Prephenate dehydrogenase of Pseudomonas aeruginosa is unstable in crude extracts or following its partial purification by gel-filtration. However, when ion-exchange chromatography (DEAE-cellulose) is the initial purification step, a stable enzyme preparation is recovered. The enzyme, having a molecular weight of approximately 150,000, has a K, for prephenate of 0.05 mM, and is inhibited competi...

The homodimeric enzyme form of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa ATCC 17933 crystallizes readily with the space group R3. The X-ray structure was solved at 2.6 A resolution by molecular replacement. Aside from differences in some loops, the folding of the enzyme is very similar to the large subunit of the quinoprotein methanol dehydrogenases from Methylobacterium ex...

BACKGROUND Amino acid dehydrogenases (L-amino acid: oxidoreductase deaminating; EC 1.4.1.X) are members of the wider superfamily of oxidoreductases that catalyze the reversible oxidative deamination of an amino acid to its keto acid and ammonia with the concomitant reduction of either NAD+, NADP+ or FAD. These enzymes have been received much attention as biocatalysts for use in biosensors or...

The early steps in the biosynthesis of the aromatic amino acids in microorganisms leading to the formation of alicyclic precursors are rather well known (1, 2). Information regarding the regulation of these steps is beginning to accumulate (3, 4). A considerable gap, however, still exists in our knowledge about the properties and the regulation of the enzymes involved in the final aromatization...

Phenylalanine dehydrogenase (L-phenylalanine:NAD oxidoreductase, deaminating; EC 1.4.1.-) was found in various thermophilic actinomycetes. We purified the enzyme to homogeneity from Thermoactinomyces intermedius IFO 14230 by heat treatment and by Red Sepharose 4B, DEAE-Toyopearl, Sepharose CL-4B, and Sephadex G-100 chromatographies with a 13% yield. The relative molecular weight of the native e...

L-Arogenate is a commonplace amino acid in nature in consideration of its role as a ubiquitous precursor of L-phenylalanine and/or L-tyrosine. However, the questions of whether it serves as a chemoattractant molecule and whether it can serve as a substrate for catabolism have never been studied. We found that Pseudomonas aeruginosa recognizes L-arogenate as a chemoattractant molecule which can ...

the purpose of the current research is investigating the phenylalanine removal by using magnetic nanoparticles (fe3o4) from water samples. the effect of ph, contact time and phenylalanine concentration on phenylalanine adsorption efficiency by magnetite nanoparticles are studied in a batch system. transmission electron microscopy (tem), x-ray diffraction patterns (xrd) and fourier transform inf...

We present three novel mutations in the G6PD gene and discuss the changes they cause in the 3-dimensional structure of the enzyme: 573C-->G substitution that predicts Phe to Leu at position 191 in the C-terminus of helix alphae, 851T-->C mutation which results in the substitution 284Val--> -->Ala in the beta+alpha domain close to the C-terminal part of helix alphaj, and 1175T-->C substitution t...