β-Alanyl peptide synthesis by Streptomyces S9 aminopeptidase

Arima, Jiro; Morimoto, Masazumi; Usuki, Hirokazu; Mori, Nobuhiro; Hatanaka, Tadashi

doi:10.1016/j.jbiotec.2010.03.007

Cited by 16 publications

(7 citation statements)

References 25 publications

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“…In another case, specificity toward acyl acceptors of peptidase belonging to family S9 was changed by the exchange of catalytic Ser with Cys. 22) In the case of this study, the hydrolytic activity of eryngase decreased by the mutation of Ser524 with Cys. Aminolysis activity of S524C mutant was maintained when L-Phe-NH 2 was used as a substrate.…”

Section: Discussionmentioning

confidence: 53%

“…Our recent study demonstrated that biologically active dipeptides such as cyclo (L-Pro-L-His) (anti-hyperglycemic activity), 21) carnosine derivatives (β-Ala-L-His, a dipeptide with protective functions), 22) and cyclo (D-Pro-L-Arg) (chitinase inhibitor) 23) were synthesized using serine peptidases from Streptomyces. Similarly to the serine peptidases from Streptomyces, eryngase is applicable to produce D-kyotorphin and L-kyotorphin derivatives, L-Tyr-D-Arg and L-Tyr-L-Arg, respectively, which are analgesic neuropeptides.…”

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confidence: 99%

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Gene cloning and biochemical characterization of eryngase, a serine aminopeptidase of Pleurotus eryngii belonging to the family S9 peptidases

Arima

Tokai

Chiba

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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Pleurotus eryngii serine aminopeptidase that has peptide bond formation activity, redesignated as eryngase, was cloned and expressed. Eryngase has a family S9 peptidase unit in the C-terminal region having a catalytic triad of Ser, Asp, and His. In the phylogenetic relations among the subfamilies of family S9 peptidase (S9A, prolyl oligopeptidase; S9B, dipeptidyl peptidase; S9C, acylaminoacyl peptidase; S9D, glutamyl endopeptidase), eryngase existed alone in the neighbor of S9C subfamily. Mutation of the active site Ser524 of the eryngase with Ala eliminated its catalytic activity. In contrast, S524C mutant maintained low catalytic activity. Investigation of aminolysis activity using l-Phe-NH2 as a substrate showed that S524C mutant exhibited no hydrolysis reaction but synthesized a small amount of l-Phe-l-Phe-NH2 by the catalysis of aminolysis. In contrast, wild-type eryngase hydrolyzed the product of aminolysis l-Phe-l-Phe-NH2. Results show that the S524C mutant preferentially catalyzed aminolysis when on an l-Phe-NH2 substrate.

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Section: Discussionmentioning

confidence: 53%

mentioning

confidence: 99%

Gene cloning and biochemical characterization of eryngase, a serine aminopeptidase of Pleurotus eryngii belonging to the family S9 peptidases

Arima

Tokai

Chiba

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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“…Recently, there has been a growing interest in the synthesis of peptides for medicinal applications. [29][30][31] Promoted by this fact, we report here the synthesis of new peptidylpyrimidine derivatives for increasing the bioactivity of the synthesised compounds. Thus, the condensation of compound 6 with α-amino acids methyl ester hydrochloride in presence of tetrahydrofuran containing DCC afforded the corresponding pyrimidinylamino acid derivatives 8a-c, which can also be obtained viz two other routes:…”

Section: Resultsmentioning

confidence: 99%

Synthesis of New Peptidyl- and Glycosylpyrimidine Derivatives

Aly

Behalo

2011

Journal of Chemical Research

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A new series of 2-N-(phthalyl-or tosylamino acid)pyrimidines have been synthesised from the coupling of pyrimidine derivatives with phthalyl-or tosylamino acids. Hydrazinolysis of 2-N-phthalyl derivatives afforded unprotected amino acid derivatives. New derivatives of peptidylpyrimidines have been synthesised from the reaction of pyrimidine derivatives with α-amino acids methyl ester hydrochloride viz different routes. Also, new glycosides have been prepared from the reaction of pyrimidine derivatives with α-D-glucopyranosyl bromide. Most of the synthesised compounds showed a significant antimicrobial activity.

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“…In the presence of relatively high concentrations of primary amine, which are not achieved under physiological conditions, nucleophilic attack by an amino group instead of a water molecule forms an amide bond ( Fig. 1) [6][7][8][9][10][11]. In this reaction, termed aminolysis, the primary amine acts as an acyl acceptor.…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of d‐stereospecific amidohydrolase from Streptomyces sp. 82F2 – insight into the structural factors for substrate specificity

et al. 2015

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D-Stereospecific amidohydrolase (DAH) from Streptomyces sp. 82F2, which catalyzes amide bond formation from D-aminoacyl esters and L-amino acids (aminolysis), can be used to synthesize short peptides with a DL-configuration. We found that DAH can use 1,8-diaminooctane and other amino compounds as acyl acceptors in the aminolysis reaction. Low concentrations of 1,8-diaminooctane inhibited acyl-DAH intermediate formation. By contrast, excess 1,8-diaminooctane promoted aminolysis by DAH, producing D-Phe-1,8-diaminooctane via nucleophilic attack of the diamine on enzyme-bound D-Phe. To clarify the mechanism of substrate specificity and amide bond formation by DAH, the crystal structure of the enzyme that binds 1,8-diaminooctane was determined at a resolution of 1.49A. Comparison of the DAH crystal structure with those of other members of the S12 peptidase family indicated that the substrate specificity of DAH arises from its active site structure. The 1,8-diaminooctane molecule binds at the entrance of the active site pocket. The electrkon density map showed that another potential 1,8-diaminooctane binding site, probably with lower affinity, is present close to the active site. The enzyme kinetics and structural comparisons suggest that the location of enzyme-bound diamine can explain the inhibition of the acyl-enzyme intermediate formation, although the bound diamine is too far from the active site for aminolysis. Despite difficulty in locating the diamine binding site for aminolysis definitively, we propose that the excess diamine also binds at or near the second binding site to attack the acyl-enzyme intermediate during aminolysis.

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β-Alanyl peptide synthesis by Streptomyces S9 aminopeptidase

Cited by 16 publications

References 25 publications

Gene cloning and biochemical characterization of eryngase, a serine aminopeptidase of Pleurotus eryngii belonging to the family S9 peptidases

Gene cloning and biochemical characterization of eryngase, a serine aminopeptidase of Pleurotus eryngii belonging to the family S9 peptidases

Synthesis of New Peptidyl- and Glycosylpyrimidine Derivatives

Crystal structure of d‐stereospecific amidohydrolase from Streptomyces sp. 82F2 – insight into the structural factors for substrate specificity

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