Calcium enzymes activated

Nonrepetitive but well-defined structures of this type form many important features of enzyme active sites. In some cases, a particular arrangement of coil structure providing a specific type of functional site recurs in several functionally related proteins. The peptide loop that binds iron-sulfur clusters in both ferredoxin and high potential iron protein is one example. Another is the central loop portion of the E—F hand structure that binds a calcium ion in several calcium-binding proteins, including calmodulin, carp parvalbumin, troponin C, and the intestinal calcium-binding protein. This loop, shown in Figure 6.26, connects two short a-helices. The calcium ion nestles into the pocket formed by this structure. 

Enzyme active sites, 136,148, 225. See also Protein active sites in carbonic anhydrase, 197-199 in chymotrypsin, 173 in lysozyme, 153, 157 nonpolar (hypothetical site), 211-214 SNase, 189-190,190 steric forces in, 155-158, 209-211, 225 in subtilisin, 173 viewed as super solvents, 227 Enzyme cofactors calcium ... 

Ionized calcium is an important regulator of a variety of cellular processes, including muscle contraction, stimulus-secretion coupling, the blood clotting cascade, enzyme activity, and membrane excitability. It is also an intracellular messenger of hormone action. 

The enzyme had a requirement for calcium. The addition of EDTA to the reaction mixtures, resulted in complete loss of activity, whereas the addition of CaCl2 increased the activity (figure 8). Presumably, sufficient contaminating calcium ions were present in the dialyzed enzyme and substrate mixture to permit the limited activity of the controls, but apparently these were removed by chelation with EDTA. The optimum concentration was in the range of 5 to 15 M, and higher concentration resulted in a decrease in activity. Phoma medicaginis var. pinodella synthesizes a pectin lyase that lacked an absolute requirement for calcium ions but maximum enzyme activity required the presence of 1 mM Ca [25]. The lyase from Fusarium solani f sp. phaseoli, that is active on pectin and pectic acid, is calcium-dependent [30]. Most of the pectate lyases characterized are calcium-dependent the pectate lyase from Rhizoctonia solani [34] and the endopectate lyase fi om Fusarium solani f sp. pisi [31]. 

Kessler, M., Hajek, K., Simon, W. Four-Barreled Microelectrode for the Measurement of Potassium, Sodium, and Calcium-Ion Activity, in Ion and Enzyme Electrodes in Biology and Medicine (Kessler, M., Clark, Jr, L. C., Lubbers, D, W., Silver, I. A., Simon, W., eds.) Munich Urban and Schwarzenberg, 1976, p. 136... 

Lead also has been shown to substitute for calcium in the activation of calmodulin, but this requires higher levels of lead than does the activation of protein kinase C. Nevertheless, the affinity of lead for calmodulin is higher than that of calcium. Once activated, calmodulin regulates the activity of certain enzymes and transporters. For example, it activates c-AMP phosphodiesterase to hydrolyze and terminate the action of cAMP, another second messenger (Bressler and Goldstein 1991 Goldstein 1993 Goering 1993). 

In the presence of sucrose alone as the single substrate, initial reaction rates follow Michaelis-Menten kinetics up to 200 mM sucrose concentration, but the enzyme is inhibited by higher concentrations of substrate.30 The inhibitor constant for sucrose is 730 mM. This inhibition can be overcome by the addition of acceptors.31,32 The enzyme activity is significantly enhanced, and stabilized, by the presence of dextran, and by calcium ions. 

A few enzymes, such as the previously mentioned CNP, are believed to be fairly specific for myelin/oligodendro-cytes. There is much more in the CNS than in peripheral nerve, suggesting some function more specialized to the CNS. In addition, a unique pH 7.2 cholesterol ester hydrolase is also enriched in myelin. On the other hand, there are many enzymes that are not myelin-specific but appear to be intrinsic to myelin and not contaminants. These include cAMP-stimulated kinase, calcium/calmodulin-dependent kinase, protein kinase C, a neutral protease activity and phosphoprotein phosphatases. The protein kinase C and phosphatase activities are presumed to be responsible for the rapid turnover of MBP phosphate groups, and the PLP acylation enzyme activity is also intrinsic to myelin. 

The use of alkali and alkaline earth group metal ions, especially those of sodium, potassium, magnesium, and calcium, for maintenance of electrolyte balance and for signaling and promotion of enzyme activity and protein function are not discussed in this text. Many of these ions, used for signaling purposes in the exciting area of neuroscience, are of great interest. In ribozymes, RNAs with catalytic activity, solvated magnesium ions stabilize complex secondary and tertiary molecular structure. Telomeres, sequences of DNA at the ends of chromosomes that are implicated in cell death or immortalization, require potassium ions for structural stabilization. 

Mehorta and coworkers (1989) observed that isolated fractions of brain and heart cells from rats orally administered 0.5-10 mg endrin/kg showed significant inhibition of Ca+2 pump activity and decreased levels of calmodulin, indicating disruption of membrane Ca+2 transport mechanisms exogenous addition of calmodulin restored Ca+2-ATPase activity. In vitro exposure of rat brain synaptosomes and heart sarcoplasmic reticuli decreased total and calmodulin-stimulated calcium ATPase activity with greater inhibition in brain preparations (Mehorta et al. 1989). However, endrin showed no inhibitory effects on the calmodulin-sensitive calcium ATPase activity when incubated with human erythrocyte membranes (Janik and Wolf 1992). In vitro exposure of rat brain synaptosomes to endrin had no effect on the activities of adenylate cyclase or 3, 5 -cyclic phosphodiesterase, two enzymes associated with synaptic cyclic AMP metabolism (Kodavanti et al. 1988). 

Living cells visualization of membranes, lipids, proteins, DNA, RNA, surface antigens, surface glycoconjugates membrane dynamics membrane permeability membrane potential intracellular pH cytoplasmic calcium, sodium, chloride, proton concentration redox state enzyme activities cell-cell and cell-virus interactions membrane fusion endocytosis viability, cell cycle cytotoxic activity... 

M. Caffrey and G. W. Feigenson, Fluorescence quenching in model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics, Biochemistry 20, 1949-1961 (1981). 

YPClp and YDClp have different substrate specificity such that YPClp prefers phytoceramide (phytoCer) over dihydroceramide (dhCer) whereas YDClp prefers dhCer over phytoCer, however, neither enzyme uses the most common mammalian type ceramide having a 4-5 trans double bond on the sphingoid base as substrate. Both enzymes have a narrow pH optimum of 9.4-10, hence, are classified as alkaline ceramidases. Calcium ions activate but are not absolutely required for the activities of both enzymes. and inhibit the activities of both enzymes. None of the sphingoid bases inhibit the activities of YPC Ip and YDClp. 

Some of the main types of cellular regulation associated with rhythmic behavior are listed in Table III. Regulation of ion channels gives rise to the periodic variation of the membrane potential in nerve and cardiac cells [27, 28 for a recent review of neural rhythms see, for example, Ref. 29]. Regulation of enzyme activity is associated with metabolic oscillations, such as those that occur in glycolysis in yeast and muscle cells. Calcium oscillations originate... 

Many proteins, including many enzymes, contain hghtly bound metal ions. These may be inhmately involved in enzyme catalysis or may serve a purely structural role. The most common tightly bound metal ions found in metalloproteins include copper (Cu+ and Cu +), zinc (Zn +), iron (Fe + and Fe +), and manganese (Mn +). Other proteins may contain weakly bound metal ions that generally serve as modulators of enzyme activity. These include sodium (Na+), potassium (K+), calcium (Ca +), and magnesium (Mg +). There are also exotic cases for which enzymes may depend on nickel, selenium, molybdenum, or silicon for activity. These account for the very small requirements for these metals in the human diet. 

Removal of calcium from HRP C has a significant effect not only on enzyme activity and thermal stability, but also on the environment of the heme group. The calcium-depleted enzyme has optical, EPR, and H NMR spectra that are different from those of the native enzyme (211). Temperature dependence studies indicate that the heme iron exists as a thermal admixture of high- and low-spin states. Kinetic measurements at pH 7 show that ki, the rate constant for compound I formation, is only reduced marginally from 1.6 0.1 x 10 to 1.4 x lO M s , whereas k, the rate constant for compound II reduction, is reduced from 8.1 1.6 x 10 to 3.6 x lO M s (reducing substrate p-aminobenzoic acid), 44% of its initial value (211). There can be little doubt that this is the main reason for the loss of enzyme activity on calcium removal. 

This enzyme [EC 3.4.22.8], also referred to as clostridio-peptidase B, is an endopeptidase belonging to the peptidase family Cll that has been isolated from the bacterium Clostridium histolyticum. It catalyzes the hydrolysis of peptide bonds with a preference for the Arg—Xaa bond (including the Arg—Pro bond), but not the Lys— Xaa peptide bond. This calcium ion-activated enzyme is inactivated by EDTA. 

This calcium-ion-activated enzyme [EC 3.4.21.61] catalyzes the hydrolysis of peptide bonds at LysArg—Xaa and ArgArg—Xaa to process yeast a-factor pheromone and killer toxin precursors. 

P3. Posner, I., and Morales, A., Mechanisms of enzyme and substrate activation by lipoprotein lipase cofactors. I. A specific requirement of physiological concentrations of calcium for enzyme activity. J. Biol. Chem. 247, 2255-2265 (1972). 

Antihypertensive drugs can be divided into eight classes based on the mechanism of action diuretics, )3-adrenoblockers, centrally acting sympatholytics, peripherally acting sympatholytics, calcium channel blockers, myotropic hypotensive drugs, angiotensin-con-verting enzyme inhibitors, and calcium channel activators. 

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