allosteric enzyme वाक्य
उदाहरण वाक्य
मोबाइल
- Allosteric enzymes are generally larger in mass than other enzymes.
- Allosteric enzymes are usually under the simultaneous control of several allosteric effectors.
- These simple molecular mechanisms account for the integrative properties of allosteric enzymes.
- These structurally distinct enzyme forms have been shown to exist in several known allosteric enzymes.
- Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species.
- Allosteric enzymes tend to have several subunits.
- This denotes the fact that allosteric enzymes change shape, or conformation, on binding of the modulator.
- "' Allosteric enzymes "'is an oligmer whose biological activity is affected by other substances binding to it.
- So far, however, the material presented to me has explicitly stated that allosteric enzymes do not exhibit Michaelis-Menten kinetics.
- PFK1 is an allosteric enzyme and has a structure similar to that of hemoglobin in so far as it is a dimer of a dimer.
- Allosteric enzymes include mammalian tyrosyl tRNA-synthetase, which shows negative cooperativity, and bacterial aspartate transcarbamoylase and phosphofructokinase, which show positive cooperativity.
- The use of hemilabile ligands allows structural motifs synthesized via the WLA to be modified in situ with small molecule effectors much like allosteric enzymes in biology.
- Similar to hexokinases 1 and 2, this allosteric enzyme is inhibited by its product glucose-6-phosphate . [ provided by RefSeq, Apr 2009]
- Therefore, regulatory enzymes, by its controlled activation and are of two types : allosteric enzymes and covalently modulated enzymes; however, an enzyme can combine both types of regulation.
- Monod first brings up allosteric enzymes that are capable of recognizing compounds other than a substrate whose association with the enzyme protein has a modifying effect of heightening or inhibiting the enzyme activity with respect to the substrate.
- Next Monod makes reference to his own research and talks about the S shaped non-linear curve that is characteristic of allosteric enzymes when activity is plotted against concentration of an effector ( including the substrate ).
- Negative signaling through SHIP appears to inhibit the Ras pathway through SH2 domain competition with Grb2 and Shc and may involve consumption of intracellular lipid mediators that act as allosteric enzyme activators or that promote entry of extracellular Ca2 +.
- The kinetic properties of allosteric enzymes are often explained in terms of a conformational change between a low-activity, low-affinity " tense " or T state and a high-activity, high-affinity " relaxed " or R state.
- The binding sites for heterotropic effectors, called allosteric sites, are usually separate from the active site yet thermodynamically coupled . "'Allosteric Database "'( ASD, http : / / mdl . shsmu . edu . cn / ASD ) provides a central resource for the display, search and analysis of the structure, function and related annotation for allosteric molecules, including allosteric enzymes and their modulators.
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