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Biotin Protein Ligase
From Proteopedia
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Biotinylation is catalysed through a two-step reaction where biotin is first activated to biotinyl-5′-AMP in an ATP dependent manner. The biotin is then transferred onto the ε-amino group of a specific target lysine residue. The reaction mechanism is related to that of amino acyl-tRNA synthetases and lipoyl ligases where the reaction proceeds through the formation of an adenylated intermediate, suggesting a common ancestral relationship <ref>pmid 18442489</ref> . | Biotinylation is catalysed through a two-step reaction where biotin is first activated to biotinyl-5′-AMP in an ATP dependent manner. The biotin is then transferred onto the ε-amino group of a specific target lysine residue. The reaction mechanism is related to that of amino acyl-tRNA synthetases and lipoyl ligases where the reaction proceeds through the formation of an adenylated intermediate, suggesting a common ancestral relationship <ref>pmid 18442489</ref> . | ||
| - | 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 <ref>pmid 16510991</ref> have also provided new insights into the catalytic mechanism of BPLs. | + | 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 <ref>pmid 16510991</ref> have also provided new insights into the catalytic mechanism of BPLs. |
== Structural highlights == | == Structural highlights == | ||
Revision as of 11:50, 4 March 2018
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3D structures of Biotin Protein Ligase
Updated on 04-March-2018
References
- ↑ Pendini NR, Bailey LM, Booker GW, Wilce MC, Wallace JC, Polyak SW. Microbial biotin protein ligases aid in understanding holocarboxylase synthetase deficiency. Biochim Biophys Acta. 2008 Jul-Aug;1784(7-8):973-82. Epub 2008 Apr 9. PMID:18442489 doi:10.1016/j.bbapap.2008.03.011
- ↑ Bagautdinov B, Kuroishi C, Sugahara M, Kunishima N. Purification, crystallization and preliminary crystallographic analysis of the biotin-protein ligase from Pyrococcus horikoshii OT3. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Feb 1;61(Pt, 2):193-5. Epub 2005 Jan 8. PMID:16510991 doi:10.1107/S1744309104034360
- ↑ Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9257-61. PMID:1409631
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