Term
| Chymotrypsin cleaves peptides at the carboxyl side of which amino acids? |
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Definition
| Chymotrypsin cleaves peptides at the carboxyl side of tyrosine, tryptophan, and phenylalanine because these three amino acids contain aromatic rings, which fit into a 'hydrophobic pocket' in the enzyme |
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Term
| Trypsin predominantly cleaves peptide chains at the carboxyl side of what amino acids? |
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Definition
| Trypsin predominantly cleaves peptide chains at the carboxyl side of the amino acids lysine and arginine, except when either is followed by proline |
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Term
| Where does pepsin cleave amino acids? |
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Definition
| the N-terminal of aromatic amino acids such as phenylalanine, tryptophan, and tyrosine |
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Term
| Where does carboxypeptidase cleave at? |
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Definition
| hydrolyzes the carboxy-terminal (C-terminal) end of a peptide bond |
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Term
| Assuming Michaelis-Menton kinetics, the slope of the line in a Lineweaver-Burk plot is equal to? |
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Definition
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Term
| People who have urea cycle defects must maintain a high caloric diet. What is the best explanation for this? |
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Definition
| A high caloric diet prevents the breakdown of muscle protein to amino acids. |
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Term
| describe the catabolism of most amino acids that are not immediately required for protein synthesis |
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Definition
| The amino group is transferred to a-ketoglutarate and the remaining a-keto acid is metabolized to a TCA cycle intermediate or to acetyl CoA. |
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