Purification and properties of D-aminoacylase of Streptomyces olivaceus.

Sugie, Makiko; Suzuki, Hideo

doi:10.1271/bbb1961.42.107

Cited by 32 publications

(16 citation statements)

References 1 publication

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The experiments conducted by us thus far have not detected the activities in Alcaligenes, 18,19) Pseudomonas, 20,21) or Streptomyces, 22,23) although N-acyl-D-amino acid amidohydrolase activities have been reported in these organisms. The activities reported in this paper were not induced by (R)-N-Ac--Val, which has been reported to be a good inducer of N-acyl-D-amino acid amidohydrolases of Alcaligenes, Pseudomonas, and Streptomyces.…”

Section: Discussionmentioning

confidence: 88%

Production of (R)-3-Amino-3-phenylpropionic Acid and (S)-3-Amino-3-phenylpropionic Acid from (R,S)-N-Acetyl-3-amino-3-phenylpropionic Acid Using Microorganisms Having Enantiomer-Specific Amidohydrolyzing Activity

Kawasaki

Koyama

Kurokawa

et al. 2006

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

(R)-3-Amino-3-phenylpropionic acid ((R)--Phe) and (S)-3-amino-3-phenylpropionic acid ((S)--Phe) are key compounds on account of their use as intermediates in synthesizing pharmaceuticals. Enantiomerically pure non-natural amino acids are generally prepared by enzymatic resolution of the racemic N-acetyl form, but despite the intense efforts this method could not be used for preparing enantiomerically pure -Phe, because the effective enzyme had not been found. Therefore, screening for microorganisms capable of amidohydrolyzing (R,S)-N-acetyl-3-amino-3-phenylpropionic acid ((R,S)-N-Ac--Phe) in an enantiomer-specific manner was performed.A microorganism having (R)-enantiomer-specific amidohydrolyzing activity and another having both (R)-enantiomer-and (S)-enantiomer-specific amidohydrolyzing activities were obtained from soil samples. Using 16S rDNA analysis, the former organism was identified as Variovorax sp., and the latter as Burkholderia sp. Using these organisms, enantiomerically pure (R)--Phe (> 99:5% ee) and (S)--Phe (> 99:5% ee) with a high molar conversion yield (67%-96%) were obtained from the racemic substrate.

show abstract

Section: Discussionmentioning

confidence: 88%

Production of (R)-3-Amino-3-phenylpropionic Acid and (S)-3-Amino-3-phenylpropionic Acid from (R,S)-N-Acetyl-3-amino-3-phenylpropionic Acid Using Microorganisms Having Enantiomer-Specific Amidohydrolyzing Activity

Kawasaki

Koyama

Kurokawa

et al. 2006

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

show abstract

“…Metals at concentrations lower than 0.03 mM did not show any recovery effect, since EDT A was not removed but only diluted to about 0.03 mM after EDT A treatment. The activity of EDT A-inactivated enzyme was partially restored by Zn 2 + at 0.1 mM, and fully restored 7,8) and Pseudomonas sp. 1158.…”

Section: Effects Of Metal Ionsmentioning

confidence: 95%

“…In the absence of EDT A, Co 2 + could not replace the tightly bound Zn 2 +, and thus showed no activation on activity. Zn 2 + did not inhibit the enzyme activity of D-aminoacylases from MI4,15) Streptomyces, 7) and Pseudomonas,6) O.le 10.3 …”

mentioning

confidence: 92%

“…19) The activity of D-aminoacylase from S. olivaceus, 7) but not the DAI81 D-aminoacylase, increased significantly in the presence of Co 2 +. The fact that Co 2 + fully restored the activity of EDT A-inactivated DAI8I D-aminoacylase, but had no effect on the native DAI81 enzyme (Table III) could be explained by the stronger binding affinity of Zn 2 + to the DA18I enzyme.…”

mentioning

confidence: 98%

See 1 more Smart Citation

Characterization ofD-Aminoacylase fromAlcaligenes denitrificansDA181

Yang¹,

Hsiao²,

Li³

et al. 1992

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

“…Several D-aminoacylases screened from microorganisms in various soils have been isolated and characterized (1)(2)(3)(4)(5)(6). Because of more thermostability, high substrate specificity with hydrophobic D-amino acids such as N-acetyl-D-methionine, and high affinity to DEAE resins, the D-aminoacylase from Alcaligenes faecalis DA1 is more suitable for optical resolution of N-acyl-DL-amino acids (2).…”

mentioning

confidence: 99%

Crystal Structure of d-Aminoacylase from Alcaligenes faecalis DA1

Liaw¹,

Chen²,

Ko³

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

D-Aminoacylase is an attractive candidate for commercial production of D-amino acids through its catalysis in the hydrolysis of N-acyl-D-amino acids. We report here the first D-aminoacylase crystal structure from A. faecalis at 1.5-Å resolution. The protein comprises a small ␤-barrel, and a catalytic (␤␣) 8 -barrel with a 63-residue insertion. The enzyme structure shares significant similarity to the ␣/␤-barrel amidohydrolase superfamily, in which the ␤-strands in both barrels superimpose well. Unexpectedly, the enzyme binds two zinc ions with widely different affinities, although only the tightly bound zinc ion is required for activity. One zinc ion is coordinated by Cys 96 , His 220 , and His 250 , while the other is loosely chelated by His 67 , His 69 , and Cys 96 . This is the first example of the metal ion coordination by a cysteine residue in the superfamily. Therefore, Daminoacylase defines a novel subset and is a mononuclear zinc metalloenzyme but containing a binuclear active site. The preferred substrate was modeled into a hydrophobic pocket, revealing the substrate specificity and enzyme catalysis. The 63-residue insertion containing substrate-interacting residues may act as a gate controlling access to the active site, revealing that the substrate binding would induce a closed conformation to sequester the catalysis from solvent.N-Acyl-D-amino acid amidohydrolases (D-aminoacylases, EC 3.5.1.14) catalyze the zinc-assisted hydrolysis of N-acyl-Damino acids to produce the corresponding D-amino acids, which are intermediates in the preparation of pesticides, bioactive peptides, and antibiotics. Recently, D-amino acids have been found in bacteria, plants, and animals, and their physiological functions have received increased attention. Production of Lamino acids by optical resolution using L-aminoacylase immobilized on DEAE-Sephadex has been used in industry. Therefore, production of D-amino acids using D-aminoacylase has commercial importance.Several D-aminoacylases screened from microorganisms in various soils have been isolated and characterized (1-6). Because of more thermostability, high substrate specificity with hydrophobic D-amino acids such as N-acetyl-D-methionine, and high affinity to DEAE resins, the D-aminoacylase from Alcaligenes faecalis DA1 is more suitable for optical resolution of N-acyl-DL-amino acids (2). The DA1 D-aminoacylase shares 40 -80% sequence identity to those from A. xylosoxydans A-6, and Pyrococcus abyssi, but no significant homology with Laminoacylases (7-10). Sequence homology search also revealed that the enzyme N-terminal segment (residues 8 -96) shared significant similarity within a variety of amidohydrolases including urease (10). The structural fold was predicted to be similar to urease and dihydroorotase, which have grouped into a novel ␣/␤-barrel amidohydrolase superfamily (10, 11). And the metal ligands in D-aminoacylases have been proposed based on structural prediction (10) and mutational studies (10, 12).The high degree of global structure and the metal center ...

show abstract

Purification and properties of D-aminoacylase of Streptomyces olivaceus.

Cited by 32 publications

References 1 publication

Production of (R)-3-Amino-3-phenylpropionic Acid and (S)-3-Amino-3-phenylpropionic Acid from (R,S)-N-Acetyl-3-amino-3-phenylpropionic Acid Using Microorganisms Having Enantiomer-Specific Amidohydrolyzing Activity

Production of (R)-3-Amino-3-phenylpropionic Acid and (S)-3-Amino-3-phenylpropionic Acid from (R,S)-N-Acetyl-3-amino-3-phenylpropionic Acid Using Microorganisms Having Enantiomer-Specific Amidohydrolyzing Activity

Characterization ofD-Aminoacylase fromAlcaligenes denitrificansDA181

Crystal Structure of d-Aminoacylase from Alcaligenes faecalis DA1

Contact Info

Product

Resources

About