000 amino acids. The enzyme contains at least ten catalytic domains. The C-terminal region of ACVS bears the epimerase and the thioesterase domains and may be involved in the epimerization of LLL-ACV to LLD-ACV and in the hydrolysis of the thioester bond. Residues E3371, H3373, R3375 and E3376 belong to the epimerase active centre. Different fragments included in the C-terminal region of the enzyme control thioester hydrolysis. Role of the EGHGRE motif present in the epimerase domain of ACVS, the epimerization domain located in the third module (activating L-valine) contains seven partially conserved motifs E1 to E7, overview. The EGHGRE motif containing residues E3371, H3373, R3375 and E3376 is crucial for the activity of the ACVS, involvement of the GWSFG motif in the ACVS activity	
6.3.2.26	physiological function	the enzyme catalyzes the non-ribosomal activation and condensation of the three constituent amino acids to form the tripeptide N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine, i.e. ACV	
6.3.2.26	physiological function	after heat shock, ACVS is singificantly upregulated. Phosphopantetheinyl transferase is coregulated with ACVS, confirming its role in activating ACVS. All components for L-alpha-aminoadipic acid synthesis are present and transcriptionally active in Folsomia candida