FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE -1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH A DUAL BINDING AMP SITE INHIBITOR

Allosteric Fbpase Inhibitors Gain 10(5) Times in Potency When Simultaneously Binding Two Neighboring AMP Sites.

D-FRUCTOSE-1,6- BISPHOSPHATE 1-PHOSPHOHYDROLASE 1, FBPASE 1

RESERVOIR = 0.1M HEPES, PH7.0, 0.1M AMMONIUM ACETATE, 12% PEG 3350

FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6 -BISPHOSPHATE, 1-PHOSPHOHYDROLASE) COMPLEXED WITH THE ALLOSTERIC INHIBITOR AMP

FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6 -BISPHOSPHATE -1-PHOSPHOHYDROLASE) (E.C.3.1 .3.11) COMPLEXED WITH A DUAL BINDING AMP SITE INHIBITOR

STRUCTURE OF HUMAN LIVER FBPASE COMPLEXED WITH POTENTBENZOXAZOLE ALLOSTERIC INHIBITORS

STRUCTURE OF HUMAN LIVER FBPASE COMPLEXED WITH POTENTBENZOXAZOLE ALLOSTERIC INHIBITIORS

STRUCTURE OF HUMAN LIVER FPBASE COMPLEXED WITH A NOVELBENZOXAZOLE AS ALLOSTERIC INHIBITOR

ROK: THE INHIBITOR MOLECULES FORM DISULFIDE DIMERS
N,N'-[DITHIOBIS(ETHANE-2,1-DIYLIMINOCARBONYL)]
BIS(4-AMINOBENZENESULFONAMIDE) ACROSS SUBUNIT
INTERFACES A-C, B-D, E-G, AND F-H.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE ALLOSTERIC INHIBITORS FORM DISULFIDE DIMERS ACROSS THE AMP-SITES OF FBPASE MONOMERS A AND C, B AND D, E AND G, AND F AND H.

FRUCTOSE-1,6-BISPHOSPHATASE 1 (E.C.3.1.3.11)

HYDROLASE (PHOSPHORIC MONOESTER), DISEASE MUTATION, ALLOSTERIC ENZYME, ZINC, HYDROLASE, POLYMORPHISM, GLUCONEOGENESIS, CARBOHYDRATE METABOLISM