Sandbox Wabash5
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
Trypsin is a serine protease that contains serine, histidine<scene name='72/725334/Beidou_test_his/3'>HIS</scene>, and aspartic acid residues. Trypsin catalyzes peptide bond hydrolysis through acid catalysis, base catalysis, and covalent catalysis. In the first step serine acts as a nucleophile to attack the substrate peptide bond, which forms a tetrahedral intermediate via covalent catalysis. Then a acyl-enzyme intermediate is formed and the C-terminal fragment is released. A water molecule attacks the acyl enzyme leading to the creation of a second tetrahedral intermediate. This is followed by the release of the N-terminal fragment, which results in the creation of the active enzyme. | Trypsin is a serine protease that contains serine, histidine<scene name='72/725334/Beidou_test_his/3'>HIS</scene>, and aspartic acid residues. Trypsin catalyzes peptide bond hydrolysis through acid catalysis, base catalysis, and covalent catalysis. In the first step serine acts as a nucleophile to attack the substrate peptide bond, which forms a tetrahedral intermediate via covalent catalysis. Then a acyl-enzyme intermediate is formed and the C-terminal fragment is released. A water molecule attacks the acyl enzyme leading to the creation of a second tetrahedral intermediate. This is followed by the release of the N-terminal fragment, which results in the creation of the active enzyme. | ||
| + | |||
| + | Scene 1:catalytic triad <scene name='72/725334/Catalytic_triad/1'>catalytic triad</scene> | ||
BY: MICHAEL GREEN AND AARON BECKER AND BEIDUO CHENG | BY: MICHAEL GREEN AND AARON BECKER AND BEIDUO CHENG | ||
Revision as of 21:42, 18 February 2016
The Mechanism of Trypsin
| |||||||||||
