A catalog of stream processing optimizations

Cataloged from PDF version of article.Various research communities have independently arrived at stream processing as a programming model for efficient and parallel computing. These communities include digital signal processing, databases, operating systems, and complex event processing. Since each community faces applications with challenging performance requirements, each of them has developed some of the same optimizations, but often with conflicting terminology and unstated assumptions. This article presents a survey of optimizations for stream processing. It is aimed both at users who need to understand and guide the system's optimizer and at implementers who need to make engineering tradeoffs. To consolidate terminology, this article is organized as a catalog, in a style similar to catalogs of design patterns or refactorings. To make assumptions explicit and help understand tradeoffs, each optimization is presented with its safety constraints (when does it preserve correctness?) and a profitability experiment (when does it improve performance?). We hope that this survey will help future streaming system builders to stand on the shoulders of giants from not just their own community. © 2014 ACM

Characterization of the purified vitamin K-dependent gamma-glutamyl carboxylase.

Vitamin K-dependent carboxylase, purified from bovine liver, has properties similar to those reported for the carboxylase activity present in crude, solubilized microsomes. The purified carboxylase was found to possess the vitamin K epoxidase activity, believed to be essential for vitamin K-dependent carboxylation, but did not contain vitamin K epoxide reductase activity. Kinetic studies of the carboxylase done under defined conditions were complicated by the non-Michaelis-Menten kinetic behavior observed for reactions with two of the enzymes substrates, FLEEL and vitamin K1 hydroquinone. Initial rate experiments with the substrate FLEEL demonstrated behavior consistent with substrate inhibition and gave half-maximal activity at 1 mM FLEEL. Experiments with the substrate vitamin K1 hydroquinone also displayed non-Michaelis-Menten kinetics, as maximal activity was reached prematurely in relation to behavior at lower concentrations. Half-maximal activity was observed at 35 microM vitamin K1 hydroquinone. Initial rate experiments with varying NaH14CO3 concentration displayed Michaelis-Menten kinetics and gave a Km(app) of 0.29 mM. At cosubstrate concentrations chosen to obtain near-maximal activity, initial rate studies with varying NaH14CO3 concentration indicated a kcat near 1.0 s-1. Removal of the fourth substrate, oxygen, resulted in the loss of more than 99% of carboxylase activity. The sulfhydryl reagent N-ethylmaleimide inhibited carboxylase irreversibly, as did the anticoagulant warfarin

Stimulation of the vitamin K-dependent carboxylase from bovine liver.

Vitamin K-dependent carboxylase from bovine liver is stimulated not only by reducing agents and bivalent metal ions (especially Mn2+), but also by several organic solvents (dimethyl sulphoxide, ketones and acetonitrile). The organic solvents stimulated both the carboxylation of glutamic acid residues and the formation of vitamin K epoxide. This stimulation by organic solvents was independent of the physical state of the phospholipid; it was highest at low temperatures and could only be demonstrated with vitamin K1 and not with 3-DTT-MK-O (the thioether adduct of menadione and dithiothreitol) or t-butyl hydroperoxide, which normally can substitute for vitamin K. We suggest that organic solvents exert their effect by changing the mobility of the isoprenoid side chain of vitamin K1 within the carboxylase complex

Isolation and partial characterization of a vitamin K-dependent carboxylase from bovine aortae.

Vitamin K-dependent carboxylase activity has been demonstrated in the crude microsomal fraction of the intima of bovine aortae. The procedure for the isolation of vessel wall carboxylase is a slight modification of the general preparation procedure for tissue microsomes. The highest activity of the non-hepatic enzyme was observed at 25 degrees C and hardly any NADH-dependent vitamin K reductase could be demonstrated. The optimal reaction conditions for both vessel wall as well as liver carboxylase were similar: 0.1 M-NaCl/0.05 M-Tris/HCl, pH 7.4, containing 8 mM-dithiothreitol, 0.4% 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulphonic acid (CHAPS), 0.4 mM-vitamin K hydroquinone and 2 M-(NH4)2SO4. Warfarin inhibits the hepatic and non-hepatic carboxylase/reductase enzyme complex more or less to a similar degree. We have measured the apparent Km values for the following substrates: Phe-Leu-Glu-Glu-Leu ('FLEEL'), decarboxylated osteocalcin, decarboxylated fragment 13-29 from descarboxyprothrombin and decarboxylated sperm 4-carboxyglutamic acid-containing (Gla-)protein. The results obtained demonstrated that liver and vessel wall carboxylase may be regarded as isoenzymes with different substrate specificities. The newly discovered enzyme is the first vitamin K-dependent carboxylase which shows an absolute substrate specificity: FLEEL and decarboxylated osteocalcin were good substrates for vessel wall carboxylase, but decarboxylated fragment 13-29 and decarboxylated sperm Gla-protein were not carboxylated at all

Congenital deficiency of all vitamin K-dependent blood coagulation factors due to a defective vitamin K-dependent carboxylase in Devon Rex cats

Two Devon Rex cats from the same litter, which had no evidence of liver disease, malabsorption of vitamin K or chronic ingestion of coumarin derivatives, were found to have plasma deficiencies of factors II, VII, IX and X. Oral treatment with vitamin K1 resulted in the normalization of these coagulation factors. After taking liver biopsies it was demonstrated that the coagulation abnormality was accompanied by a defective γ-glutamyl-carboxylase, which had a decreased affinity for both vitamin K hydroquinone and propeptide. This observation prompted us to study in a well-defined in vitro system the possible allosteric interaction between the propeptide binding site and the vitamin K hydroquinone binding site on carboxylase. It was shown that by the binding of a propeptide-containing substrate to γ-glutamylcarboxylase the apparent K(M) for vitamin K hydroquinone is decreased about 20-fold. On the basis of these in vitro data the observed defect in the Devon Rex cats can be fully explained