Literature summary for 2.6.1.62 extracted from

Dai, R.; Geders, T.W.; Liu, F.; Park, S.W.; Schnappinger, D.; Aldrich, C.C.; Finzel, B.C.
Fragment-based exploration of binding site flexibility in Mycobacterium tuberculosis BioA (2015), J. Med. Chem., 58, 5208-5217.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with inhibitors 5-(pyridin-2-yl)thiophene-2-carboxamide, 4-(1H-imidazol-1-yl)benzamide, and N-methyl-1-[4-(1H-pyrazol-1-ylmethyl)phenyl]methanamine	Mycobacterium tuberculosis

Inhibitors

Inhibitors	Comment	Organism	Structure
4-(1H-imidazol-1-yl)benzamide	inhibitor identified by fragment library biophysical screening, induces Trp64 and Trp65 changes to widen the binding site, but also perturbs Tyr25. Binding induces a shift in melting temperature of +4.1 degrees	Mycobacterium tuberculosis
5-(pyridin-2-yl)thiophene-2-carboxamide	inhibitor identified by fragment library biophysical screening, induces a strong remodeling of the active site. Compound can inhibit the growth of virulent strains in biotin-deprived media. Binding induces a shift in melting temperature of +6.3 degrees	Mycobacterium tuberculosis
N-methyl-1-[4-(1H-pyrazol-1-ylmethyl)phenyl]methanamine	inhibitor identified by fragment library biophysical screening, binding is purely enthalpie-driven. Binding induces a shift in melting temperature of +5.3 degrees	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WQ81	-	-
Mycobacterium tuberculosis H37Rv	P9WQ81	-	-

Synonyms

Synonyms	Comment	Organism
bioA	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)