Ochrobactrum anthropi NCIMB 40321: a new biocatalyst with broad-spectrum l-specific amidase activity

Tweel, W.J.J. van den; Dooren, T. J. G. M. van; Jonge, P. H. de; Kaptein, Bernard; Duchateau, Alexander L. L.; Kamphuis, J.

doi:10.1007/bf00192081

Cited by 50 publications

(20 citation statements)

References 12 publications

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“…However, the low solubility of the amino acid amide caused the resolution (the enzyme optimum lies around pH 9) to proceed very slowly. The solubility problem was overcome by applying an -specific amidase from the microorganism Ochrobactrum anthropi NCIMB 40321, [20] which has a good activity at pH 6.5 and is able to withstand a higher reaction temperature (50°C). The use of this amidase resulted in an improvement of both yield and enantioselectivity giving the (R)-amide and (S)-acid in greater than 98% enantiopurity.…”

Section: Resultsmentioning

confidence: 99%

An Efficient Synthesis of 1‐Naphthylbis(oxazoline) and Exploration of the Scope in Asymmetric Catalysis

Lingen¹,

Mortel²,

Hekking³

et al. 2002

Eur J Org Chem

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Both enantiomers of 1‐naphthylglycine were obtained in 99% ee by enzymatic resolution of the corresponding racemic amino acid amide, giving access to the novel ligands (R)‐ and (S)‐naphthylbis(oxazoline). Initial studies provided insight into the scope and limitations of the (S)‐naphthyl‐substituted bis(oxazoline) and its steric influence compared to other bis(oxazolines) in catalytic asymmetric synthesis. (© Wiley‐VCH Verlag GmbH & Co KGaA, 69451 Weinheim, Germany, 2003)

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Section: Resultsmentioning

confidence: 99%

An Efficient Synthesis of 1‐Naphthylbis(oxazoline) and Exploration of the Scope in Asymmetric Catalysis

Lingen¹,

Mortel²,

Hekking³

et al. 2002

Eur J Org Chem

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“…Using whole cell biocatalysts activity towards l-Tle-NH 2 was observed in some cases. [12,13] With a d-hydantoinase (EC 3.5.2) it was possible to stereoselectively open the ring of racemic 5-tert-butylhydantoin. The resulting N-carbamoyl-d-Tle can be converted to d-Tle using a d-carbamoylase (EC 3.5.1.77) as a second enzyme or by a chemical reaction with nitrite.…”

Section: Introductionmentioning

confidence: 99%

Screening for Amidases: Isolation and Characterization of a Novel D-Amidase from Variovorax paradoxus

Krieg

Ansorge‐Schumacher²,

Kula

2002

Advanced Synthesis & Catalysis

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“…These substrates are readily available on a large scale via Strecker synthesis on the corresponding aldehydes or ketones (6,39). To further expand the scope of this technology, we isolated a new Ochrobactrum anthropi strain that combines high amidase activity toward ␣-hydrogen-and ␣,␣-disubstituted ␣-amino acid amides, ␣-hydroxy acid amides, and ␣-N-hydroxyamino acid amides with strict L-selectivity (50). The industrial attractiveness of this strain is further increased by its broad pH optimum, enabling resolution reactions between pH 5 and 8.5, and its very good temperature stability.…”

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confidence: 99%

l-Selective Amidase with Extremely Broad Substrate Specificity fromOchrobactrum anthropiNCIMB 40321

Sonke¹,

Ernste²,

Tandler³

et al. 2005

Appl Environ Microbiol

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An industrially attractive L-specific amidase was purified to homogeneity from Ochrobactrum anthropi NCIMB 40321 wild-type cells. The purified amidase displayed maximum initial activity between pH 6 and 8.5 and was fully stable for at least 1 h up to 60°C. The purified enzyme was strongly inhibited by the metal-chelating compounds EDTA and 1,10-phenanthroline. The activity of the EDTA-treated enzyme could be restored by the addition of Zn 2؉ (to 80%), Mn 2؉ (to 400%), and Mg 2؉ (to 560%). Serine and cysteine protease inhibitors did not influence the purified amidase. This enzyme displayed activity toward a broad range of substrates consisting of ␣-hydrogen-and (bulky) ␣,␣-disubstituted ␣-amino acid amides, ␣-hydroxy acid amides, and ␣-N-hydroxyamino acid amides. In all cases, only the L-enantiomer was hydrolyzed, resulting in E values of more than 150. Simple aliphatic amides, ␤-amino and ␤-hydroxy acid amides, and dipeptides were not converted. The gene encoding this L-amidase was cloned via reverse genetics. It encodes a polypeptide of 314 amino acids with a calculated molecular weight of 33,870. Since the native enzyme has a molecular mass of about 66 kDa, it most likely has a homodimeric structure. The deduced amino acid sequence showed homology to a few other stereoselective amidases and the acetamidase/ formamidase family of proteins (Pfam FmdA_AmdA). Subcloning of the gene in expression vector pTrc99A enabled efficient heterologous expression in Escherichia coli. Altogether, this amidase has a unique set of properties for application in the fine-chemicals industry.Enantiomerically pure ␣-amino acids, both natural and unnatural, form an important class of chiral building blocks for the pharmaceutical and agrochemical industries. Examples of important ␣-hydrogen-␣-amino acids are D-phenylglycine (DPhg) and D-p-hydroxyphenylglycine, which are produced as side chains for the manufacture of semisynthetic ␤-lactam antibiotics such as ampicillin, amoxicillin, and cephalexin (14, 53), and D-valine, an intermediate for the pyrethroid insecticide fluvalinate (28). Another frequently used ␣-hydrogen-␣-amino acid is L-tert-leucine, which is used as a building block for a variety of antiviral (e.g., anti-human immunodeficiency virus), antiarthritis, and anticancer drugs under development and as a chiral auxiliary in chemical asymmetric synthesis (5, 10). Besides ␣-hydrogen-␣-amino acids, ␣,␣-disubstituted ␣-amino acids also constitute a group of compounds of increasing importance, as exemplified by the use of L-␣-methyl-3,4-dihydroxyphenylalanine (L-␣-methyldopa) as an antihypertensive drug (34, 42), ␣-methylvaline as an intermediate for the herbicide Arsenal and related herbicides (47, 49), and L-␣-methylphenylglycine as a building block for the new fungicide fenamidone (27).Enantiomerically pure ␣-amino acids can be produced on a commercial scale by a number of different processes, both chemical and enzymatic. Biocatalytic processes that have been commercialized include the acylase process operated by Degussa (8) a...

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Ochrobactrum anthropi NCIMB 40321: a new biocatalyst with broad-spectrum l-specific amidase activity

Cited by 50 publications

References 12 publications

An Efficient Synthesis of 1‐Naphthylbis(oxazoline) and Exploration of the Scope in Asymmetric Catalysis

An Efficient Synthesis of 1‐Naphthylbis(oxazoline) and Exploration of the Scope in Asymmetric Catalysis

Screening for Amidases: Isolation and Characterization of a Novel D-Amidase from Variovorax paradoxus

l-Selective Amidase with Extremely Broad Substrate Specificity fromOchrobactrum anthropiNCIMB 40321

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