Production of D‐ and L‐Amino Acids from D, L‐5‐Monosubstituted Hydantoins<sup>a</sup>

Syldatk, Christoph; Dombach, Giselher; Gross, Christiane; Müller, Ralf; Wagner, Fritz

doi:10.1111/j.1749-6632.1988.tb25851.x

Cited by 12 publications

(6 citation statements)

References 5 publications

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“…The chemicals used were commercially available and reagent grade. The substances tested as inducers were purchased from Sigma, Fluka, ICN, or Degussa or were synthesized as described elsewhere (34).…”

Section: Microorganism T Variabilis Dsm 70714 Was Used In All Expermentioning

confidence: 99%

“…In view of the production of D-AO by T. variabilis, further investigations were carried out with N-carbamoyl-DL-alanine. This com- pound can be synthesized easily by reacting DL-alanine with cyanate (34). The optimum concentration of N-carbamoyl-DLalanine (range tested, 0 to 50 mM) was 5 mM, which resulted in an enzyme activity of about 14 kat g of YDW Ϫ1 .…”

Section: Screening For New Inducers Of D-aomentioning

confidence: 99%

See 1 more Smart Citation

Induction of the d-Amino Acid Oxidase from Trigonopsis variabilis

Hörner¹,

Wagner²,

Fischer³

1996

Appl Environ Microbiol

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Induction of the D-amino acid oxidase (EC. 1.4.3.3) from the yeast Trigonopsis variabilis was investigated by using a minimal medium containing glucose as the carbon and energy source, (NH 4) 2 SO 4 as the nitrogen source, and various D-and DL-amino acid derivatives as inducers. The best new inducers found were Ncarbamoyl-D-alanine, N-acetyl-D-tryptophan, and N-chloroacetyl-D-␣-aminobutyric acid; when the induction effects of these compounds were compared with the effects of D-alanine as the nitrogen source and inducer, the resulting activities of D-amino acid oxidase per gram of dried yeast were 4.2, 2.1, and 1.5 times higher, respectively. The optimum concentration of the best inducer, N-carbamoyl-D-alanine, was 5 mM. This inducer could also be used in its racemic form. The induction was pH dependent. After cultivation of the yeast in a 50-liter bioreactor, D-amino acid oxidase activity of about 3,850 kat (231,000 U) was obtained. In addition, production of the D-amino acid oxidase was found to be significantly dependent on the metal salt composition of the medium. Addition of zinc ions was required to obtain high D-amino acid oxidase levels in the cells. The optimum concentration of ZnSO 4 was about 140 M.

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Section: Microorganism T Variabilis Dsm 70714 Was Used In All Expermentioning

confidence: 99%

Section: Screening For New Inducers Of D-aomentioning

confidence: 99%

Induction of the d-Amino Acid Oxidase from Trigonopsis variabilis

Hörner¹,

Wagner²,

Fischer³

1996

Appl Environ Microbiol

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“…The racemization of all other hydantoins is a very long process [7]. Increased racemization rates are obtained at alkaline pH values and higher temperatures [8].…”

Section: Introductionmentioning

confidence: 99%

Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58

et al. 2004

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A novel hydantoin racemase gene of Agrobacterium tumefaciens C58 (AthyuA2) has been cloned and expressed in Escherichia coli BL21. The recombinant protein was purified in a one-step procedure and showed an apparent molecular mass of 27000 Da in SDS-gel electrophoresis. Size exclusion chromatography analysis determined a molecular mass of approximately 100000 Da, suggesting that the native enzyme is a tetramer. The optimum pH and temperature for hydantoin racemase activity were 7.5 and 55 degrees C, respectively, with L-5-ethylhydantoin as substrate. Enzyme activity was strongly inhibited by Cu(2+) and Hg(2+). No effect on enzyme activity was detected with any other divalent cations, EDTA or DTT, suggesting that it is not a metalloenzyme. Kinetic studies showed the preference of the enzyme for hydantoins with short rather than long aliphatic side chains or hydantoins with aromatic rings.

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“…23) The broad substrate range of the processes is valuable, especially for the production of D-amino acids and unnatural L-amino acids. [35][36][37] A practical representative is the production of D-phydroxyphenylglycine, a building block for semisynthetic penicillins and cephalosporins, from racemic 5-(phydroxyphenyl)hydantoin. The process, involving one chemical step for racemic 5-(p-hydroxyphenyl)hydantoin synthesis from phenol, glyoxylic acid, and urea, and two enzymatic steps with immobilized D-hydantoinase and D-carbamoylase, 38,39) has been used in commercial production since 1995.…”

Section: Analysis and Application Of Microbial Hydantoin Metabolismmentioning

confidence: 99%

Screening and Industrial Application of Unique Microbial Reactions Involved in Nucleic Acid and Lipid Metabolisms

Ogawa

Soong

Kishino

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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Bioprocesses, which involve biocatalysts for the production of useful compounds, are expected to become a leading player in green chemistry. The first step in bioprocess development is screening for useful biological reactions in the immense number of microorganisms with infinite diversity and versatility. This review introduces some examples of bioprocess development that started from process design stemming from the discovery of unique metabolic processes, reactions, and enzymes in microbial nucleic acid and lipid metabolisms.

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Production of D‐ and L‐Amino Acids from D, L‐5‐Monosubstituted Hydantoins^a

Cited by 12 publications

References 5 publications

Induction of the d-Amino Acid Oxidase from Trigonopsis variabilis

Induction of the d-Amino Acid Oxidase from Trigonopsis variabilis

Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58

Screening and Industrial Application of Unique Microbial Reactions Involved in Nucleic Acid and Lipid Metabolisms

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Production of D‐ and L‐Amino Acids from D, L‐5‐Monosubstituted Hydantoinsa

Cited by 12 publications

References 5 publications

Induction of the d-Amino Acid Oxidase from Trigonopsis variabilis

Induction of the d-Amino Acid Oxidase from Trigonopsis variabilis

Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58

Screening and Industrial Application of Unique Microbial Reactions Involved in Nucleic Acid and Lipid Metabolisms

Contact Info

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Resources

About

Production of D‐ and L‐Amino Acids from D, L‐5‐Monosubstituted Hydantoins^a