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Q: In a different enzyme which binds polyketide substrates (a compound with multiple carbonyl groups), you might expect to find which amino acids in the binding site to stablise the binding of the substrate?
The dynamic site is fit as a fiddle of a three-dimensional separated that is made out of amino acids from various buildups of the essential amino corrosive grouping. The amino acids that assume a critical part in the coupling specificity of the dynamic site are normally not neighboring each other in the essential structure, however shape the dynamic site as an aftereffect of collapsing in making the tertiary structure. This dynamic site locale is moderately little contrasted with whatever is left of the catalyst. Like a ligand-restricting site, the dominant part of a compound (non-restricting amino corrosive deposits) exist essentially to serve as a system to bolster the structure of the dynamic site by giving right introduction. The remarkable amino acids contained in a dynamic site advance particular connections that are fundamental for appropriate authoritative and coming about catalysis. Catalyst specificity relies on upon the game plan of molecules in the dynamic site.
Correlative shapes amongst protein and substrate(s) permit a more noteworthy measure of frail non-covalent associations including electrostatic powers, Van der Waals strengths, hydrogen holding, and hydrophobic communications. Particular amino acids likewise permit the arrangement of hydrogen bonds. That demonstrates the uniqueness of the microenvironment for the dynamic site.
A reactant group of three alludes to the three amino corrosive deposits that capacity together at the focal point of the dynamic site of some hydrolase and transferase catalysts (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases).
An Acid-Base-Nucleophile group of three is a typical theme for producing a nucleophilic deposit for covalent catalysis.
The deposits frame a charge-transfer system to spellbind and initiate the nucleophile, which assaults the substrate, shaping a covalent middle of the road which is then hydrolysed to recover free chemical and discharge the item.
The nucleophile is most usually a serine or cysteine amino corrosive, however every so often threonine. Since catalysts overlay into complex three-dimensional structures, the buildups of a synergist set of three can be a long way from each other along the amino-corrosive grouping (essential structure), be that as it may, they are united close in the last crease
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A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
biochemistry if you could please help me answer the following questions! * 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
I have the need to complete the sentences. Thanks for your help < Energy and Enzymes Building Vocabulary: Enzymes Part A Drag the terms on the left to the appropriate blanks on the right to complete the sentences. Reset Help an enzyme, causing it to lose its shape and High temperatures or changes in pH can biological activity Enzymes speed up chemical reactions by lowering the proceed much more quickly An enzyme is considered a(n) used up activation energy induced...
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biochemistry if you could please help me answer the following questions! 741) (5 pts) Transition state theory relates the rate constant to the free energy of activation, AG. How can enzymes reduce the activation energy barrier? a) decrease the free energy of the product b) high affinity binding to the transition state c) increase the free energy of the substrate d) increase entropy upon release of product e) bind to the substrate with high affinity 2) (5 pts) Which is...
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high and detecting one product at a time Question 77 The initial velocity of an enzyme reaction (vo) describes A) The concentration of the enzyme at maximal velocity B) The concentration of substrate at maximal velocity C) The concentration of both at the start of the reaction D) The rate of the reaction when the substrate and enzyme are first med Question 78 What is the shape of a typical plot of initial rate vs substrate concentration tres kinetics? A)...
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