Biotin Protein Ligase

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Biotin Protein Ligase
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The attachment of biotin onto requiring proteins is catalysed by the ubiquitous enzyme biotin protein ligase (BPL), also known as the biotin inducible repressor, BirA, in E.coli and holocarboxylase synthase (HCS) in mammals. It was once believed a separate HCS existed for each of the carboxylases. However, with the availability of modern recombinant DNA technology and complete genome sequences, there is good evidence that only one biotin protein ligase is present in most bacteria, yeast and mammals. Arabidopsis thaliana and other plants species are a notable exception to this rule as they contain two HCS genes, one encoding a cytoplasmic enzyme and the other a chloroplast targeted enzyme. Of all the BPL’s, E.coli (BirA) is by far the most characterised and understood family member. A recent ensemble of BPL structures from the thermophilic archea Pirococcus Horikoshii OT3 have also provided new insights into the catalytic mechanism of BPLs.

Revision as of 12:50, 3 June 2008

The attachment of biotin onto requiring proteins is catalysed by the ubiquitous enzyme biotin protein ligase (BPL), also known as the biotin inducible repressor, BirA, in E.coli and holocarboxylase synthase (HCS) in mammals. It was once believed a separate HCS existed for each of the carboxylases. However, with the availability of modern recombinant DNA technology and complete genome sequences, there is good evidence that only one biotin protein ligase is present in most bacteria, yeast and mammals. Arabidopsis thaliana and other plants species are a notable exception to this rule as they contain two HCS genes, one encoding a cytoplasmic enzyme and the other a chloroplast targeted enzyme. Of all the BPL’s, E.coli (BirA) is by far the most characterised and understood family member. A recent ensemble of BPL structures from the thermophilic archea Pirococcus Horikoshii OT3 have also provided new insights into the catalytic mechanism of BPLs.

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