An aminoacylase activity from Streptomyces ambofaciens catalyzes the acylation of lysine on α‐position and peptides on N‐terminal position

Abstract

The presence of aminoacylase activities was investigated in a crude extract of Streptomyces ambofaciens ATCC23877. First activities catalyzing the hydrolysis of N‐α or ε‐acetyl‐L‐lysine were identified. Furthermore, the acylation of lysine and different peptides was studied and compared with results obtained with lipase B of Candida antarctica (CALB). Different regioselectivities were demonstrated for the two classes of enzymes. CALB was able to catalyze acylation only on the ε‐position whereas the crude extract from S. ambofaciens possessed the rare ability to catalyze the N‐acylation on the α‐position of the lysine or of the amino‐acid in N‐terminal position of peptides. Two genes, SAM23877_1485 and SAM23877_1734, were identified in the genome of Streptomyces ambofaciens ATCC23877 whose products show similarities with the previously identified aminoacylases from Streptomyces mobaraensis. The proteins encoded by these two genes were responsible for the major aminoacylase hydrolytic activities. Furthermore, we show that the hydrolysis of N‐α‐acetyl‐L‐lysine could be attributed to the product of SAM23877_1734 gene.

Development of a One-Step Multiplex PCR Assay for Differential Detection of Four species (Enterobacter cloacae, Enterobacter hormaechei, Enterobacter roggenkampii, and Enterobacter kobei) Belonging to Enterobacter cloacae Complex With Clinical Significance

“…To avoid high sequence homology between all of the candidate unique genes which might be a consequence of the high identity threshold chosen for pan-genome construction, and to obtain species-specific primers with high possibility, the pair-wise blast was further performed. Four species-specific genes were obtained for the four species, respectively, including a gene (ECL_01098) encoding an aminoacylase ( Curley and van Sinderen, 2000 ; Dettori et al., 2018 ) in the genome of E. cloacae ssp. cloacae strain ATCC 13047 (accession no.…”

Enzymatic Strategies for the Biosynthesis of N‐Acyl Amino Acid Amides

“…In 100 % tris buffer, the crude extract of ATCC23877 strain catalyzed the synthesis of medium‐ to long‐chain (C 8 ‐C 18 ) NAAAs, with yields of 15–25 % for L‐lysine, L‐arginine, L‐methionine, L‐leucine, and L‐phenylalanine, [17h] and under optimized conditions, produced 22 mM of N‐undecenoyl‐L‐phenylalanine [17i] . Uniquely, the crude enzyme catalyzed the N‐acylation of lysine on the α‐position of lysine to generate N‐α‐acyl‐L‐lysine, [17g–h] as opposed to the ϵ‐position with S. mobaraensis aminoacylases. Apart from the Streptomyces strains, Burkholderia sp .…”

Novel recombinant aminoacylase from Paraburkholderia monticola capable of N-acyl-amino acid synthesis

“…Synthetic activity towards acyl-amino acids has also been shown from cell extract of S. ambofaciens . The activity could be attributed to homologs of the S. mobaraensis enzymes, mainly to SamAA (Bourkaib et al 2020a ; Dettori et al 2018 ). Furthermore, homologs of SmPVA were found in S. lavendulae (Torres-Bacete et al 2015 ) and Streptomyces sp.…”