[Isolation and properties of tyrosine phenol-lyase from Citrobacter intermedius].
A method for preparation of homogeneous tyrosine phenol lyase (EC 4.199.2) from Citrobacter intermedius has been developed. The cells were cultivated in the media with a view to obtain a cell culture with a high activity of tyrosine phenol lyase. The isoelectric point for the enzyme lies at pH 4.9. Tyrosine phenol lyase is strictly stereospecific: it catalyzes the formation of pyruvate only from L-tyrosine, but not from D-tyrosine. Kinetic studies showed that K+ and NH4+ cations are non-competitive activators of the enzyme (Ka = 3.57 X 10(-3) and 1.34 X 10(-4) M, respectively).
D002848:Chromatography, DEAE-Cellulose; D002954:Citrobacter / Q000201:enzymology* / Q000254:growth & development; D004789:Enzyme Activation / Q000187:drug effects; D007526:Isoelectric Point; D007700:Kinetics; D008190:Lyases / Q000302:isolation & purification*; D011188:Potassium / Q000494:pharmacology; D000644:Quaternary Ammonium Compounds / Q000494:pharmacology; D013237:Stereoisomerism; D013379:Substrate Specificity; D014447:Tyrosine Phenol-Lyase / Q000302:isolation & purification* / Q000378:metabolism
D000644:Quaternary Ammonium Compounds; D008190:Lyases; D014447:Tyrosine Phenol-Lyase; D011188:Potassium
Vydelenie i nekotorye svoĭstva tirozin--fenol-liazy iz Citrobacter intermedius.