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 | 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell surface | - |
Mycobacterium tuberculosis | 9986 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WQA3 | - |
- |
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 | Comment | Organism |
---|---|---|
physiological function | gene product is required for the growth of Mycobacterium tuberculosis on gluconeogenetic substrates and in glucose-containing medium | Mycobacterium tuberculosis |