Chymotrypsin: Difference between revisions
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==Substrate binding and catalysis== | ==Substrate binding and catalysis== | ||
<Structure load='7gch' size='300' frame='true' align='right' caption='[[7gch]] Bovine chymotrypsin with bound inhibitor' scene='38/387136/Bovine_chymotrypsin_overview/ | <Structure load='7gch' size='300' frame='true' align='right' caption='[[7gch]] Bovine chymotrypsin with bound inhibitor' scene='38/387136/Bovine_chymotrypsin_overview/3' /> | ||
[[Image:LPFstructure.jpg|left]] | [[Image:LPFstructure.jpg|left]] | ||
Features of the substrate binding site can be seen in the structure of bovine chymotrypsin bound to the inhibitor N-acetyl-L-leucyl-L-phenylalanyl trifuoromethyl ketone (Ac-Leu-Phe-CF<sub>3</sub>), which resembles a peptide substrate (see structure in left figure). The colored backgrounds in the figure indicate the four components of structure and shows the bond (yellow on black background) that is position to be cleaved. The default scene shows the three peptide chains of chymotrypsin in spacefill and colored tuquoise, beige, and violet. The inhibitor, which is shown in CPK ball & stick, is sitting in the active site. In this <scene name='38/387136/Bovine_chymotrypsin_active_sit/1'>closeup of the active site</scene>, the residues of catalytic triad are shown in CPK ball & stick and labelled, and the inhibitor is in light gray ball & stick with its phenyl group in orchid. By moving the structure back and forth with your mouse, it is easy to see that the phenyl group is located in the hydrophobic binding pocket of the enzyme. The binding pocket determines the enzyme's preference for cleavage of peptides on the C-terminal side of aromatic residues. | Features of the substrate binding site can be seen in the structure of bovine chymotrypsin bound to the inhibitor N-acetyl-L-leucyl-L-phenylalanyl trifuoromethyl ketone (Ac-Leu-Phe-CF<sub>3</sub>), which resembles a peptide substrate (see structure in left figure). The colored backgrounds in the figure indicate the four components of structure and shows the bond (yellow on black background) that is position to be cleaved. The default scene shows the three peptide chains of chymotrypsin in spacefill and colored tuquoise, beige, and violet. The inhibitor, which is shown in CPK ball & stick, is sitting in the active site. In this <scene name='38/387136/Bovine_chymotrypsin_active_sit/1'>closeup of the active site</scene>, the residues of catalytic triad are shown in CPK ball & stick and labelled, and the inhibitor is in light gray ball & stick with its phenyl group in orchid. By moving the structure back and forth with your mouse, it is easy to see that the phenyl group is located in the hydrophobic binding pocket of the enzyme. The binding pocket determines the enzyme's preference for cleavage of peptides on the C-terminal side of aromatic residues. | ||
