Active Site Loop Dynamics of a Class IIa Fructose 1,6-Bisphosphate Aldolase from Mycobacterium tuberculosis

Class II fructose 1,6-bisphosphate aldolases (FBAs, EC 4.1.2.13) comprise one of two families of aldolases. Instead of forming a Schiff base intermediate using an ε-amino group of a lysine side chain, class II FBAs utilize Zn(II) to stabilize a proposed hydroxyenolate intermediate (HEI) in the rever...

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Veröffentlicht in:	Biochemistry (Easton) 2013-02, Vol.52 (5), p.912-925
Hauptverfasser:	Pegan, Scott D, Rukseree, Kamolchanok, Capodagli, Glenn C, Baker, Erica A, Krasnykh, Olga, Franzblau, Scott G, Mesecar, Andrew D
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Catalytic Domain Dihydroxyacetone Phosphate - metabolism Fructose-Bisphosphate Aldolase - antagonists & inhibitors Fructose-Bisphosphate Aldolase - chemistry Fructose-Bisphosphate Aldolase - genetics Fructose-Bisphosphate Aldolase - metabolism Hydroxamic Acids - metabolism Kinetics Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Mycobacterium tuberculosis Mycobacterium tuberculosis - chemistry Mycobacterium tuberculosis - enzymology Mycobacterium tuberculosis - genetics Mycobacterium tuberculosis - metabolism Protein Binding Sequence Alignment Substrate Specificity
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