Alpha-amino acid ester hydrolases: Properties and applications

Kurochkina, V. B.; Sklyarenko, A. V.; Березина, О. В.; Yarotskii, S. V.

doi:10.1134/s0003683813080036

Cited by 6 publications

(5 citation statements)

References 45 publications

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“…Subsequently, we characterised the enzyme for industrial application. AEHs from different microbial sources show similar biochemical, physicochemical and catalytic properties (Kurochkina et al 2013), and the present data show that SmAEH has high activity under conditions of pH 9.0 at 30 °C. Although AEH from S. siyangensis showed maximal activity at pH 8.5 and 25 °C (Hirao et al 2013), optimal pH and temperature values may differ between substrates (Malathi and Chakraborty 1991).…”

Section: Discussionsupporting

confidence: 68%

“…(Yokozeki and Hara 2005). Biochemical, physicochemical and catalytic properties of AEHs have been studied previously and by 2013, dipeptide-synthetic activities were documented in ten wild-type and mutant strains, which are known to express AEHs comprising multiple subunits (Kurochkina et al 2013). The present data show that AEH from S. maltophilia is a tetramer, whereas other studies show that AEH from Pseudomonas melanogenum comprises two identical subunits of 72 kDa (Kim and Byun 1990).…”

Section: Discussionmentioning

confidence: 99%

“…Peptides are important sources of nutrition, and are increasingly considered for biomedical applications (Santos et al 2012). Peptides are used as pharmaceuticals, flavour-active ingredients in natural health products, nutraceuticals, and functional foods (Mine et al 2011;Santos et al 2012), and dipeptides and tripeptides attract considerable attention because of their cost effectiveness and potential oral activity, and because they are easily characterised in structural, molecular and quantitative functional studies (Kurochkina et al 2013).…”

Section: Introductionmentioning

confidence: 99%

“…Multiple methods are available for synthesising peptides, and peptide bonds between amino acids are widely produced using chemical and chemo-enzymatic techniques (Guzmán et al 2007;Kurochkina et al 2013;Yagasaki and Hashimoto 2008). However, these methods require the introduction and elimination of protective groups, or the synthesis of intermediates, and therefore, have limited industrial utility (Yokozeki and Suzuki 2010).…”

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of Stenotrophomonas maltophilia-derived l-amino acid ester hydrolase for synthesizing dipeptide, isoleucyl-tryptophan

et al. 2018

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In the present study, we purified α-amino acid ester hydrolase (AEH) from cell-free extracts of the strain HS1. The approximately 70-kDa AEH from HS1 (SmAEH) was homogeneous in sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analyses, and was present as a tetramer in gel-filtration experiments. The activity of the SmAEH enzyme was then determined by monitoring the synthesis of the antihypertensive agent dipeptide isoleucyl-tryptophan (Ile-Trp) from isoleucyl methyl ester (Ile-OMe) and tryptophan (Trp). In these experiments, SmAEH had wide substrate specificity for acyl donors, such as Gly-OMe, β-Ala-OMe, Pro-OMe and Trp-OMe and Ile-OMe, and maximal activity were observed under conditions of pH 9.0 and 30 °C. SmAEH also showed the greatest stability at pH 9.0, whereas its activity was reduced by 40% after 10-min incubation at approximately 50 °C. In subsequent activity assays in the presence of various metal ions, Ag strongly inhibited enzyme activity. Finally, SmAEH activity was completely inhibited by phenylmethanesulfonyl fluoride (PMSF), suggesting that the protein is a serine protease.

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Section: Discussionsupporting

confidence: 68%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Purification and characterization of Stenotrophomonas maltophilia-derived l-amino acid ester hydrolase for synthesizing dipeptide, isoleucyl-tryptophan

et al. 2018

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“…Esterases can hydrolyze ester bonds but also carry out esterification and transesterification reactions. AEHs catalyze the synthesis of β‐lactam antibiotics using an α‐amino acid ester [such as d ‐phenylglycine (Phg) methyl ester] as a donor and a β‐lactam as an acceptor (10). They also are able to hydrolyze product antibiotics, and some AEHs exhibit α‐aminopeptidase activities (11).…”

mentioning

confidence: 99%

New aminopeptidase from “microbial dark matter” archaeon

Michalska

Steen²,

Chhor

et al. 2015

FASEB j.

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Marine sediments host a large population of diverse, heterotrophic, uncultured microorganisms with unknown physiologies that control carbon flow through organic matter decomposition. Recently, single-cell genomics uncovered new key players in these processes, such as the miscellaneous crenarchaeotal group. These widespread archaea encode putative intra- and extracellular proteases for the degradation of detrital proteins present in sediments. Here, we show that one of these enzymes is a self-compartmentalizing tetrameric aminopeptidase with a preference for cysteine and hydrophobic residues at the N terminus of the hydrolyzed peptide. The ability to perform detailed characterizations of enzymes from native subsurface microorganisms, without requiring that those organisms first be grown in pure culture, holds great promise for understanding key carbon transformations in the environment as well as identifying new enzymes for biomedical and biotechnological applications.

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