Bioproduction of L-Aspartic Acid and Cinnamic Acid by L-Aspartate Ammonia Lyase from Pseudomonas aeruginosa PAO1.

Applied Biochemistry and Biotechnology
Arti T PatelDarshan H Patel


Aspartase (L-aspartate ammonia lyase, EC catalyses the reversible amination and deamination of L-aspartic acid to fumaric acid which can be used to produce important biochemical. In this study, we have explored the characteristics of aspartase from Pseudomonas aeruginosa PAO1 (PA-AspA). To overproduce PA-AspA, the 1425-bp gene was introduced in Escherichia coli BL21 and purified. A 51.0-kDa protein was observed as a homogenous purified protein on SDS-PAGE. The enzyme was optimally active at pH 8.0 and 35 °C. PA-AspA has retained 56% activity after 7 days of incubation at 35 °C, which displays the hyperthermostablility characteristics of the enzyme. PA-AspA is activated in the presence of metal ions and Mg2+ is found to be most effective. Among the substrates tested for specificity of PA-AspA, L-phenylalanine (38.35 ± 2.68) showed the highest specific activity followed by L-aspartic acid (31.21 ± 3.31) and fumarate (5.42 ± 2.94). K m values for L-phenylalanine, L-aspartic acid and fumarate were 1.71 mM, 0.346 μM and 2 M, respectively. The catalytic efficiency (k cat/K m) for L-aspartic acid (14.18 s-1 mM-1) was higher than that for L-phenylalanine (4.65 s-1 mM-1). For bioconversion, from an initial concentration of 1000...Continue Reading


Jan 1, 1992·Folia primatologica; international journal of primatology·S G Egler
Mar 25, 1985·Nucleic Acids Research·J S TakagiY Shimura
Jul 31, 1986·Biochemical and Biophysical Research Communications·J S TakagiM Kanehisa
Nov 1, 1971·Archives of Biochemistry and Biophysics·F B Rudolph, H J Fromm
Jun 20, 1995·Archives of Biochemistry and Biophysics·M Y YoonP F Cook
Aug 1, 1997·Journal of Medicinal Chemistry·Y NishimuraY Iizuka
May 21, 1999·Archives of Biochemistry and Biophysics·Yasushi KawataN Yumoto
Aug 11, 2006·Clinical Cancer Research : an Official Journal of the American Association for Cancer Research·Francis GilesKapil Bhalla
Feb 17, 2007·European Journal of Medicinal Chemistry·Roman LesykAndrzej Gzella
Jul 7, 2007·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·M Jason MacDonald, Godwin B D'Cunha
Mar 26, 2011·Current Medicinal Chemistry·P DeF Bedos-Belval
Jun 15, 2011·Biochemistry·Guntur FibriansahAndy-Mark W H Thunnissen
Feb 14, 2012·Applied Biochemistry and Biotechnology·Ram Sarup Singh, Mukesh Yadav
Apr 20, 2012·Mini Reviews in Medicinal Chemistry·M Sova
Aug 9, 2015·Journal of Industrial Microbiology & Biotechnology·Takahisa TajimaJunichi Kato
Feb 29, 2016·Applied Biochemistry and Biotechnology·Manisha J PatelDarshan H Patel


Jan 8, 2020·Critical Reviews in Biochemistry and Molecular Biology·R E Viola

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