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Protein crystallography enzymatic mechanism studies

Hen egg white lysozyme is a small protein of Mr 14 500 and 129 amino acid residues. This enzyme was introduced in Chapter 1, where it was pointed out that examination of the crystal structure of the enzyme stimulated most of the solution studies. Hen egg white lysozyme has the distinction of being the first enzyme to have had its structure solved by x-ray crystallography.207 It is an atypical member of the hexosaminidase class of glycosyl transfer enzymes. It catalyzes the hydrolysis of substrates with retention of stereochemistry. T4 lysozyme was for many years thought to have the same fold and mechanism of lysozyme, despite there being no sequence homology. But it has now been found that the T4 enzyme has inversion of configuration and so operates by a different mechanism.208,209 A mechanism proposed for the enzymatic reaction was based on the structure of the... [Pg.587]


See other pages where Protein crystallography enzymatic mechanism studies is mentioned: [Pg.154]    [Pg.183]    [Pg.24]    [Pg.607]    [Pg.371]    [Pg.423]    [Pg.2779]    [Pg.147]    [Pg.1]    [Pg.2778]    [Pg.213]    [Pg.170]    [Pg.397]   


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