Sandbox 42: Difference between revisions
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== Active site and Binding == | == Active site and Binding == | ||
Hen white lysozyme's substrate binding site accomodates six residue oligosaccharides. Glu 35 and Asp 52 are the enzyme's active site residues. These residues have distinctly different microenvironments which are critical for their catalytic action. Asp 52 forms hydrogen bonds with surrounding residues including Asn46, Asp48, Ser50 and Asn59 on the anti-parallel beta-sheet and is negatively charged allowing for electrostatic stabilization of the reaction intermediate.<ref> PMID:19605465 </ref> Glu 35 conversely is surrounded by hydrophobic residues and its side chain stays protonated allowing for acid catalysis. Catalysis proceeds through the formation of a covalent intermediate. | Hen white lysozyme's substrate binding site accomodates six residue oligosaccharides. Glu 35 and Asp 52 are the enzyme's <scene name='Sandbox_42/Active_site/1'>active site residues</scene>active site residues. These residues have distinctly different microenvironments which are critical for their catalytic action. Asp 52 forms hydrogen bonds with surrounding residues including Asn46, Asp48, Ser50 and Asn59 on the anti-parallel beta-sheet and is negatively charged allowing for electrostatic stabilization of the reaction intermediate.<ref> PMID:19605465 </ref> Glu 35 conversely is surrounded by hydrophobic residues and its side chain stays protonated allowing for acid catalysis. Catalysis proceeds through the formation of a covalent intermediate. | ||
== References == | == References == | ||
<references/> | <references/> | ||
