Search results for "enzyme substrate complex"
showing 2 items of 2 documents
Retarded Elimination of a High-Molecular Enzyme-Substrate-Complex after Hydroxyethyl-Starch-Infusion
1978
During a pharmacokinetic study with hydroxyethyl starch we found, that this plasma substitute induces a regular increase of serum amylase. In 54 patients after infusion of 500 ml 6% hydroxyethyl starch (HES) an increase of serum amylase was observed, which in 51 cases exceeded the upper limit of normal (190 U/l). In most cases serum amylase reached values twice as high as the basal value. Renal function influenced duration of increased serum amylase values, but did not influence maximum increases (201 ±15 U/l; mean ± SEM). In patients with advanced renal failure (GFR = 2–10 ml/min) serum amylase was still markedly elevated after 72 hours (298 ± U/l; mean ± SEM). In patients with normal rena…
Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site
2003
Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a …