Production and Purification of
            <scp>d</scp>
            -Aminoacylase from
            <i>Alcaligenes denitrificans</i>
            and Taxonomic Study of the Strain

Tsai, Ying-Chieh; Tseng, Ching‐Ping; Hsiao, Kuang-Ming; Chen, Lingyun

doi:10.1128/aem.54.4.984-989.1988

Cited by 44 publications

(13 citation statements)

References 17 publications

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“…In our previous article, the production and characterization of the D-aminoacylase produced by Alcaligenes denitrificans subsp. denitrificans DA181 was reported (13). This enzyme exhibited not only high stereospecificity but also high specific activity in comparison with the D-aminoacylases from Pseudomonas and Streptomyces spp.…”

Section: D-aminoacylase (N-acetyl-d-amino Acid Amidohydrolase)mentioning

confidence: 89%

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Purification and Characterization of d -Aminoacylase from Alcaligenes faecalis DA1

Yang

Lin

Tseng

et al. 1991

Appl Environ Microbiol

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A D-aminoacylase from Alcaligenes faecalis DAl has been purified to homogeneity by a simple purification procedure with two columns, Fractogel DEAE-650 and HW-50. The specific activity of the purified enzyme was found to be 580 U/mg of protein with N-acetyl-DL-methionine as the reaction substrate. The apparent molecular weight and isoelectric point of this enzyme were determined to be 55,000 and 5.4, respectively.

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Section: D-aminoacylase (N-acetyl-d-amino Acid Amidohydrolase)mentioning

confidence: 89%

“…has been studied from species of Pseudomonas (1,2,4,5), Streptomyces (11,12), and recently Alcaligenes (8,10,13). In our previous article, the production and characterization of the D-aminoacylase produced by Alcaligenes denitrificans subsp.…”

Section: D-aminoacylase (N-acetyl-d-amino Acid Amidohydrolase)mentioning

confidence: 99%

Purification and Characterization of d -Aminoacylase from Alcaligenes faecalis DA1

Yang

Lin

Tseng

et al. 1991

Appl Environ Microbiol

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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%

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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“…The mutations were confirmed by DNA sequencing. D-Aminoacylase activity was measured using N-acetyl-D-methionine as substrate coupled to a D-amino acid oxidase enzyme assay as previously described (Tsai et al 1988). For the inhibition assay, each thiol-specific reagent was incubated with the enzyme for 20…”

Section: Site-directed Mutagenesis and Characterization Of The Mutantsmentioning

confidence: 99%

Structural‐based mutational analysis of d‐aminoacylase from Alcaligenes faecalis DA1

Hsu¹,

Lai²,

Chang³

et al. 2002

Protein Science

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D-Aminoacylase is an attractive candidate for commercial production of D-amino acids through its catalysis in the zinc-assistant hydrolysis of N-acyl-D-amino acids. We report here the cloning, expression, and structural-based mutation of the D-aminoacylase from Alcaligenes faecalis DA1. A 1,007-bp PCR product amplified with degenerate primers, was used to isolate a 4-kb genomic fragment, encoding a 484-residue D-aminoacylase. The enzyme amino-terminal segment shared significant homology within a variety of enzymes including urease. The structural fold was predicted by 3D-PSSM to be similar to urease and dihydroorotase, which have grouped into a novel ␣/␤-barrel amidohydrolase superfamily with a virtually indistinguishable binuclear metal centers containing six ligands, four histidines, one aspartate, and one carboxylated lysine. Three histidines, His-67, His-69, and His-250, putative metal ligands in D-aminoacylase, have been mutated previously, the remaining histidine (His-220) and aspartate (Asp-366) Asp-65, and four cysteines were then characterized. Substitution of Asp-65, Cys-96, His-220, and Asp-366 with alanine abolished the enzyme activity. The H220A mutant bound approximately half the normal complement of zinc ion as did H250N. However, the C96A mutant showed little zinc-binding ability, revealing that Cys-96 may replace the carboxylated lysine to serve as a bridging ligand. According to the urease structure, the conserved amino-terminal segment including Asp-65 may be responsible for structural stabilization. Therefore, production of D-amino acids by D-aminoacylase has commercial importance.To search for new D-aminoacylases suitable for D-amino acid production, microorganisms in various soils were screened. Two D-aminoacylases from Alcaligenes denitrificans DA181 (Tsai et al. 1988;Yang et al. 1992) and A. faecalis DA1 (Yang et al. 1991;Tsai et al. 1992) were isolated and showed higher specific activity and better stereospecificity than those from Pseudomonas and Streptomyces (Sugie and Suzuki 1978;Kubo et al. 1980). Two other D-aminoacylase-producing strains, A. denitrificans MI-4 (Sakai et al. 1991), and A. xylosoxydans A-6 (Moriguchi et al. 1993), were subsequently screened. Three genes encoding for the A-6 D-aminoacylases have been cloned and expressed in Escherichia coli (Wakayama et al. 1995a,b,c). These A-6 D-aminoacylases share 45%-50% sequence iden-

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Production and Purification of d -Aminoacylase from Alcaligenes denitrificans and Taxonomic Study of the Strain

Cited by 44 publications

References 17 publications

Purification and Characterization of d -Aminoacylase from Alcaligenes faecalis DA1

Purification and Characterization of d -Aminoacylase from Alcaligenes faecalis DA1

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

Structural‐based mutational analysis of d‐aminoacylase from Alcaligenes faecalis DA1

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