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The crystal structure of an HSL-homolog EstE5 complex with PMSF reveals a unique configuration that inhibits the nucleophile Ser144 in catalytic triads
The crystal structure of an HSL-homolog EstE5 complex with PMSF reveals a unique configuration that inhibits the nucleophile Ser144 in catalytic triads
http://www.piercenet.com/product/pmsf-phenylmethylsulfonyl-fluoride
http://www.piercenet.com/product/pmsf-phenylmethylsulfonyl-fluoride
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Hormone-sensitive lipase can be inhibited by phenylmethylsufonyl flouride (PMSF) entering into the active site. PMSF inhibits enzymes by binding to the serine residue of the serine protease active sites so that the normal catalytic activity cannot be carried out. This inhibitor will only bind to the active site serine because of its increased activity from being in the catalytic triad.
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==References==
==References==
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<references />

Revision as of 23:34, 30 March 2014

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[1]

Structure

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References

  1. Kanwar SS, Kaushal RK, Jawed A, Gupta R, Chimni SS. Methods for inhibition of residual lipase activity in colorimetric assay: a comparative study. Indian J Biochem Biophys. 2005 Aug;42(4):233-7. PMID:23923547
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