D-Aminoacylase from a novel producer: Stenotrophomonas maltophilia ITV-0595

Muñiz-Lozano, F E; Domínguez-Sánchez, Genoveva; Dιaz-Viveros, Y; Barradas-Dermitz, Dulce

doi:10.1038/sj.jim.2900589

Cited by 11 publications

(4 citation statements)

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“…1996), S . maltophilia is an l ‐aminoacylase and d ‐aminoacylase producer, producing chiral amino acids by enantioselectively hydrolysing N ‐acyl groups in amino acid derivatives (Muniz‐Lozano et al. 1998; Wakayama et al.…”

Section: Discussionmentioning

confidence: 99%

Isolation and identification of a novel valienamine-producing bacterium

2007

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Aims: To isolate, identify and assess valienamine production by a soil bacterial isolate from a wheat field in Hangzhou, China. Methods and Results: A validamycin A‐degrading bacterial strain, numbered ZJB‐041, was isolated and identified as Stenotrophomonas maltophilia, based on morphology, physiological tests, ATB system (ID32 GN), and 16S rDNA analysis. The strain was capable of producing valienamine by decomposing validamycin A. After fermentation in shaking flasks at 30°C for 7 days, 96·0% of 34·49 mmol l−1 of validamycin A was degraded and 2·65 mmol l−1 of valienamine was obtained. The resting cells of this strain also produced valienamine by degrading validamycin A. After 72 h of incubation in 0·2 mol l−1 of phosphate buffer (pH 7·5), 90·2% of 17·16 mmol l−1 of validamycin A was degraded, and 1·77 mmol l−1 of valienamine was obtained. Conclusions: Our data suggested that S. maltophilia ZJB‐041, a bacterial isolate, has the potential for validamycin A degradation and valienamine production. Significance and Impact of the Study: The validamycin A‐degrading bacterium could potentially be utilized in the disposal of validamycin residues and in the production of valienamine.

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Section: Discussionmentioning

confidence: 99%

Isolation and identification of a novel valienamine-producing bacterium

2007

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“…or Streptomyces olivaceus can be used. [13][14][15] Watanabe et al 9 also developed D-pipecolic acid synthesis via hydrolysis of Boc-D-amino-6-bromohexanoic acid ethyl ester to Boc-D-2-amino-6-bromohexanoic acid followed by removal of the Boc group and consequent cyclization by addition of triethylamine as reported in the case of L-pipecolic acid. Many studies were performed on amino acid racemases; nevertheless, no pipecolic acid racemase has been hypothesized to be involved in D-pipecolic acid catabolism so far.…”

Section: Industrial Synthesis Of D-pipecolic Acidmentioning

confidence: 99%

“…denitrificans , Escherichia coli , Stenotrophomonas maltophilia ITV‐0595, Pseudomonas sp., and Amycolatopsis sp. or Streptomyces olivaceus can be used . Watanabe et al also developed D‐pipecolic acid synthesis via hydrolysis of Boc‐D‐amino‐6‐bromohexanoic acid ethyl ester to Boc‐D‐2‐amino‐6‐bromohexanoic acid followed by removal of the Boc group and consequent cyclization by addition of triethylamine as reported in the case of L‐pipecolic acid.…”

Section: Synthesis Of Pipecolic Acidmentioning

confidence: 99%

Significance of the Natural Occurrence of L‐ Versus D‐Pipecolic Acid: A Review

et al. 2013

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Pipecolic acid naturally occurs in microorganisms, plants, and animals, where it plays many roles, including the interactions between these organisms, and is a key constituent of many natural and synthetic bioactive molecules. This article provides a review of current knowledge on the natural occurrence of pipecolic acid and the known and potential significance of its L- and D-enantiomers in different scientific disciplines. Knowledge gaps with perspectives for future research identified within this article include the roles of the L- versus the D-enantiomer of pipecolic acid in plant resistance, nutrient acquisition, and decontamination of polluted soils, as well as rhizosphere ecology and medical issues.

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“…N-acyl-D-amidohydrolase (EC.3.5.1.81, N-D-AAase) is an enzyme capable of catalysing the hydrolysis of N-acyl-D-amino acids to yield the corresponding D-amino acid and the organic acid. They have been found in a number of bacterial species, including members of the Alcaligenes, Streptomyces, Pseudomonas, Stenotrophomonas, Amycolatopsis and Sebekia [14][15][16][17][18][19][20][21][22]. So far, all N-D-AAases characterized consist of monomeric proteins of 45-55 kDa except for the Pseudomonas sp.…”

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confidence: 99%

Identification and characterization of a new gene from Variovorax paradoxus Iso1 encoding N‐acyl‐d‐amino acid amidohydrolase responsible for d‐amino acid production

Lin¹,

Su²,

Tsai³

et al. 2002

European Journal of Biochemistry

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An N-acyl-D-amino acid amidohydrolase (N-D-AAase) was identified in cell extracts of a strain, Iso1, isolated from an environment containing N-acetyl-D-methionine. The bacterium was classified as Variovorax paradoxus by phylogenetic analysis. The gene was cloned and sequenced. The gene consisted of a 1467-bp ORF encoding a polypeptide of 488 amino acids. The V. paradoxus N-D-AAase showed significant amino acid similarity to the N-acyl-D-amino acid amidohydrolases of the two eubacteria Alcaligenes xylosoxydans A-6 (44-56% identity), Alcaligenes facelis DA1 (54% identity) and the hyperthermophilic archaeon Pyrococcus abyssi (42% identity). After over-expression of the N-D-AAase protein in Escherichia coli, the enzyme was purified by multistep chromatography. The native molecular mass was 52.8 kDa, which agreed with the predicted molecular mass of 52 798 Da and the enzyme appeared to be a monomer protein by gel-filtration chromatography. A homogenous protein with a specific activity of 516 UAEmg )1 was finally obtained. After peptide sequencing by LC/MS/ MS, the results were in agreement with the deduced amino acid sequence of the N-D-AAase. The pI of the enzyme was 5.12 and it had an optimal pH and temperature of 7.5 and 50°C, respectively. After 30 min heat treatment at 45°C, between pH 6 and pH 8, 80% activity remained. The N-D-AAase had higher hydrolysing activity against N-acetyl-D-amino acid derivates containing D-methionine, D-leucine and D-alanine and against N-chloroacetyl-D-phenylalanine. Importantly, the enzyme does not act on the N-acetyl-L-amino acid derivatives. The enzyme was inhibited by chelating agents and certain metal ions, but was activated by 1 mM of Co 2+ and Mg 2+ . Thus, the N-D-AAase from V. paradoxus can be considered a chiral specific and metaldependent enzyme.

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D-Aminoacylase from a novel producer: Stenotrophomonas maltophilia ITV-0595

Cited by 11 publications

References 10 publications

Isolation and identification of a novel valienamine-producing bacterium

Isolation and identification of a novel valienamine-producing bacterium

Significance of the Natural Occurrence of L‐ Versus D‐Pipecolic Acid: A Review

Identification and characterization of a new gene from Variovorax paradoxus Iso1 encoding N‐acyl‐d‐amino acid amidohydrolase responsible for d‐amino acid production

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