Isolation and Characterization of N-Long Chain Acyl Aminoacylase from Pseudomonas diminuta

Shintani, Yasushi; Fukuda, Hirosuke; Okamoto, Nobuhiko; Murata, Kousaku; Kimura, Akira

doi:10.1093/oxfordjournals.jbchem.a134879

Cited by 8 publications

(2 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, the enzyme does not show any activity toward N -acetyl- l -amino acids, indicating that the enzyme is classified as a type of long chain acyl aminoacylase. Aminoacylases showing such a wide substrate specificity have not been reported to date ( − ). Furthermore, the enzyme shows deacylation activity toward N -lauroyl- l -dipeptides, although it has no peptidase activity.…”

Section: Resultsmentioning

confidence: 99%

A Novel Acylase from Streptomyces mobaraensis that Efficiently Catalyzes Hydrolysis/Synthesis of Capsaicins as Well as N-Acyl-l-amino Acids and N-Acyl-peptides

Koreishi

Zhang

Imanaka

et al. 2005

J. Agric. Food Chem.

View full text Add to dashboard Cite

A novel enzyme that catalyzes efficient hydrolysis of capsaicin (8-methyl-N-vanillyl-6-nonenamide) was isolated from the culture broth of Streptomyces mobaraensis. The enzyme consisted of two dissimilar subunits with molecular masses of 61 and 19 kDa. The enzyme was activated and stabilized in the presence of Co2+. It showed a pH optimum of about 8 and was stable at temperatures of up to 55 degrees C for 1 h at pH 7.8. The specific activity of the enzyme for the hydrolysis of capsaicin was 10(2)-10(4) times higher than those for the enzymes reported to date. In an aqueous/n-hexane biphasic system, capsaicin analogues such as octanoyl, decanoyl, and lauroyl vanillylamides were synthesized from the corresponding fatty acids and vanillylamine at yields of 50% or greater. In addition, the enzyme catalyzed the deacylation of N-lauroyl-L-amino acids and N-lauroyl-L-dipeptides and the efficient synthesis of Nalpha-lauroyl-L-lysine, Nepsilon-lauroyl-L-lysine, and various N-lauroyl-peptides in aqueous solution in both the absence and the presence of glycerol.

show abstract

Section: Resultsmentioning

confidence: 99%

A Novel Acylase from Streptomyces mobaraensis that Efficiently Catalyzes Hydrolysis/Synthesis of Capsaicins as Well as N-Acyl-l-amino Acids and N-Acyl-peptides

Koreishi

Zhang

Imanaka

et al. 2005

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…First, studies have reported the isolation of bacterial N-acyl amino acids from cultured environmental isolates, yet the enzymatic origins of these metabolites were not described (26,33,41). Second, microbial enzymes that either hydrolytically degrade or fur-ther modify long-chain N-acyl amino acids have been recognized for many years (5,15,21,31). Third, E. coli-based heterologous expression of related N-acylhomoserine lactone synthases and lyso-ornithine lipid synthases (OlsB homologs) results in the accumulation of only the corresponding natively produced metabolites (16,39).…”

Section: Discussionmentioning

confidence: 99%

Long-Chain N -Acyl Amino Acid Synthases Are Linked to the Putative PEP-CTERM/Exosortase Protein-Sorting System in Gram-Negative Bacteria

Craig

Cherry

2011

J Bacteriol

View full text Add to dashboard Cite

Clones that encode the biosynthesis of long-chain N-acyl amino acids are frequently recovered from activitybased screens of soil metagenomic libraries. Members of a diverse set of enzymes referred to as N-acyl amino acid synthases are responsible for the production of all metagenome-derived N-acyl amino acids characterized to date. Based on the frequency at which N-acyl amino acid synthase genes have been identified from metagenomic samples, related genes are expected to be common throughout the global bacterial metagenome. Homologs of metagenome-derived N-acyl amino acid synthase genes are scarce, however, within the sequenced genomes of cultured bacterial species. Toward the goal of understanding the role(s) played by N-acyl amino acids in environmental bacteria, we looked for conserved genetic features that are positionally linked to metagenome-derived N-acyl amino acid synthase genes. This analysis revealed that N-acyl amino acid synthase genes are frequently found adjacent to genes predicted to encode PEP-CTERM motif-containing proteins and, in some cases, other conserved elements of the PEP-CTERM/exosortase system. Although relatively little is known about the PEP-CTERM/exosortase system, its core components are believed to represent the putative Gram-negative equivalent of the LPXTG/sortase protein-sorting system of Gram-positive bacteria. During the course of this investigation, we were able to provide evidence that an uncharacterized family of hypothetical acyltransferases, which had previously been linked to the PEP-CTERM/exosortase system by bioinformatics, is a new family of N-acyl amino acid synthases that is widely distributed among the PEP-CTERM/exosortase system-containing Proteobacteria.

show abstract

Long-chain-fatty-acyl-glutamate deacylase

Schomburg

Stephan

1998

Enzyme Handbook 16

View full text Add to dashboard Cite

Isolation and Characterization of N-Long Chain Acyl Aminoacylase from Pseudomonas diminuta

Cited by 8 publications

References 0 publications

A Novel Acylase from Streptomyces mobaraensis that Efficiently Catalyzes Hydrolysis/Synthesis of Capsaicins as Well as N-Acyl-l-amino Acids and N-Acyl-peptides

A Novel Acylase from Streptomyces mobaraensis that Efficiently Catalyzes Hydrolysis/Synthesis of Capsaicins as Well as N-Acyl-l-amino Acids and N-Acyl-peptides

Long-Chain N -Acyl Amino Acid Synthases Are Linked to the Putative PEP-CTERM/Exosortase Protein-Sorting System in Gram-Negative Bacteria

Long-chain-fatty-acyl-glutamate deacylase

Contact Info

Product

Resources

About