Mutagenesis identifies a conserved tyrosine residue important for the activity of uroporphyrinogen III synthase from Anacystis nidulans.
Uroporphyrinogen III synthase from the cyanobacterium Anacystis nidulans was overproduced in Escherichia coli and analyzed by site specific mutagenesis. Of the nine conserved amino acids altered, only a single tyrosine mutant (Y166F) showed any significant decrease in activity suggesting this residue is critical for proper substrate binding and/or catalysis.
Roessner
Charles A
CA
Center for Biological NMR, Department of Chemsitry, P.O. Box 30012, Texas A&M University, College Station, TX 77842-3012, USA. c-roessner@tamu.edu
Ponnamperuma
Krishan
K
Scott
A I
AI
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D017124:Conserved Sequence; D000458:Cyanobacteria / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000502:physiology; D008969:Molecular Sequence Data; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D013329:Structure-Activity Relationship; D014443:Tyrosine / Q000235:genetics / Q000378:metabolism*; D014576:Uroporphyrinogen III Synthetase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D014443:Tyrosine; D014576:Uroporphyrinogen III Synthetase