Question

Consider the trypsin binding-pocket specificity structure scenario and critical AAs interactions within: G226-D189-G216 (see slide): a single nucleotide polymorphism within the D189 codon resulted in a first nucleotide Guanine replacement by Cytosine. What is the consequence of this mutation relative to binding pocket- substrate specificity?

Enzymes vary in specificity pocket Vary in amino acids in pocket Controls chemical environment Scissile bond Also controls pocket dimensions Chymotrypsin Gly residues make deep pocket Pocket fits aromatic ring Phe Gly 216 Trypsin Gly 226 Pocket same dimensions as chymotrypsin, but different side chain at bottom Ser 189 Asp () readily binds Lys (+) or Arg (+) ys Ala Gly 216 Thr 216 Elastase Val 226 Bulkier groups on walls of pocket Pocket smaller Binds small nonpolar side chains Asp 189 Trypsin Elastase

Answer 1

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