Sandbox Reserved 994: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Corey Mier (talk | contribs) No edit summary |
No edit summary |
||
| Line 26: | Line 26: | ||
[[Image:B-lactam hydrolysis3.png|800px|left|thumb|alt=text|β-lactam antibiotics (basic structure of a β-lactam is shown above) are hydrolyzed by β-lactamase enzymes, utilizing a covalent catalysis serine-based mechanism. The β-lactamase cleaves the amide bond of the four membered ring which renders the antibiotic inactive before it reaches its bacterial target, the transpeptidase enzymes.]] | [[Image:B-lactam hydrolysis3.png|800px|left|thumb|alt=text|β-lactam antibiotics (basic structure of a β-lactam is shown above) are hydrolyzed by β-lactamase enzymes, utilizing a covalent catalysis serine-based mechanism. The β-lactamase cleaves the amide bond of the four membered ring which renders the antibiotic inactive before it reaches its bacterial target, the transpeptidase enzymes.]] | ||
[[Image:Beta-lactamase resized mechanism.png|500px| | [[Image:Beta-lactamase resized mechanism.png|500px|none|thumb|alt=text|The mechanism of attack involves a catalytic serine residue, a carboxylated lysine, and another active site serine which contributes to proton movement (A). A high energy tetrahedral intermediate (B) is generated and an acyl enzyme intermediate (C) is formed after the cleavage of the four-membered ring. KCX84 activates the deacylating water which completes the reaction leaving a hydrolyzed β-lactam ring and a regenerated β-lactamase.<ref name="Leonard" />]] | ||
<scene name='69/691536/Closeupdrug/1'>close up</scene><ref>PMID: 10817708</ref> | <scene name='69/691536/Closeupdrug/1'>close up</scene><ref>PMID: 10817708</ref> | ||
