Antibiotic and anti-parasitic agents that modulate class II fructose 1,6-bisphosphate aldolase
This invention provides a family of compounds that inhibit Class II fructose 1,6-bisphosphate aldolase (FBA), which is implicated in the pathogenic activity of a broad range of bacterial and parasitic agents. The compounds were identified by empirical testing, and provide a basis for further derivat...
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creator | AHRENDT KATERI PEGAN SCOTT DUSAN COWEN BRYAN CAPODAGLI GLENN C |
description | This invention provides a family of compounds that inhibit Class II fructose 1,6-bisphosphate aldolase (FBA), which is implicated in the pathogenic activity of a broad range of bacterial and parasitic agents. The compounds were identified by empirical testing, and provide a basis for further derivatization and optimization of 8-hydroxyquinoline-2-carboxylic acid and related compounds. Crystal structure shows that the compounds don't bind directly to the catalytic site of the enzyme, and so are not defined simply as substrate analogs. Instead, they create a pocket by induced fit, resulting a powerful and specific inhibitory effect on FBA activity. |
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The compounds were identified by empirical testing, and provide a basis for further derivatization and optimization of 8-hydroxyquinoline-2-carboxylic acid and related compounds. Crystal structure shows that the compounds don't bind directly to the catalytic site of the enzyme, and so are not defined simply as substrate analogs. 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The compounds were identified by empirical testing, and provide a basis for further derivatization and optimization of 8-hydroxyquinoline-2-carboxylic acid and related compounds. Crystal structure shows that the compounds don't bind directly to the catalytic site of the enzyme, and so are not defined simply as substrate analogs. 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The compounds were identified by empirical testing, and provide a basis for further derivatization and optimization of 8-hydroxyquinoline-2-carboxylic acid and related compounds. Crystal structure shows that the compounds don't bind directly to the catalytic site of the enzyme, and so are not defined simply as substrate analogs. Instead, they create a pocket by induced fit, resulting a powerful and specific inhibitory effect on FBA activity.</abstract><oa>free_for_read</oa></addata></record> |
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subjects | AGRICULTURE ANIMAL HUSBANDRY BEER BIOCHEMISTRY BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES, AS HERBICIDES CHEMISTRY COMPOSITIONS OR TEST PAPERS THEREFOR CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL ORENZYMOLOGICAL PROCESSES ENZYMOLOGY FISHING FORESTRY HETEROCYCLIC COMPOUNDS HUMAN NECESSITIES HUNTING INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIRCHEMICAL OR PHYSICAL PROPERTIES MEASURING MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEICACIDS OR MICROORGANISMS METALLURGY MICROBIOLOGY MUTATION OR GENETIC ENGINEERING ORGANIC CHEMISTRY PEST REPELLANTS OR ATTRACTANTS PHYSICS PLANT GROWTH REGULATORS PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTSTHEREOF PROCESSES OF PREPARING SUCH COMPOSITIONS SPIRITS TESTING TRAPPING VINEGAR WINE |
title | Antibiotic and anti-parasitic agents that modulate class II fructose 1,6-bisphosphate aldolase |
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