Non-Competitive Inhibition by Active Site Binders
نویسندگان
چکیده
منابع مشابه
Competitive inhibition of aristolochene synthase by phenyl-substituted farnesyl diphosphates: evidence of active site plasticity.
Analogues of farnesyl diphosphate (FPP, ) containing phenyl substituents in place of methyl groups have been prepared in syntheses that feature use of a Suzuki-Miyaura reaction as a key step. These analogues were found not to act as substrates of the sesquiterpene cyclase aristolochene synthase from Penicillium roqueforti (AS). However, they were potent competitive inhibitors of AS with K(I)-va...
متن کاملActive Site-directed Inhibition by Optically Pure Epoxyalkyl Cellobiosides Reveals Differences in Active Site Geometry
1,31,4-@-~-Glucan 4-glucanohydrolases (EC 3.2.1.73) from Bacillus subtilis and barley (Hordeum vulgare) with identical substrate specificities but unrelated primary structures have been probed with (R,S)epoxyalkyl (-propyl, -butyl, -pentyl) 8-cellobiosides and with optically pure (3s)and (3R)-3,4-cellobiosides as active site-directed inhibitors. The optimal aglycon length for inactivation diff...
متن کاملMechanism-Based Studies of the Active Site-Directed Inhibition and Activation of Enzyme Transketolase
Derivatives of phenyl-keto butenoic acids have been reported to be inhibitors of pyruvate decarboxylase, (PDC). The inhibition of transketolase, a thiamine requiring enzyme such as PDF, by meta nitrophenyl derivative of 2-oxo-3-butenoic acid (MNPB) is reported here. These studies indicate that the inhibitor binds to the enzyme at the active site. A two-step inhibition was observed, first th...
متن کاملThe Non-competitive Inhibition of Brain
A non-competitive inhibition by glucose-6-P1 of brain (1, 2) and other animal tissue (1) hexokinases has been described, as well as a similar inhibition of brain hexokinase by L-sorbose-1-P (3). The present paper is concerned with the specificity for inhibition of brain hexokinase by glucose6-P and related compounds. Ry means of a comparison of the structures of twenty-five compounds, six of xv...
متن کاملIdentification of Plasmodium falciparum spermidine synthase active site binders through structure-based virtual screening.
Seven novel binders, binding in the active site of Plasmodium falciparum spermidine synthase, were identified by structure-based virtual screening. The binding of these compounds was experimentally verified by NMR techniques. Spermidine synthase, an enzyme involved in the polyamine pathway, has been suggested as a target for treating malaria. The virtual screening protocol combined 3D pharmacop...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Chemical Biology & Drug Design
سال: 2010
ISSN: 1747-0277,1747-0285
DOI: 10.1111/j.1747-0285.2010.00972.x