1btu: Difference between revisions
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Revision as of 15:52, 30 October 2007
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PORCINE PANCREATIC ELASTASE COMPLEXED WITH (3S, 4R)-1-TOLUENESULPHONYL-3-ETHYL-AZETIDIN-2-ONE-4-CARBOXYLIC ACID
OverviewOverview
beta-Lactam inhibitors of transpeptidase enzymes involved in cell wall, biosynthesis remain among the most important therapeutic agents in, clinical use. beta-Lactams have more recently been developed as inhibitors, of serine proteases including elastase. All therapeutically useful, beta-lactam inhibitors operate via mechanisms resulting in the formation, of hydrolytically stable acyl-enzyme complexes. Presently, it is difficult, to predict which beta-lactams will form stable acyl-enzyme complexes with, serine enzymes. Further, the factors that result in the seemingly special, nature of beta-lactams versus other acylating agents are unclear-if indeed, they exist. Here we present the 1.6 A resolution crystal structure of a, stable acyl-enzyme complex formed between porcine pancreatic ... [(full description)]
About this StructureAbout this Structure
1BTU is a [Single protein] structure of sequence from [Sus scrofa] with CA, SO4 and 2BL as [ligands]. Active as [Pancreatic elastase], with EC number [3.4.21.36]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
Inhibition of elastase by N-sulfonylaryl beta-lactams: anatomy of a stable acyl-enzyme complex., Wilmouth RC, Westwood NJ, Anderson K, Brownlee W, Claridge TD, Clifton IJ, Pritchard GJ, Aplin RT, Schofield CJ, Biochemistry. 1998 Dec 15;37(50):17506-13. PMID:9860865
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