When transaminated, the three branched-chain amino acids (valine, leucine, and isoleucine) form compounds that have the characteristic odor of maple syrup. Anenzyme called a-keto acid dehydrogenase converts these compounds into CoA esters. Give the structure of the valine-derived compound that smells like maple syrup.Draw the molecule on the canvas by choosing buttons from the Tools (for bonds), Atoms, and Advanced Template toolbars. The single bond is active bydefault.NN[1]A21H2D EXP.LLCONT.17Marvin JSby ChemAxon&HCNOSCIBr1PLLF

Maple syrup urine disease is caused by a deficiency in the branched-chain α-keto acid dehydrogenase…

Answered: When transaminated, the three…

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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The four-carbon sugar erythrose-4-phosphate is the starting material in the synthesis of many compounds. Name two important examples.
Draw the first tetrahedral intermediate of the chymotrypsin mechanism (a single structure, no arrows required). Circle the oxyanion hole. How does the oxyanion hole of chymotrypsin compare to that of carboxypeptidase?
There are two competing processes for the manufacture of lactic acid, chemical and biochemical syntheses. The chemical synthesis involves the hydrocyanation of acetaldehyde, while the biochemical synthesis involves the fermentation of sugars or starch. Discuss the TWO advantages and THREE disadvantages of synthesising lactic acid via the biochemical route.
A carboxypeptidase is a metalloenyme (its active site contains one or more metal ions essential for the function) that catalyzes the hydrolysis of the peptide bond of the terminal amino acid of a polypeptide chain (where the free carboxyl group occurs). The binding of an L-alanyl-L-tyrosine peptide substrate in the active site of the enzyme is represented in the scheme below: Glu Zn++ COO™ OH H3C CH₂ HC NH IO C H H Poche apolaire -H H O+N: C N H H H NH₂ Arg 145 Туг 248 NB: This scheme gives a planar representation of the spatial structure of the active site where indicated contacts (hatched lines) are supposed to occur in the 3D structure of the enzyme. 1- Describe the interactions that occur between the ligand and amino acid residues of the active site. 2- What would be the impact on the Km value if we replace L-alanyl-L-tyrosine by the following substrates: L-alanyl-L-phenylalanine; L-alanyl-L-aspartate; L-aspartyl-L- tyrosine.
The glycine cleavage system is a group of four enzymes that together catalyze the following reaction: Use the following information to determine the sequence of reactions carried out by the glycine cleavage system:a. The first enzyme is a PLP-requiring decarboxylase.b. The second enzyme is aminomethyltransferase. This enzyme has a lipoate coenzyme.c. The third enzyme synthesizes N5,N10-methylene-THF and also forms +NH4.d. The fourth enzyme is an FAD-requiring enzyme.e. The cleavage system also requires NAD+ .
the following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.
Progesterone is a female hormone that plays a critical role in the menstrual cycle by preparing the lining of the uterus for implantation of an egg. During W. S. Johnson's biomimetic synthesis of progesterone (a synthesis that draws inspiration from and mimics naturally occurring, biosynthetic pathways), one of the final reactions in the synthesis was believed to have proceeded via the following intermediate. Use resonance structures to explain why this intermediate is particularly stable. (J. Am. Chem. Soc. 1971, 93,4332-4334). SHAR
With the aid of the simple generic diagram, identify and explain how the type of chemical bonding stabilizes a secondary structure present in 3GRS (glutathione reductase).
A picture of the two disaccharide repeats of hyaluronic acid are shown below. Name the two different glycosidic linkages. Are these the same linkages as those found in glycogen?
Define aminoacyl (A) site
Homocystinuria is caused by a defect in cystathionine beta-synthase (or 13-synthase), which leads to an accumulation of homocysteine in the blood. This accumulation causes symptoms such as a tall, thin frame, flushed cheeks, and osteoporosis (thinning of the bones). These individuals should limit their intake of proteins that contain methionine, such as egg whites. Using your understanding of biochemistry, explain why people with Homocystinuria should not consume egg whites and other such proteins.
An oligosaccharide is a repeating unit of a-D-galactopyranosyl-(a-1 >3)-allopyranoside. Each disaccharide unit is linked via B-1 --->4 glycosidic bond. The oligosaccharide has 10 monosaccharide residues. Required: Is this oligosaccharide a good substrate for glycolysis? Why or why not? Provide two reasons and discuss corn prehensively.

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