Sandbox Reserved 468: Difference between revisions
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Taken from a publication of the crystal structure [3]. | Taken from a publication of the crystal structure [3]. | ||
[[Image:MMP_crystal.jpg]] | [[Image:MMP_crystal.jpg]] | ||
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'''Linker region''' | '''Linker region''' | ||
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Taken from a publication of the crystal structure [3]. | Taken from a publication of the crystal structure [3]. | ||
[[Image:Linker.jpg]] | [[Image:Linker.jpg]] | ||
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'''Hemopexin-like domain''' | '''Hemopexin-like domain''' | ||
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In the third mechanism, the Manzetti-mechanism, Manzetti Sergio and colleagues showed that the interaction between water and zinc during catalysis was unlikely. They then suggested a third mechanism where a histidine participates in catalysis by allowing the Zn2+ ion to assume a quasi-penta coordinated state. In this state, the Zn2+ ion is coordinated with the two oxygen atoms from the catalytic glutamic acid, the substrate's carbonyl oxygen atom, and the two histidine residues, and can polarize the glutamic acid's oxygen atom, proximate the scissile bond, and induce it to act as reversible electron donor. This forms an oxyanion transition state. At this stage, a water molecule acts on the dissociated scissile bond and completes the hydrolyzation of the substrate [5][6]. | In the third mechanism, the Manzetti-mechanism, Manzetti Sergio and colleagues showed that the interaction between water and zinc during catalysis was unlikely. They then suggested a third mechanism where a histidine participates in catalysis by allowing the Zn2+ ion to assume a quasi-penta coordinated state. In this state, the Zn2+ ion is coordinated with the two oxygen atoms from the catalytic glutamic acid, the substrate's carbonyl oxygen atom, and the two histidine residues, and can polarize the glutamic acid's oxygen atom, proximate the scissile bond, and induce it to act as reversible electron donor. This forms an oxyanion transition state. At this stage, a water molecule acts on the dissociated scissile bond and completes the hydrolyzation of the substrate [5][6]. | ||
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'''Inhibition''' | '''Inhibition''' | ||
