1euf
From Proteopedia
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BOVINE DUODENASE(NEW SERINE PROTEASE), CRYSTAL STRUCTURE
Overview
The three-dimensional structure of duodenase, a serine protease from, bovine duodenum mucosa, has been determined at 2.4A resolution. The, enzyme, which has both trypsin-like and chymotrypsin-like activities, most, closely resembles human cathepsin G with which it shares 57% sequence, identity and similar specificity. The catalytic Ser195 in duodenase adopts, the energetically favored conformation typical of serine proteinases and, unlike the strained state typical of lipase/esterases. Of several waters, in the active site of duodenase, the one associated with Ser214 is found, in all serine proteinases and most lipase/esterases. The conservation of, the Ser214 residue in serine proteinase, its presence in the active site, and participation in a hydrogen water network involving the catalytic, triad (His57, Asp107, and Ser195) argues for its having an important role, in the mechanism of action. It may be referred to as a fourth member of, the catalytic triad. Duodenase is one of a growing family of enzymes that, possesses trypsin-like and chymotrypsin-like activity. Not long ago, these, activities were considered to be mutually exclusive. Computer modeling, reveals that the S1 subsite of duodenase has structural features, compatible with effective accommodation of P1 residues typical of trypsin, (Arg/Lys) and chymotrypsin (Tyr/Phe) substrates. The determination of, structural features associated with functional variation in the enzyme, family may permit design of enzymes with a specific ratio of trypsin and, chymotrypsin activities.
About this Structure
1EUF is a Single protein structure of sequence from Bos taurus with NAG and PO4 as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of bovine duodenase, a serine protease, with dual trypsin and chymotrypsin-like specificities., Pletnev VZ, Zamolodchikova TS, Pangborn WA, Duax WL, Proteins. 2000 Oct 1;41(1):8-16. PMID:10944388
Page seeded by OCA on Tue Nov 20 14:19:30 2007
