Enzymes in signaling

Phospholipases of type Cfi function as effector enzymes in signal transmission by various G protein coupled receptors. The initiating external signals are diverse (see Fig. 5.16) and include hormones, neurohormones and sensory signals such as odorous agents and light (in nonvertebrates). 

Most of the signals conveyed by AC/cAMP are mediated through phosphorylation reactions catalyzed by the protein kinases. Figure 12.1 illustrates the involvement of adenylyl cyclase as the effector enzyme in signal transduction. 

A kinase is an enzyme that catalyzes the transfer of the terminal phosphate of a nucleotide to suitable substrates. Protein and lipidkinases play important roles in signaling. 

The phosphorylation and dephosphorylation of seryl, threonyl, and tyrosyl residues regulate the activity of certain enzymes of lipid and carbohydrate metabolism and the properties of proteins that participate in signal transduction cascades. 

One main line of future research could be in the inhibitory/activating effect on key enzymes involved in the pathogenesis of arteriosclerosis. In particular, enzymes regulating signal transduction involved in phosphorylation of proteins, such as PKC and tyrosine protein kinase, seems to be somehow modulated by different polyphenols and may represent a possible target for polyphenol activity. 

The PelX protein contains 749 amino-acids including an amino-terminal signal sequence of 26 amino-adds. The celliilar localisation of the enzyme has not been rigorously determined. In E. chrysanthemi CUCPB1237, the exo-pectate lyase activity was cell-bound (14). The presence of this type of enzyme in the bacterial periplasm appeared normal since it acts better on oligomers produced by endo-pectate lyases than on long polymeric substrates (15). 

This gene is broadly distributed in skeletal muscle, heart, uterus, and in a variety of non-muscle cells. The mRNA levels are particularly high in intestine, lung and spleen, whereas they are very low in liver, testes, kidney and pancreas. In the muscle tissue SERCA3 may be confined primarily to non-muscle cells (vascular smooth muscle, endothelial cells, etc.). The C-terminus of SERCA3 is Asp-Gly-Lys Lys-Asp-Leu-Lys (Table I) it may serve as a sorting signal for retention of the enzyme in the endoplasmic reticulum [57]. 

The addition of ethanolamine to the enzyme-coenzyme complex resulted in greater than 90% loss in signal intensity. When the substrate supply was exhausted, the original ESR spectrum reappeared slowly but did not regain its full intensity after 30 minutes. Under the experimental... 

Fig. 4. Anaerobic titration of xanthine oxidase with xanthine at pH 8.2 with a reaction time of 2 min. at about 20°. The integrated intensity of the Rapid molybdenum EPR signals (in arbitrary units) is plotted against the number of moles of xanthine added per mole of active enzyme. Activity/A4jo for the enzyme samples used was 112 corresponding to an active enzyme content of 57%. Thus the molar ratios of xanthine/total xanthine oxidase have been multiplied by 1.76 to refer to the active form only. Some of the EPR spectra (recorded at about — 130° and 9.3 GHz) are reproduced to show the changes in signal type as the amount of xanthine is increased. (Data re-calculated from ref. 88, with intensities corrected for variations in tube diameter and enzyme concentration calculated in terms of active enzyme.)...

NO is a gaseous neurotransmitter implicated in signaling in the central and peripheral nervous system as well as in the immune system and the vasculature. NO is formed from L-arginine by nitric oxide synthase (NOS). There are three isoforms of NOS. All isoforms require NADPH as a cofactor, use L-arginine as a substrate, and are inhibited by Nw-nitro-L-arginine methyl ester (L-NAME). The three isoforms are separate gene products. One isoform of NOS is a cytosolic, calcium/calmodulin-independent, inducible enzyme (iNOS). It is found in macrophages, neutrophils, vascular smooth muscle, and endothelia. The iNOS... 

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