Independent catalysis of the short form HisG fromLactococcus lactis
| Autor: | Fiona M. Given, Gerd Mittelstädt, Emily J. Parker, Emma K. Livingstone |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Monosaccharide Transport Proteins Protein subunit Allosteric regulation Biophysics Biochemistry Catalysis Amino Acyl-tRNA Synthetases 03 medical and health sciences Bacterial Proteins Structural Biology Catalytic Domain Genetics Protein Isoforms Histidine Amino Acid Sequence Molecular Biology Peptide sequence 030102 biochemistry & molecular biology biology Chemistry Lactococcus lactis food and beverages Cell Biology ATP Phosphoribosyltransferase biology.organism_classification ATP phosphoribosyltransferase 030104 developmental biology |
| Zdroj: | FEBS Letters. 590:2603-2610 |
| ISSN: | 0014-5793 |
| Popis: | 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 HisGS , the catalytic subunit, and four subunits of HisZ, a histidyl-tRNA synthetase paralogue. Previous studies have suggested that HisGS requires HisZ for catalysis. Here, we reveal that the dimeric HisGS 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. |
| Databáze: | OpenAIRE |
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