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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/17888
Title: A stereo-inverting D-phenylglycine aminotransferase from Pseudomonas stutzeri ST-201: Purification, characterization and application for D- phenylglycine synthesis
Authors: Suthep Wiyakrutta
Vithaya Meevootisom
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology;Immunology and Microbiology
Issue Date: 4-Jul-1997
Citation: Journal of Biotechnology. Vol.55, No.3 (1997), 193-203
Abstract: D-phenylglycine aminotransferase (D-PhgAT) from a newly isolated soil bacterium, Pseudomonas stutzeri ST-201, was purified to electrophoretic homogeneity and characterized. The molecular weight (M(r)) of the native enzyme was estimated to be 92000. It is composed of two subunits identical in molecular weight (M(r) = 47 500). The isoelectric point (pl) of the native enzyme was 5.0. The enzyme catalyzed reversible transamination specific for D-phenylglycine or D-4-hydroxyphenylglycine in which 2-oxoglutarate was an exclusive amino group acceptor and was converted into L-glutamic acid. Neither the D- nor L-isomer of phenylalanine, tyrosine, alanine, valine, leucine, isoleucine or serine could serve as a substrate. The enzyme was most active at alkaline pH with maximum activity at pH 9-10. The temperature for maximum activity was 35-45°C. The apparent K(m) values for D-phenylglycine and for 2-oxoglutarate at 35°C, pH 9.5 were 1.1 and 2.4 mM, respectively. The enzyme activity was strongly inhibited by typical inhibitors of pyridoxal phosphate-dependent enzymes. Possible application of this enzyme for synthesis of enantiomerically pure D-phenylglycine was demonstrated.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0031552598&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/17888
ISSN: 01681656
Appears in Collections:Scopus 1991-2000

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