Literature summary for 4.1.2.13 extracted from

de la Paz Santangelo, M.; Gest, P.M.; Guerin, M.E.; Coincon, M.; Pham, H.; Ryan, G.; Puckett, S.E.; Spencer, J.S.; Gonzalez-Juarrero, M.; Daher, R.; Lenaerts, A.J.; Schnappinger, D.; Therisod, M.; Ehrt, S.; Sygusch, J.; Jackson, M.
Glycolytic and non-glycolytic functions of Mycobacterium tuberculosis fructose-1,6-bisphosphate aldolase, an essential enzyme produced by replicating and non-replicating bacilli (2011), J. Biol. Chem., 286, 40219-40231.

Crystallization (Commentary)

Crystallization (Comment)	Organism
native form and in complex with a hydroxamate substrate analog, to 2.35- and 1.9 A resolution, respectively. Inhibitor attachment has no effect on the plasminogen binding activity of the enzyme, it competes with the natural substrate, fructose 1,6-bisphosphate, and substantiates a reaction mechanism associated with metallodependent aldolases involving recruitment of the catalytic zinc ion by the substrate upon active site binding	Mycobacterium tuberculosis

Crystallization (Comment)

Organism

native form and in complex with a hydroxamate substrate analog, to 2.35- and 1.9 A resolution, respectively. Inhibitor attachment has no effect on the plasminogen binding activity of the enzyme, it competes with the natural substrate, fructose 1,6-bisphosphate, and substantiates a reaction mechanism associated with metallodependent aldolases involving recruitment of the catalytic zinc ion by the substrate upon active site binding

Mycobacterium tuberculosis

Inhibitors

Inhibitors	Comment	Organism	Structure
N-(4-hydroxybutyl)-glycolohydroxamic acid bisphosphate	inhibitor attachment has no effect on the plasminogen binding activity of the enzyme but competes with the natural substrate, fructose 1,6-bisphosphate, and substantiates a reaction mechanism associated with metallodependent aldolases involving recruitment of the catalytic zinc ion by the substrate upon active site binding	Mycobacterium tuberculosis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell surface	-	Mycobacterium tuberculosis	9986	-

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WQA3	-	-

Expression

Organism	Comment	Expression
Mycobacterium tuberculosis	protein is produced under various axenic growth conditions including oxygen depletion and hence by non-replicating bacilli, and also in vivo in the lungs of infected guinea pigs and mice. Enzyme binds human plasmin(ogen) and protects bound plasmin from regulation by alpha2-antiplasmin	additional information

General Information

General Information	Comment	Organism
physiological function	gene product is required for the growth of Mycobacterium tuberculosis on gluconeogenetic substrates and in glucose-containing medium	Mycobacterium tuberculosis