Aspartate ammonia-lyase (AAL) catalyzes the reversible conversion reactions of aspartate to fumaric acid and ammonia. In this work, Lactobacillus paracasei LpAAL gene was heterologously expressed in Escherichia coli. As well as a recombinant His-tagged protein, maltose-binding protein (MBP) fused used enhance its solubility expression level. Both proteins showed broad substrate specificity, cat...

We have isolated an enzyme, phenylalanine ammonia-lyase (EC 4.3.1.5.), from the rootlets of Zea mays var. СЕ-IV. After partial purification by fractional salting out with ammonium sulfate and gel chromatography on Sephadex G-100, we obtained a preparation of a 40-fold greater specific activity than that of the crude homogenate. We hbve determined the ap­ parent Michaelis constant and the activa...

The oscillations in phenylalanine aunnnia-lyase activity from Spirodels pelyrhiza and phenylalanine ammonia-lyase and tyrosine ammonia-lyase activities from Lemnas perpusilam disayed a circadian rhythm under continuous lght. Rhythmiclty in enzymic activity could not be detected in continuous darkness since under this condition phenylalanine ammonialyase activity remains at a fairly constantly l...

L-Phenylalanine ammonia-lyase has been purified from elicitortreated alfalfa (Medicago sativa L.) cell suspension cultures using two protocols based on different sequences of chromatofocusing and hydrophobic interaction chromatography. Three distinct forms of the intact enzyme were separated on the basis of affinity for Octyl-Sepharose, with isoelectric points in the range pH 5.1 to 5.4. The na...

The present report shows that the effect of red and far red light on the synthesis of phenylalanine ammonia-lyase can be ascribed to the action of phytochrome Pfr. This is true not only for short term irradiation but also for the action of continuous far red light. In the latter case, the model worked out by Hartmann implicating some excited species of phytochrome has to be taken into account.

Trichosporon cutaneum phenylalanine ammonia lyase was selected as a model to investigate the dual substrate activity of this family of enzymes. Sequencing of the PAL gene identified an extensive intron region at the N-terminus. Five amino acid residues differing from a prior report were identified. Highest Phe : Tyr activities (1.6  ± 0.3 : 0.4 ± 0.1  μ mol/h g wet weight) were induced by Tyr. ...

Phenylalanine ammonia-lyase (RgPAL) from Rhodotorula glutinis JN-1 stereoselectively catalyzes the conversion of the l-phenylalanine into trans-cinnamic acid and ammonia, and was used in chiral resolution of dl-phenylalanine to produce the d-phenylalanine under acidic condition. However, the optimum pH of RgPAL is 9 and the RgPAL exhibits low catalytic efficiency at acidic side. Therefore, a mu...