In the majority of cases, amino acid catabolism can be broken down into a two-step process; ‘transamination’ followed by ‘oxidative deamination’. Serine doesn’t follow this two-step process; fully explain the reaction and mechanism involved in the degradation process used to form its α-keto acid.

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the structures of chymotrypsin and other serine proteases revealed that the active sites of these enzymes shared a particular sterochemical arrangement of residues crucial to their activity. This came to be known as the catalytic triad, as it consisted of the oponyomous serine (Ser) residue, along with a histidine (His) and an aspartate (Asp) residue. Which of the following would result in the greatest decrease in function of the catalytic triad found in serine proteases? O Mutation to Ser, Cys, Asp O Mutation to Ser, His, Asp O Mutation to Cys, His, Asp O Mutation to Ser, His, Glu

H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14

Can u help me to explain to me, please? I stuggled my homework and i need help to understand it

Help filling in the blanks:   Pyridoxal phosphate, PLP, is produced from pyridoxine or vitamin B6. PLP is considered a/an [1C/2C/acyl/amino/carboxyl] carrier. In transaminases, PLP forms a [Schiff base/acetal/phosphoanhydride/condensation] with an amino acid and causes the [a- amino/a-carbon/a-carboxyl] to become [electrophilic/nucleophilic] allowing replacement of the amino group on the amino acid with a ketone. PLP is also used by several other enzymes that work on amino acids because in forming a covalent bond with amino acids it provides for an opportunity for nucleophilic attack and because PLP is conjugated, the cofactor is able to [delocalize/transfer/reduce/stabilize] pi electrons in the substrate and thus [stabilize/delocalize/transfer/reduce] the transition state of the reaction.     Production of citrulline occurs in the [cytosol/mitochondrial matrix] while the rest of the urea cycle occurs in the [cytosol/mitochondrial matrix]. Urea is produced in the…

Can u help me to explain to me, please? I stuggled. I don't understand The a-ketoglutarate that is produced inthe reaction is now free to accept a new quaternary ammonium group from another amino acid in a transamination reaction.

Phosphoribosyltransferase (PRT) catalyzes the attachment of a salvaged purine nitrogenous base on the activated form of ribose-5-phosphate called 5-phosphoribosyl- α α-pyrophosphate ( α α-PRPP). True Or False

Explain why people with a hereditary deficiency of carnitine acyltransferase II have muscle weakness. Why are the symptoms more severe during fasting?

Compare and contrast the biological roles of the following amino acids the following pairs ofamino acids. Once you have documented these role state which member of the pair is most important and why.