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Independent catalysis of the short form HisG from Lactococcus lactis
Author(s) -
Livingstone Emma K.,
Mittelstädt Gerd,
Given Fiona M.,
Parker Emily J.
Publication year - 2016
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 - 10.1002/1873-3468.12277
Subject(s) - lactococcus lactis , chemistry , protein subunit , biochemistry , histidine , stereochemistry , allosteric regulation , adenosine triphosphate , biology , enzyme , bacteria , genetics , lactic acid , gene
ATP‐phosphoribosyltransferase (ATP‐PRT) catalyses the first step of histidine biosynthesis. Two different forms of ATP‐PRT have been described; the homo‐hexameric long form, and the hetero‐octameric short form. Lactococcus lactis possesses the short form ATP‐PRT comprising four subunits of HisG S , the catalytic subunit, and four subunits of HisZ, a histidyl‐tRNA synthetase paralogue. Previous studies have suggested that HisG S requires HisZ for catalysis. Here, we reveal that the dimeric HisG S does display ATP‐PRT activity in the absence of HisZ. This result reflects the evolutionary relationship between the long and short form ATP‐PRT, which acquired allosteric inhibition and enhanced catalysis via two divergent strategies.