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Mutagenesis identifies a conserved tyrosine residue important for the activity of uroporphyrinogen III synthase from Anacystis nidulans
Author(s) -
Roessner Charles A,
Ponnamperuma Krishan,
Scott A.I
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03056-9
Subject(s) - uroporphyrinogen iii decarboxylase , tyrosine , biochemistry , mutagenesis , mutant , site directed mutagenesis , escherichia coli , chemistry , enzyme , residue (chemistry) , atp synthase , biology , gene , heme
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.