opic a PROBLEMS 1. Carbo residues from its oxypeptidase, which sequentially remo
ID: 203260 • Letter: O
Question
opic a PROBLEMS 1. Carbo residues from its oxypeptidase, which sequentially removes carboxyl terminal amino aod peptide substrates, is a single polypeptide of 307 amino acids catalytic groups in the active site are furnished by Arg and Glu Explain how the two amino acid residues can catalyze a reaction in the space of a few angstroms 2. Fumarase catalyzes conversion of fumarate to malate: 3. The esters of fumarate and malate are not the substrates of fumarase. What interactions arise between the fumarase active site and the substrate molecule? 3. The velocity of peptide hydrolysis depends on the nature of amino acid R-graup at the N-end of the peptide. Iit increases in the sequence: Presence in the side chain of such functional groups as -cooH, -NH -OH decreases the velocity of hydrolysis. What bonds are formed between the substrate molecule and active site? 4. Name the class of the enzymes catalyzing the following reactions: 2. HOOC-CH(CH1-COSCoA HOOC-CHrCHrcoscoA 3. H,N-CO-NHz +H2O CO2 +2NH, 4. CH,-CO-COOH+ NH, + NADH H' CHrCH(NH.)-COOH + NAD, Hr 5. HOOC-CHeCH-COOH + H2O HOOC-CHz-CH(OH)-COOH 6, Galactose + ATP galactose 1-phosphate + ADP 7. R-CHrCHrCOOH + Enzyme-FAD-R-CH:CH-COOH + Enzyme-FADH2 8, coz + CH3-CO-COOH+ ATP HOOC-CHrCO-COOH + ADP + HsPO4 NH + HN-CO-NH 10. CH3-CH(NHz)-COOH CH,-CH-COOH + NH3 1. A mutant form of LDH in which Argm in the active site is replaced with Gln shows only 5% of the pyruvate binding and 0,07% of the activity of wild-type enzyme. Provide a plausible explanation for the effects of this mutation 23Explanation / Answer
Carboxypeptidase is metalloenzyme consists of Zn+2 as a metal cofactor at the active site, along with five amino acid residues involved in substrate binding: Arg-71, Arg-127, Asn-144, Arg-145, Tyr-248, and Glu-270.
Arg145 and Glu270 are the catalytic residues. Substrate hydrolysis is initiated by nucleophilic attack of Glu-270 on the peptide carbonyl group.
4.1) pyruvate decarboxylase
2) Methyl malonylCoA mutase
3) UREASE
4) Transaminase
6) Galactokinase
7) acyl CoA dehydrogenase
8) Pyruvate carboxylase
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