Help me please dear ! Question 5The first step in the catabolism of most amino acids is which of the following?Transfer of alpha amino group to alpha ketoglutarateTransfer of the alpha carboxylate group to alphe ketoglutarateOxidation of the amine group to C=OO Decarboxylation of the CO2 group

Amino acids are biomolecules that have an amino group, a carboxyl group and a side group linked to…

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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QUESTION 26 In the câtalytic mechanism of an aminotransferase, one substrate binds and reacts, leaving behind an amine group covalently attached to the enzyme, then the second substrate can bind. This is best described as: Association dissociation O random single displacement ping-pong or double displacement O ordered single displacement QUESTION 27 For a Michaelis-Menten enzyme, kį = 4.0 x 10° M's,k] = 2.0 x 10° s-!, and kɔ = 5.0 x 10 s What is its Km? Give your answer in uM in four significant figures in normal notation. QUESTION 28 Which amino acid is most likely to break an alpha helix? Click Save and Submit to save and submit. Click Save All Answers to save all answers. 798 Mostly cloudy P Type here to search
Question 8 The major structural component of the exoskeletons of invertebrates is composed of N-acetyl-B-D-galactosamine joined by B-1,4-glycosidic bonds True False
Question 12 In the tertiary structure of a protein, the R-group of valine can interact with the R-group of via a _ O leucine; hydrophobic interaction O lysine, electrostatic interaction O threonine, hydrogen bond alanine; hydrogen bond
QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
Question 5 An a-helix has the sequence: NH3-Ser-Glu-Gly-Asp-Trp-Gln-Leu-His-Val-Phe-Ala-Lys-Val-Glu- COO-. The carbonyl oxygen (in the peptide bond) of the W5 residue is hydrogen bonded to the amide nitrogen of H8 E2 O V9 O S1
QUESTION 10 UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?
Question 5 The core protein of a proteoglycan is noncovalently attached to: O oligosaccharides. glycosaminoglycans O keratin sulfate. O hyaluronic acid backbone
QUESTION 10 In the deoxy state of HB, which of the following does not occur? O An intra-chain salt bridge between Val 98 and Tyr 145. O An intra-chain salt bridge between Histidine 146 and Aspartate 94 side chains O A peptide bond between Tyr 145 and His 146. O An inter-chain salt bridge between Histidine 146 and Lys 40
QUESTION 10 Catabolic metabolic pathways generally involve what type of chemical reactions? Reactions that are spontaneous inside an active cell. Reactions that require the use of energy. Reactions that result in the release energy. Reactions that build complex molecules.
Question 20 of 25 The figure below illustrates what reactions of amino acids? coo C=0 CH₂ CH₂ =0 00 + NHⒸ Decarboylation Cystine formation Esterification Transamination Peptide bond formation Transmethylation NAD(P)H+H Oxidative deamination Amide formation NAD(P) H₂ +H₂O COO CH₂ I میں CH₂ COOⒸ ATP ADP +P₁ H₂N-CH NHO CH₂ CH₂ NH₂ 20
Question 10 Proteoglycans are often made up of glycosaminoglycans (chondroitin sulfate, keratan sulfate, and dermatan sulfate) that are covalently linked to a core protein. O True O False
QUESTION 18 Stable molecules that resemble the transition state of enzyme catalyzed reactions are very potent inhibitors. Provide an explanation as to why these compounds are better than inhibitors based on the substrate. TT TT Paragraph v v 3 (12pt) = - E · T Arial T T, O Mashups 66 HTHL CSS CS Scanned with CamScanner

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The first step in the catabolism of most amino acids is which of the following? Transfer of alpha amino group to alpha ketoglutarate Transfer of the alpha carboxylate group to alphe ketoglutarate Oxidation of the amine group to C=O Decarboxylation of the CO2 group