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==4Q7Q Structure and Proposed Functionality== | ==4Q7Q Structure and Proposed Functionality== | ||
(NOTE TO ALL EDITORS: This page is part of a final project for a biochemistry lab at Elizabethtown College. Please do not edit this.) | (NOTE TO ALL EDITORS: This page is part of a final project for a biochemistry lab at Elizabethtown College. Please do not edit this. -Neil Divins) | ||
4Q7Q is a homodimeric protein complex that originates from the bacterial species Chitinophaga Pinensis and has a mass of 58.5 kDa. It is a member of the SGNH Hydrolase Superfamily with structural and sequential similarities to esterases and lipases. Current evidence suggests it causes the hydrolysis of esters and/or acetyl groups on lipids/lipid-like molecules via a serine protease-like active site. | 4Q7Q is a homodimeric protein complex that originates from the bacterial species Chitinophaga Pinensis and has a mass of 58.5 kDa. It is a member of the SGNH Hydrolase Superfamily with structural and sequential similarities to esterases and lipases. Current evidence suggests it causes the hydrolysis of esters and/or acetyl groups on lipids/lipid-like molecules via a serine protease-like active site. | ||
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We also believe 4Q7Q undergoes several significant structural changes during enzymatic activities. Analysis into other members of its family reveal mechanisms wherein serine and histidine residues shift during substrate binding. <ref name="GDSL" /> | We also believe 4Q7Q undergoes several significant structural changes during enzymatic activities. Analysis into other members of its family reveal mechanisms wherein serine and histidine residues shift during substrate binding. <ref name="GDSL" /> | ||
== Experimental Data == | |||
</StructureSection> | </StructureSection> | ||
