Determine the type of biochemical reaction that occurs in the reaction shown below. O redox isomerization group transfer C-C bond formation/cleavage hydrolysis/condensation Ex-xx-xx OH (ATP) OH OH OH OH OH + AMP OPO₂² OH OH +AMP OH (ADP)
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- The biosynthesis of vitamin D₂ is a two-step reaction, requiring two types of concerted pericyclic reactions. Draw in the arrows for each step and identify the structure of precalciferol. If an electrocyclic reaction is required, identify if it occurs through a conrotatory or disrotatory reaction. HO H H ergosterol hv precalciferol Cast HO ergocalciferola What would be the appropriate name for an enzyme that catalyzes each of the following reactions: b H3C iOH OH NH₂ alanine ligase alanine oxidoreductase alanine isomerase alanine transferase OH H3C CH3 H3C NO₂ propanone transferase propan-2-ol hydrolase propan-2-ol oxidoreductase propan-2-ol isomerase OH H3C CH3Draw the amino acid product that results from a transamination reaction involving pyruvate and glutamate, shown in the image below. Draw the product as it would occur at the pH of most body fluids, including all charges. You do not need to draw the other product of the reaction. O NH3 3D CH3-C-C-o-+ 0-CH-CH CH2-C-0--→? pyruvate glutamate Draw the molecule on the canvas by choosing buttons from the Tools (for bonds), Atoms, and Advanced Template toolbars. The single bond is active by default. Include all hydrogen atoms and charges. > View Available Hint(s) CONT. H. N. NV CI Br 1] -C- C1 SI
- 1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Serios(i) During the Pyruvate Decarboxylase (PDC) catalysed reaction, a covalent coenzyme intermediate is formed. On the skeleton of the covalent coenzyme intermediate below draw the appropriate double bonds, charges, and electron pairs to illustrate the two resonance forms of this intermediate. Name each form in the boxes provided. HO S R' N -R HO S R' N -Rcomplete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.
- Functional groups and linkages assignment Complete the reactions below. Circle and identify all functional groups and linkages in reactants and products. Also identify the type of biochemical reaction. [10 A] a) CH3CH2CH2 C-N-CH2CH2CH2CH3 H2O > H.Given the following reaction, identify the class and subclass of the enzyme involved. H. CH2OH H-C-OH C=0 но-с-н но-с-н H-C-OH H-C-OH H-C-OH H-C-OH CH2OPO,2 CH2OPO,2- Class: [ Select] [ Select ] Ligase Hydrolase Lyase Subcla Transferase Isomerase OxidoreductasePhosphocreatine (G0ʹ = -43.1 kJ/mol) has a higher phosphoryl group transfer potential than ATP (G0ʹ = -30.5 kJ/mol). However, under certain physiological conditions, phosphoryl group is transferred from ATP to creatine. Explain this discrepancy. Many biochemical conversions are carried out via multi-step pathways although similar conversions can be done in an organic chemistry lab in fewer steps. Explain why energetically it is reasonable to use multiple steps in biochemical conversions. What are isozymes? Humans contain several isozymes of hexokinase. Why does the body need several isozymes of hexokinase? 1,3-bisphosphoglycerate is used to produce ATP. Which of the two phosphates of 1,3- bisphosphoglycerate is transferred to ADP to make ATP. Explain why it is this specific phosphate and not the other one. Triose phosphate isomerase is a diffusion-controlled enzyme. What reaction is catalyzed by this enzyme (structures of molecules not needed)? Explain why…
- Y,G,I,F,L,Y what is the biochemical propities of this residues.Enzyme X exhibits maximum activity at pH = 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. a Tyr residue on the enzyme is involved in the reaction. a His residue on the enzyme is involved in the reaction the enzyme uses NADH has a cofactor. the enzyme uses coenzyme A has a cofactor.HO-C-CH,-CH,~ Identify the enzyme needed in each of the following reactions as an isomerase, a decarboxylase, a dehydrogenase, a protease, or a phosphatase. о CH;-C-Č-OH → CH;-Č–H + CO, СНО CH,OH НС—ОН C=0 HO-CH — НО -СН НС—ОН НС—ОН HO-CH Но -СH CH-OPO,?- ČH-OPO,- Но -С—СН,—CH, —С—ОН — Но -С—СН—СH-С-ОН + 2Н H;N-CH-C-NH-CH-CO0 +H;O → CH; ČH3 2 H;N-CH-CO0- ČH3