Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

AC1LCUYA [5-(6-aminopurin-9-yl)-3,4- dihydroxy...

Synonyms: AGN-PC-00A58J, CTK8I6637

Streaker, E.D. et al., Abbott, J. et al., Eisenberg, M.A. et al., Kwon, K. et al., Kwon, K. et al., et al.

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Disease relevance of BIO-5-AMP

Cooperative association of the Escherichia coli biotin repressor with the biotin operator is allosterically activated by binding of the corepressor, bio-5'-AMP [1].

High impact information on BIO-5-AMP

The repressor protein can activate biotin in the presence of ATP to form biotinyl-5'-adenylate, the co-repressor which remains tightly bound to the repressor protein [2].
The Escherichia coli biotin repressor is an allosteric DNA binding protein and is activated by the small molecule bio-5'-AMP [3].
In this work, the allosteric mechanism has been quantitatively probed by measuring the biotin operator binding and dimerization properties of three biotin repressor species: the apo or unliganded form, the biotin-bound form, and the holo or bio-5'-AMP-bound form [4].
BirA65-321 is, moreover, identical to intact BirA in catalysis of synthesis of bio-5'-AMP and in transfer of biotin from the adenylate to BCCP [5].
Transcription of Escherichia coli biotin operon is repressed by biotin repressor in the presence of biotinyl-5'-adenylate as a corepressor [6].

Biological context of BIO-5-AMP

The assembly states of the biotin operon repressor (BirA) and its complex with the allosteric effector, bio-5'-AMP, have been determined by analytical gel filtration chromatography [7].

Analytical, diagnostic and therapeutic context of BIO-5-AMP

In this work, isothermal titration calorimetry has been employed to examine the detailed thermodynamics of binding of three loop mutants to biotin and bio-5'-AMP [8].

References

Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor. Kwon, K., Streaker, E.D., Ruparelia, S., Beckett, D. J. Mol. Biol. (2000) [Pubmed]
Purification and properties of the biotin repressor. A bifunctional protein. Eisenberg, M.A., Prakash, O., Hsiung, S.C. J. Biol. Chem. (1982) [Pubmed]
Use of binding enthalpy to drive an allosteric transition. Brown, P.H., Beckett, D. Biochemistry (2005) [Pubmed]
The biotin repressor: thermodynamic coupling of corepressor binding, protein assembly, and sequence-specific DNA binding. Streaker, E.D., Gupta, A., Beckett, D. Biochemistry (2002) [Pubmed]
Evidence for interdomain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant. Xu, Y., Beckett, D. Biochemistry (1996) [Pubmed]
DNaseI footprinting studies of Escherichia coli biotin repressor-operator interactions. Lin, K.C., Shiuan, D. J. Biochem. (1993) [Pubmed]
Cooperative binding of the Escherichia coli repressor of biotin biosynthesis to the biotin operator sequence. Abbott, J., Beckett, D. Biochemistry (1993) [Pubmed]
Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase. Kwon, K., Streaker, E.D., Beckett, D. Protein Sci. (2002) [Pubmed]

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