caa a22 4500 397557337 CHVBK 20180308164806.0 cr unu---uuuuu 161202e199604 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021297 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021297 A Novel Phenylserine Dehydratase from Pseudomonas pickettii PS22: Purification, Characterization, and Sequence of Its Phosphopyridoxyl Peptide [Elektronische Daten] [Heiwa Okuda, Shinji Nagata, Haru Misono] A novel phenylserine dehydratase [EC 4.2.1.-], which catalyzes the deamination of L-threo-3-phenylserine to yield phenylpyruvate and ammonia, was purified to homogeneity from a crude extract ofPseudomonas pickettii PS22 isolated from soil. The enzyme was a monomer having a molecular mass of about 38 kDa and contained 1 mol of pyridoxal 5'-phosphate per mol of enzyme. The enzyme exhibited absorption maxima at 279 and 416 nm. No appreciable spectral change was observed over the pH range of 6.0 to 8.0. The maximal reactivity was obtained at about pH 7.5. The enzyme was highly specific for L-threo-3-phenylserine (Km, 0.21 mM). L-erythro-3-Phenylserine, L-threonine, L-serine, and D-serine were inert. The enzyme was inhibited by phenylhydrazine, hydroxylamine, p-chloromercuribenzoate, and HgCl2, but not by L-isoleucine, L-threonine, or L-serine. AMP, ADP, and ATP did not affect the enzyme activity. The N-terminal ami no acid sequence was not similar to those of biosynthetic and biodegradative L-threonine dehydratases and L-serine dehydratases. The isolated tryptic phosphopyridoxyl peptide, however, contained a pyridoxal 5′-phosphate-binding consensus amino acid sequence of amino acid dehydratases. © by the Journal of Biochemistry Regular Papers nationallicence phenylserine deaminase nationallicence phenylserine dehydratase nationallicence phosphopyridoxyl peptide nationallicence Pseudomonas pickettii nationallicence pyridoxal 5′-phosphate nationallicence Okuda Heiwa Laboratory of Applied Microbiology, Department of Bioresources Science, Kochi University, Nankoku, Kochi 783 aut Nagata Shinji Laboratory of Applied Microbiology, Department of Bioresources Science, Kochi University, Nankoku, Kochi 783 aut Misono Haru Laboratory of Applied Microbiology, Department of Bioresources Science, Kochi University, Nankoku, Kochi 783 aut The Journal of Biochemistry Oxford University Press 119/4(1996-04), 690-696 0021-924X 119:4<690 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021297 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021297 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Okuda Heiwa Laboratory of Applied Microbiology, Department of Bioresources Science, Kochi University, Nankoku, Kochi 783 aut NATIONALLICENCE 700 1- Nagata Shinji Laboratory of Applied Microbiology, Department of Bioresources Science, Kochi University, Nankoku, Kochi 783 aut NATIONALLICENCE 700 1- Misono Haru Laboratory of Applied Microbiology, Department of Bioresources Science, Kochi University, Nankoku, Kochi 783 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/4(1996-04), 690-696 0021-924X 119:4<690 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford