Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Bacillus subtilis Marburg TI (thy,trpC2) has at least four endonuclease activities as assayed by measuring the conversion of single-stranded circular f1 DNA to the linear form by agarose gel electrophoresis. One of them, which is specific for single-stranded DNA (named endonuclease MII), was purified about 320 times by two chromatographic steps and gel filtration, thereby eliminating exonuclease and phosphomonoesterase activities. This activity requires divalent cations but does not require ATP. The molecular weight estimated by gel filtration was about 57,000 daltons. The cleavage products have 5'-phosphoryl termini. At low concentrations, double-stranded DNA is not split to any detectable extent. At high concentrations, however, double-stranded superhelical DNA is attacked to yield open-circular and linear DNA's. The activity of the enzyme towards single-stranded circular DNA relative to that towards double-stranded linear DNA was calculated to be approximately 5,000:1 by comparing the initial rates of introducing single-strand breaks into the DNA's.
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PMID:Purification and characterization of an endonuclease specific for single-stranded DNA from Bacillus subtilis Marburg. 4 35

Intact Angiostrongylus cantonensis is able to hydrolyse glucose-phosphate esters, mononucleotides and rho-nitrophenyl phosphate as well as beta-glycerophosphate in vitro. Reciprocal inhibition studies suggest that the hydrolysis of such substrates is due to a non-specific phosphomonoesterase. Molybdate ions, which exert no effect on either the uptake of glucose or the production of lactate, inhibit the hydrolysis of glucose-1-phosphate in the external medium and simultaneously lower the production of lactate by the intact worms in vitro.
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PMID:Acid phosphatase activity demonstrated by intact Angiostrongylus cantonesis with special reference to its function. 4 61

The non-specific phosphomonoesterase (enzyme I) extracted from the larva of the codworm (Phocanema decipiens) is different from the enzyme (enzyme II) from the muscle of its host, the codfish (Gadus morhua). The pH optima were 4.0 and 4.5, and the KM values for p-nitrophenyl phosphate hydrolysis were 1.8 mM and 6.5 mM for enzymes I and II respectively. The specific specific activity in units (0.01 mumol/min) per mg protein was 4.80 +/- 0.85 and 0.54 +/- 0.07 for enzymes I and II respectively. The specific activity from uninfected muscles was only 0.39 (SD +/- 0.017) units per mg of protein. Both enzymes were inhibited by NaF, HgCl2, and cysteine but were stimulated by 2-mercaptoethanol. EDTA and iodoacetamide had no effect on enzyme I but enzyme II was activated by EDTA and inhibited by iodoacetamide. Cadmium ions inhibited both the enzymes but a conspicuous feature with enzyme II was in the increase in percentage inhibition by lowering the concentration of CD2+.
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PMID:A comparison of the non-specific acid phosphomonoesterase activity in the larva of Phocanema decipiens (Nematoda) with that of the muscle of its host the codfish (Gadus morhua). 4 95

The total membrane-bound ATP hydrolytic activity in human epidermis is due to the activities of at least three differently located enzymes, namely Mg++-activated ATPase, phosphomonoesterase and adenyl cyclase. Cytochemical studies on psoriatic epidermis with various inhibitory and stimulatory substances showed reduced activities of ATPase and phosphomonoesterase, and a lack of sensitivity of adenyl cyclase to specific stimulators such as isoproterenol and glucagon. Since no differences of basal adenyl cyclase activity were observed between normal and psoriatic human skin without stimulation, it seems likely that in psoriasis a latent defect of adenyl cyclase may exist, resulting in a deficient response of this enzyme to regulatory agents. In conclusion, the present study reveals that not a single enzyme but the entire membrane-bound nucleotide metabolism is altered in psoriatic keratinocytes, causing a disturbance of the membrane-bound energy utilization, similar to findings in proliferating tumour cells.
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PMID:Ultrastructural localization and differentiation of membrane-bound ATP utilizing enzymes including adenyl cyclase in normal and psoriatic epidermis. 17 85

In Anacystis nidulans, upon infection with cyanophage AS-1, after a lag period of 1 h the level of deoxyribonuclease (DNase) activity increaded rapidly up to 15- to 20-fold in 4 to 5 h in the light. In contrast, the ribonuclease and phosphomonoesterase activities increased significantly only 4 to 5 h after infection, i.e. as late as 1 h prior to lysis. In complete darkness, the nuclease levels remained unaltered. However, when the infected cells were exposed to light for 1 or 2 h after infection, the DNase level increased essentially to the same extent in the dark as in continuous light, although the complete replication cycle of the virus was impaired in the dark and cells lysed only in the continuously illuminated cultures. Inhibition of photosystem II with 3-(3,4-dichlorophenyl)-1-dimethylurea during the early illumination period strongly decreased the subsequent, infection-dependent increase in DNase activity in the dark. The virus-induced increase in DNase activity was also inhibited by chloramphenicol. The data suggest that, in spite of the obligate photoautotrophic nature of A. nidulans, dark metabolism is able to support fully the formation of some specific proteins if the triggering of their synthesis takes place in light.
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PMID:Formation in the dark, of virus-induced deoxyribonuclease activity in Anacystis nidulans, an obligate photoautotroph. 17

The nucleotide sequences at the 5' termini of rabbit alpha and beta globin mRNAs have been determined. Periodate oxidation of globin mRNA followed by reduction with 3H-sodium borohydride and subsequent analysis of the 3H-labeled mRNA reveals the presence of the "cap" structure m7G5'ppp- blocking the 5' terminus. After periodate oxidation, beta elimination, and phosphomonoesterase treatment to remove the m7G5'ppp- "cap," the 5' end of globin mRNA was labeled with 32P using gamma-32P-ATP and T4 polynucleotide kinase. The 5'-32P-labeled alpha and beta globin mRNAs were then resolved from each other by polyacrylamide gel electrophoresis under denaturing conditions and sequenced separately. The 5' terminal nucleotide sequences determined are: alpha--m7G5'ppp5m6AmC(m)ACUUCUGG- BETA--M7G5'ppp5m6AmC(m) ACUUGCUUUUGACACAA Besides the m7G "cap" structure, the two sequences are identical for the first six nucleotides and then diverge. No initiator codon is present within the first ten nucleotides from the 5' end of the alpha globin mRNA, and the first nineteen nucleotides from the 5' end of beta globin mRNA.
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PMID:Nucleotide sequences at the 5'termini of rabbit alpha and beta globin mRNA. 18 43

Haemoglobin-free human erythrocyte ghosts that were prepared in the presence of EDTA and were then exposed to Ca2+ showed a substantial loss of phosphatidylinositol phosphate and phosphatidylinositol diphosphate, measured either chemically or by loss of 32P from the lipids of prelabelled membranes. At the same time there was, as reported previously (Allan, D. and Michell, R.H., (1976) Biochim. Biophys. Acta 455, 824--830), and approximately equivalent rise in the diacylglycerol content of the membranes. Analysis of the 32P-labelled water-soluble material released during this process showed that the major products were inositol diphosphate and inositol triphosphate. No change was seen in the phosphatidylinositol or phosphatidate content of the membranes, and there was no Ca2+-activated loss of 32P from the phosphatidate of prelabelled membranes: this suggests that Ca2+ did not activate phosphoinositide phosphomonoesterases or phosphatidate phosphomonoesterase in human erythrocyte membranes. It is concluded that human erythrocyte membranes contain at their cytoplasmic surface a Ca2+-activated phosphodiesterase that is active against both phosphatidylinositol phosphate and phosphatidylinositol diphosphate. Rabbit erythrocytes also contained this enzyme, but in these cells there was also evidence for the presence of a Ca2+-activated phosphatidate phosphomonoesterase.
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PMID:A calcium-activated polyphosphoinositide phosphodiesterase in the plasma membrane of human and rabbit erythrocytes. 20 46

The effect of certain metabolites of Penicillium brevi-compactum on the biosynthesis of exocellular ribonucleases and phosphomonoesterase was studied. Their synthesis was found to be inhibited by RNA and AMP, as well as by high concentrations of these enzymes in the medium. The mechanism which regulates the biosynthesis of exocellular phosphohydrolases by both phosphate and the enzymes is discussed.
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PMID:[Regulation of the biosynthesis of extracellular phosphohydrolases in Penicillium brevicompactum]. 21 70

The rabbit iris smooth muscle has been shown to contain triphosphoinositide phosphomonoesterase (phosphatidyl-myo-inositol-4,5-bisphosphate phosphohydrolase, EC 3.1.3.36) and phosphodiesterase (triphosphoinositide inositoltrisphosphohydrolase, EC 3.1.4.11) activities. Under our experimental conditions about 77% of the phosphomonoesterase and 61% of the phosphodiesterase activities were localized in the particulate fraction. The kinetic properties of the enzymes in the microsomal fraction were examined. The enzyme preparation was specific to polyphosphoinositides; it did not attack phosphatidylinositol under the present assay condition. The effects of Ca2+ and Mg2+ were also studied. Although the microsomal enzymes did not require added divalent cations for their activities, both the phosphomonoesterase and phosphodiesterase were appreciably inhibited by 1 mM EDTA. Phosphodiesterase and phosphomonoesterase were stimulated by Ca2+ and Mg2+, respectively. The demonstration of triphosphoinositide phosphodiesterase in the iris muscle, coupled with the findings that this enzyme is activated by Ca2+ and is not influenced by acetylcholine add further support to our previous conclusion (J. Pharmacol. Exp. Ther. (1978) 204, 655--668; J. Neurochem. (1978) 30, 517--525) that an increased Ca2+ influx, following the interaction between the neurotransmitter and its receptor, could act to stimulate the phosphodiesterase, thus leading to increased triphosphoinositide breakdown and increased phosphatidic acid via increased diacylglycerol.
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PMID:Studies on the properties of triphosphoinositide phosphomonoesterase and phosphodiesterase of rabbit iris smooth muscle. 21 33

Purified phosphodiesterase-phosphomonoesterase was found to be composed of four isozymes with different isoelectric points. These isozymes, phosphodiesterase-phosphomonoesterases 1-4, were separated from one another by repeated isoelectric focusing. Very little difference in amino acid composition, enzymic properties or circular dichroism spectra was detected among the isozymes. Far-ultraviolet circular dichroism spectra showed that the enzyme contained about 10% alpha-helix and 40% beta-structure. Phosphodiesterase-phosphomonesterase is a glycoprotein, because it was adsorbed on concanavalin A-Sepharose 4B and gave a band of carbohydrate coincident with that of protein or enzymic activity on polyacrylamide disc gel electrophoresis. Carbohydrate analyses revealed that the enzyme contained 37 micron of N-acetylglucosamine and 358 micron of mannose per mg of protein. The carbohydrate contents of the four isozymes were almost the same.
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PMID:Phosphodiesterase-phosphomonesterases from Fusarium moniliforme. Separation and properties of four isozymes. 21 23


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