By John W. Pelley PhD
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Additional resources for Elsevier's Integrated Review Biochemistry: With STUDENT CONSULT Online Access, 2e
3-2). , dipeptide [two amino acids] or oligopeptide [relatively few amino acids]). The properties of a polypeptide are determined by the side chains of their amino acids. PATHOLOGY Hemoglobin Mutations Sickle cell hemoglobin (HbS) and hemoglobin C (HbC) both have single amino acid substitutions in residue 6 of the bglobin. Sickle cell globin has a nonpolar substitution (valine) for the normal polar residue (glutamate), whereas hemoglobin C has a polar substitution (lysine) for the polar glutamate.
L A single substrate (S) binds reversibly to form the enzyme substrate complex, ES. KEY POINTS ABOUT ACTIVE SITE PROPERTIES n Amino acid residues of the active site may be far apart in the primary structure owing to the folding required for tertiary structure. n The active site is induced to undergo a change in conformation when the substrates bind. n The requirements for substrate binding are so specific that the amino acids forming the active site for the same enzyme are highly conserved between different species.
L Affinity labels are substrate analogs that react with one or more of the amino acids that make up the active site; sequence determination of the labeled enzyme allows identification of active site amino acids. l X-ray diffraction analysis with either the substrate or a transition state analog bound to an active site reveals spatial relationships within the active site. l Site-directed mutagenesis creates mutant enzymes with amino acid substitutions at active sites; substitutions that alter normal activity help identify amino acids crucial to the active site.
Elsevier's Integrated Review Biochemistry: With STUDENT CONSULT Online Access, 2e by John W. Pelley PhD