Substrate (chemistry)

About: Substrate (chemistry) is a research topic. Over the lifetime, 35902 publications have been published within this topic receiving 740722 citations. The topic is also known as: enzyme substrate.

Substrate depletion in different types of muscle and in liver during prolonged running.

Abstract: BALDWIN, K. M., J. S. REITMAN, R. L. TERJUNG, W. W, WINDER, AND J. 0. HOLLOSZY. Substrate depktion in dz’fmnt types of muscle and in liver during prolonged running. Am. J. Physiol. 2 2 5(5) : 1045-l 050. 1973,KDepletion of glycogen and triglyceride stores in red, white, and intermediate types of skeletal muscle and of glycogen in liver was studied in rats subjected to prolonged exercise. Groups of rats were killed after 15, 60, and 120 min of running up an 8’ incline at a) 1 mph, b) I mph with I min at 1.5 mph every 9 min, and c) alternate 30-set intervals at 0.5 and 1,5 mph. White muscle underwent little or no change in glycogen and triglyceride concentrations in response to the three exercise tests. In red muscle and intermediate muscle, the decrease in glycogen concentration ranged from 42 to 727, after 2 hr; glycogen decreased most sharply during the first 15 min of all three exercise tests and then stabilized or decreased more slowly. Triglyceride concentration in red muscle decreased approximately 4Oaj’, after 2 hr of all three exercise tests. Little or no change in triglyceride concentration occurred in white and intermediate muscle. Liver glycogen decreased progressively during all three exercise tests and was depleted approximately 85y0 after 2 hr. These results suggest that in the rat performing prolonged moderate exercise, a) white muscle contracts infrequently and b) liver glycogen can be a more important source of energy than muscle glycogen.

Spectroscopic Studies of Substrate Interactions with Clavaminate Synthase 2, a Multifunctional α-KG-Dependent Non-Heme Iron Enzyme: Correlation with Mechanisms and Reactivities

Abstract: Using a single ferrous active site, clavaminate synthase 2 (CS2) activates O2 and catalyzes the hydroxylation of deoxyguanidinoproclavaminic acid (DGPC), the oxidative ring closure of proclavaminic acid (PC), and the desaturation of dihydroclavaminic acid (and a substrate analogue, deoxyproclavaminic acid (DPC)), each coupled to the oxidative decarboxylation of cosubstrate, α-ketoglutarate (α-KG). CS2 can also catalyze an uncoupled decarboxylation of α-KG both in the absence and in the presence of substrate, which results in enzyme deactivation. Resting CS2/FeII has a six-coordinate FeII site, and α-KG binds to the iron in a bidentate mode. The active site becomes five-coordinate only when both substrate and α-KG are bound, the latter still in a bidentate mode. Absorption, CD, MCD, and VTVH MCD studies of the interaction of CS2 with DGPC, PC, and DPC provide significant molecular level insight into the structure/function correlations of this multifunctional enzyme. There are varying amounts of six-coordin...

Metal oxide film formation method and apparatus

Abstract: In a metal oxide film formation method, a source gas mixture of organic compound gases containing at least three metals, and an oxidation gas are individually prepared. While the substrate is heated, the oxidation gas is supplied to a substrate set in a closed vessel at a predetermined pressure, and then the gas mixture is supplied. A metal oxide film is formed on the substrate. A metal oxide film formation apparatus is also disclosed.