New developments in the chemo-enzymatic production of amino acids

Kamphuis, J.; Boesten, W. H. J.; Broxterman, Quirinus B.; Hermes, H. F. M.; Balken, J. A. M. van; Meijer, E. M.; Schoemaker, Hans E.

doi:10.1007/bfb0000733

Cited by 33 publications

(20 citation statements)

References 68 publications

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“…[96] Keller and Hamilton have accomplished the optical resolution of R(+)2-trifluoromethylalanine by partial hydrolysis of the racemic N-trifluoroacetyl derivative with an enantioselectivity of 99.1 % using hog kidney aminoacylase. [97] In contrast, experiments with 2-fluoromethylalanine revealed that the acylase was unable to discriminate between the enantiomers.…”

Section: Enzymatic Resolution Using Acylase Activitymentioning

confidence: 99%

Fluorine in Peptide Design and Protein Engineering

2005

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The use of fluorine has become well established in the analysis of protein structure and function, e.g. in tools such as 19F NMR spectroscopy. The application of the unique electronic properties of this element for the structural and chemical modification of peptides and proteins emerged as a promising approach. However, the influences of amino acid fluorination on side‐chain interactions in proteins are still controversially discussed. The systematic investigation of the interaction properties of fluoroalkyl groups in a native polypeptide environment broadens the scope of fluorinated amino acids to the rational design of structural motifs and protein interfaces. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2005)

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Section: Enzymatic Resolution Using Acylase Activitymentioning

confidence: 99%

Fluorine in Peptide Design and Protein Engineering

2005

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“…The cells were disrupted and the extract was assayed for D-stereospeci¢c endopeptidase activity with (D-Phe) 4 as a substrate. The cell-free extract showed hydrolytic activity on the substrate to produce (D-Phe) 2 , suggesting that the Adp2 protein was expressed in an active form in E. coli. Culture supernatant of the E. coli transformant showed no hydrolytic activity on (D-Phe) 4 .…”

Section: Puri¢cation Of the Adp2 From E Coli Transformantmentioning

confidence: 99%

“…These results suggest that Adp2 recognize a D-con¢guration of the second residue from the NH 2 -terminus of the substrate. Adp2 hydrolyzed the substrate (D-Phe) 4 to a large amount of (D-Phe) 2 …”

Section: Substratementioning

confidence: 99%

“…The reaction was performed at 30 ‡C for 5^15 min and stopped by adding 0.1 ml of 2 N HClO 4 . The amount of (D-Phe) 2 formed in the reaction mixture was determined with a Waters 600E HPLC apparatus equipped with an ODS-80Ts column (P0.46U15 cm) from Tosoh at a £ow rate of 1.0 ml min 31 , using the solvent system of methanol:5 mM H 3 PO 4 = 7:13. Absorbance of eluate was monitored at 254 nm.…”

Section: Assay For Adp Activitymentioning

confidence: 99%

“…Absorbance of eluate was monitored at 254 nm. One unit of the enzyme was de¢ned as the amount catalyzing the formation of 2 Wmol of (D-Phe) 2 /min from (D-Phe) 4 under the above conditions. Protein was determined by the method of Bradford [23] using bovine serum albumin as a stan- dard protein.…”

Section: Assay For Adp Activitymentioning

confidence: 99%

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Genes for an alkaline d-stereospecific endopeptidase and its homolog are located in tandem onBacillus cereusgenome

Komeda

Asano

2003

FEMS Microbiology Letters

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Alkaline D-peptidase (Adp) from Bacillus cereus DF4-B is a D-stereospecific endopeptidase acting on oligopeptides composed of D-phenylalanine and the primary structure deduced from its gene, adp, shows a similarity with D-stereospecific hydrolases from Ochrobactrum anthropi strains. We have isolated DNA fragments covering the flanking region of adp from DF4-B genome and found an additional gene, adp2, located upstream of adp. The deduced amino acid sequence of Adp2 showed 96% and 85% identity with those of Adp from B. cereus strains AH559 and DF4-B, respectively. The recombinant Adp2 expressed in Escherichia coli was purified to homogeneity and characterized. It had hydrolyzing activity toward (D-Phe) 3 , (D-Phe) 4 , and (D-Phe) 6 but did not act on (L-Phe) 4 , D-Phe-NH 2 , and L-Phe-NH 2 , some characteristics that are closely related to those of Adp from strain DF4-B. These results indicate that highly homologous genes encoding D-stereospecific endopeptidases are arranged in a tandem manner on the genomic DNA of B. cereus DF4-B.

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