3-Carbamoyl-α-picolinic acid production by imidase-catalyzed regioselective hydrolysis of 2,3-pyridinedicarboximide in a water-organic solvent, two-phase system

Ogawa, Jun; Soong, Chee-Leong; Ito, Masato; Segawa, Toshinori; Prana, Titik K.; Prana, Made Sri; Shimizu, Sakayu

doi:10.1007/s002530000400

Cited by 9 publications

(3 citation statements)

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“…The chemo-and regioselectivities of amidases are utilized for the production of antibiotics (penicillin acylase), the hydrolysis of C-terminal amide groups in peptides (peptide amidase), the analysis of glycoproteins [peptide-N 4 -(N-acetyl-␤-D-glucosaminyl)asparagine amidase F], or the transformation of cyclic imides (halfamidase, imidase) (5,25,50,55,57,59). Enantioselective amidases are used for the production of optical active D-or L-␣-amino acids, hydroxycarboxylic acids, or ␣-methylarylacetic and ␣-methoxyarylacetic acids.…”

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confidence: 99%

Cloning and Heterologous Expression of an Enantioselective Amidase from Rhodococcus erythropolis Strain MP50

Trott

Bürger

Calaminus

et al. 2002

Appl Environ Microbiol

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The gene for an enantioselective amidase was cloned from Rhodococcus erythropolis MP50, which utilizes various aromatic nitriles via a nitrile hydratase/amidase system as nitrogen sources. The gene encoded a protein of 525 amino acids which corresponded to a protein with a molecular mass of 55.5 kDa. The deduced complete amino acid sequence showed homology to other enantioselective amidases from different bacterial genera. The nucleotide sequence approximately 2.5 kb upstream and downstream of the amidase gene was determined, but no indications for a structural coupling of the amidase gene with the genes for a nitrile hydratase were found. The amidase gene was carried by an approximately 40-kb circular plasmid in R. erythropolis MP50. The amidase was heterologously expressed in Escherichia coli and shown to hydrolyze 2-phenylpropionamide, ␣-chlorophenylacetamide, and ␣-methoxyphenylacetamide with high enantioselectivity; mandeloamide and 2-methyl-3-phenylpropionamide were also converted, but only with reduced enantioselectivity. The recombinant E. coli strain which synthesized the amidase gene was shown to grow with organic amides as nitrogen sources. A comparison of the amidase activities observed with whole cells or cell extracts of the recombinant E. coli strain suggested that the transport of the amides into the cells becomes the rate-limiting step for amide hydrolysis in recombinant E. coli strains.Acylamide amidohydrolases (amidases) are used in biocatalysis for the chemoselective, regioselective, or enantioselective hydrolysis of various amides (17, 59). The chemo-and regioselectivities of amidases are utilized for the production of antibiotics (penicillin acylase), the hydrolysis of C-terminal amide groups in peptides (peptide amidase), the analysis of glycoproteins [peptide-N 4 -(N-acetyl-␤-D-glucosaminyl)asparagine amidase F], or the transformation of cyclic imides (halfamidase, imidase) (5,25,50,55,57,59). Enantioselective amidases are used for the production of optical active D-or L-␣-amino acids, hydroxycarboxylic acids, or ␣-methylarylacetic and ␣-methoxyarylacetic acids. L-specific aminoamidases have been reported for Pseudomonas putida, Mycobacterium neoaurum, and Stenotrophomonas maltophilia, and a D-specific amino acid amidase has been found in Ochrobactrum anthropi. These enzymes usually also convert certain peptides and are therefore referred to as aminopeptidases (3,21,22,41).An evolutionarily different group of amidases has been found which enantioselectively converts 2-methylphenylacetamide (2-phenylpropionamide) and other ␣-methylarylacetamides. This group of amidases has been found in different rhodococci but also in gram-negative organisms, such as Pseudomonas chlororaphis B23 or Agrobacterium tumefaciens d3 (6,31,44,45,49).One of the best-characterized amidases with the ability to enantioselectively hydrolyze various ␣-methylarylacetamides that has been described is from Rhodococcus erythropolis MP50. This isolate was obtained from an enrichment with naproxen nitrile as sole nitrogen s...

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confidence: 99%

Cloning and Heterologous Expression of an Enantioselective Amidase from Rhodococcus erythropolis Strain MP50

Trott

Bürger

Calaminus

et al. 2002

Appl Environ Microbiol

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“…Phthalimide-assimilating Arthrobacter ureafaciens O-86 was selected as the best strain and applied to the cyclohexanone-water two phase reaction system, pH 5.5, in which the spontaneous random hydrolysis of 2,3-pyridinedicarboxyimide was avoided and the enzyme maintained its activity. Under optimized conditions, with the periodical addition of 2,3-pyridinedicarboxyimide (in total, 40 mM), 36.6 mM 3-carbamoyl--picolinic acid accumulated in the water phase with a molar conversion yield of 91.5% and a regioisomeric purity of 94.5% in 2 h. 45) Based on the finding that imidase hydrolyzes sulfurcontaining cyclic imides, enzymatic stereoselective conversion of thiazolidinedione derivatives to optically active -mercapto acids was established in a fashion similar to the hydantoinase process for optically active -amino acid production (Fig. 4c).…”

Section: Analysis and Application Of Microbial Cyclic Imide Metabolismmentioning

confidence: 99%

“…44) Another imidase, phthalimidase, with specificity toward phthalimide derivatives was found in Alcaligenes ureafaciens. 45) Half-amides, the products of imidase, were further metabolized to dicarboxylates by half-imidase. The enzyme was purified from Blastobacter sp.…”

Section: Analysis and Application Of Microbial Cyclic Imide 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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Hydrolysis and Formation of Hydantoins

Ogawa

Horinouchi

Shimizu

2012

Enzyme Catalysis in Organic Synthesis

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3-Carbamoyl-α-picolinic acid production by imidase-catalyzed regioselective hydrolysis of 2,3-pyridinedicarboximide in a water-organic solvent, two-phase system

Cited by 9 publications

References 0 publications

Cloning and Heterologous Expression of an Enantioselective Amidase from Rhodococcus erythropolis Strain MP50

Cloning and Heterologous Expression of an Enantioselective Amidase from Rhodococcus erythropolis Strain MP50

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

Hydrolysis and Formation of Hydantoins

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