Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.5.1.1 (asparaginase)
2,695 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Seven Mycobacterium strains were grown statically on salts-glycerol-asparagine (Sauton) or on salts-glucose-glutamate (Sym) media. At desired time of incubation, the bacteria were washed with water, disintegrated with powdered corundum and in resulting cell-free extracts L-asparaginase activity was determined by the Conway method. The majority of experiments were performed on M. phlei which exhibited considerable rise in L-asparaginase activity with increasing age of the culture. This change did not occur on Sym medium because of Zn2+, which proved to abolish the effect of the enzyme induction in vivo but did not inhibit the activity in vitro. Addition of rifampicin to Sauton culture media resulted in a low enzyme level. Exogenous asparagine and glycerol were not indispensable for the enzyme synthesis and could be replaced by glutamate and glucose, respectively.
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PMID:L-asparaginase activity of Mycobacterium phlei under various growth conditions. 24 89

Human glycoasparaginase (N4-(beta-N-acetyl-D-glucosaminyl)-L-asparaginase, EC 3.5.1.26) hydrolyzes a series of compounds that contain L-asparagine residue with free alpha-amino and alpha-carboxyl groups. Substrates include high mannose and complex type glycoasparagines as well as those that lack the di-N-acetylchitobiose moiety, L-aspartic acid beta-methyl ester and L-aspartic acid beta-hydroxamate. The enzyme is inactive toward L-asparagine and L-glutamine and glycoasparagines containing substituted alpha-amino and/or alpha-carboxyl groups. In the presence of the acyl acceptor hydroxylamine, glycoasparaginase catalyzes the synthesis of L-aspartic acid beta-hydroxamate from aspartyl-glucosamine, L-aspartic acid beta-methyl ester, and L-aspartic acid. 13C NMR studies using 18O-labeled L-aspartic acid demonstrate that glycoasparaginase catalyzes an oxygen exchange between water and the carboxyl group at C-4 of L-aspartic acid. These results indicate that glycoasparaginase reacts as an exo-hydrolase toward the L-asparagine moiety of the substrates and the free alpha-amino and alpha-carboxyl groups are required for the enzyme reaction. The results are consistent with an L-asparaginase-like reaction pathway which involves a beta-aspartyl enzyme intermediate. Since glycoasparaginase is active toward a series of structurally different glycoasparagines, we suggest the revised systematic name of N4-(beta-glycosyl)-L-asparaginase for the enzyme.
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PMID:Substrate specificity and reaction mechanism of human glycoasparaginase. The N-glycosidic linkage of various glycoasparagines is cleaved through a reaction mechanism similar to L-asparaginase. 155 92

Acylation of L-asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) with complete retention of catalytic activity was achieved. Several parameters of the acylation method, based on the binding of palmitoyl residues to epsilon-NH2 groups of protein, were optimized. The correlation between the acylation degree of L-asparaginase and the retention of catalytic activity was established. For a palmitoyl chloride/protein molar ratio ranging from 50 to 900, a degree of modification of 10 to 30% and a retention of catalytic activity of 98 to 60% respectively, was observed. Hydrophobicity of 30% acylated protein was correlated with turbidity in water and octanol and was compared with the native protein. Acylated protein incorporated into liposomes, showed an increase in catalytic activity in intact form as compared to the native enzyme. By the introduction of a sequential acylation cycle, an improvement of the degree of modification with a maximal value at 50% was obtained. Total retention of catalytic activity was achieved by acylation in the presence of 8 mM L-asparagine in a reactional medium.
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PMID:Acylation of L-asparaginase with total retention of enzymatic activity. 212 8

This study suggests the presence of an entero-portal recirculation of amino acids. Endogenous sources of amino acids are secreted at high concentration into the small intestine. Most of the amino acids are absorbed as the content passes down the small intestine. Plasma amino acid concentrations are on the average only 1-5% of the concentrations in the duodunum. This is true even in rats on 24 hours of water and sugar with no exogenous sources of amino acids. For example, the PLASMA:DUODENUM concentrations (mumole/litre) are: Asparagine 37:7164, Tyrosine 94:9579, and glutamine/histidine 409:9708. This entero-portal recirculation of amino acids means the potential of a method for specific depletion of body amino acids by oral ingestion of bioreactants like immobilized enzymes. Preliminary studies used artificial cells to immobilize asparaginase,glutaminase and tyrosinase by microencapsulation. Six hours after 1 oral administration, asparagine, glutamine and tyrosine in the ileum were lowered to 10% of the level of the control. Artificial cells containing no enzymes were used as the control.
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PMID:Plasma/intestinal concentration patterns suggestive of entero-portal recirculation of amino acids: effects of oral administration of asparaginase, glutaminase and tyrosinase immobilized by microencapsulation in artificial cells. 315 Sep 43

The decay of the indole triplet of single tryptophan-containing proteins and model compounds can be readily determined at room temperature in solution by monitoring the triplet absorption or emission following an exciting laser pulse. The dioxygen triplet quenching constants, can be measured for all these molecules and compared to the analogous singlet values determined by fluorescence methods. The dioxygen triplet quenching constant (tkq) ranged from a high of 5.1.10(9) M-1.s-1 for the exposed indole of corticotropin to a low of 0.1.10(9) M-1.s-1 for the buried indole of asparaginase. The ratio of these values with their respective dioxygen singlet quenching constants (skq), tkq/skq, ranged from 0.3 to 0.6 for aqueous exposed polypeptide indoles. For globular proteins the tkq/skq value is observed to be 0.2 +/- 0.1. This lower value for protein indoles is not attributable to 'bulk' environmental or hydrogen bonding effects, since the magnitude of tkq/skq (= 0.5 +/- 0.1) for model indoles was independent of solvent dielectric constant, polarity, and proticity. Temperature-dependence studies were done to test whether tkq could be used to characterize the nature of the protein matrix. The activation energy (Ea) for tkq was found to be 11 +/- 2 kcal/mol for most proteins. This Ea was independent of whether the indole side-chain was solvent exposed or buried in the non-aqueous protein interior. Large Ea values were also obtained for model indoles, naphthalene and nalidixic acid, dissolved in water, whereas the same compounds dissolved in 95% ethanol exhibited much smaller Ea values. These data, in combination with the observation that the tkq of model indoles is insensitive to changes in solvent viscosity, indicate that dioxygen quenching at the triplet level can not be easily used to characterize the dynamics of proteins.
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PMID:Determination of the dioxygen quenching constant for protein and model indole triplets. 319 Nov 39

L-asparaginase, covalently bound with water-soluble CM-cellulose, exhibited the elevated antileukemic activity in mice with inoculated lymphoid leukemia L5178y as compared with the native enzyme. The antileukemic activity of the immobilized enzyme was shown to depend on the content of the polymer bound with the enzyme; the polymer amount may be altered during the enzyme modification. The prolonged effect of immobilized L-asparaginase was observed in rabbit circulation.
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PMID:[High molecular weight L-asparaginase derivatives based on a water-soluble carboxymethyl cellulose: biological properties]. 342 Jul 97

The mechanism of the enzyme asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) from Escherichia coli was examined using 13C NMR spectroscopy. The pH-dependent oxygen exchange reactions between water and aspartic acid were followed by use of the 18O isotope-induced shift of the resonance positions of directly bonded 13C nuclei. Both L-1- and L-1,4-[13C]aspartic acid were used in experiments with previously 18O-labeled aspartic acid, or in experiments involving the use of 18O-labeled solvent water. Asparaginase catalyzes a relatively efficient exchange between the oxygens of water and those on one carboxyl group of aspartic acid. Exchange at C-4 occurs rapidly but, within experimental error, no exchange at C-1 could be detected. These and related experiments involving the position of 18O incorporation during hydrolysis of aspartic acid beta-methyl ester are all consistent with possible acyl-enzyme mechanisms involving C-4, but do not support a free aspartic acid anhydride mechanism.
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PMID:The 18O isotope effect in 13C nuclear magnetic resonance spectroscopy: mechanistic studies on asparaginase from Escherichia coli. 351 41

To understand how vertebrates utilize angiotensins during evolutionary development studies were undertaken to synthesize and/or characterize angiotensin-like peptides from nonmammalian species. These studies indicated the presence of a new L-asparaginase amidohydrolase type enzyme in eel plasma which deamidates L-asparagine residue at the amino terminus of the angiotensin peptides, thereby implying that l-asparaginyl decapeptide (rather than l-aspartyl decapeptide) is the natural form of angiotensin inherent in eel plasma. Pharmacological properties of the nonmammalian angiotensins compared with the synthetic analogs in one representative species of three distinct classes of vertebrates suggest that: in spite of variation in position 9 of the nonmammalian angiotensins I, the pressor activity of these peptides in rat and in dogfish shark is due to their conversion into the corresponding angiotensin II; in relatively more primitive stages of evolution, when vertebrates lived in salt water (e.g., dogfish shark) pressor action of exogenous angiotensin II appears to be due to the release of catecholamines (and not through direct vasoconstrictor effects, as in the mammalian species); and frog-skin angiotensin II has properties that may prove to be compatible with a role in the regulation of salt and water in amphibians.
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PMID:Synthesis and pharmacology of nonmammalian angiotensins and their evolutionary development. 384 91

L-Asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) from Erwinia carotovora undergoes extensive dissociation from active tetramer to inactive monomers when freeze-dried. The monomeric state is stabilized by reconstitution of the freeze-dried enzyme with buffers of high pH and high ionic strength. Some compounds, particularly sugars and sugar derivatives, prevent dissociation on freeze-drying, whereas others, such as urea and chaotropic ions, increase dissociation. The effects of additives are not related to water retention. The dissociation is completely reversible on reconstitution at neutral pH, but the alkali-stabilized monomer only partially reassociates when the pH is brought back to neutrality.
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PMID:The effect of freeze-drying on the quaternary structure of L-asparaginase from Erwinia carotovora. 665 94

Inoculation of bone marrow and spleen cells of C3H/Sumice strain mice demonstrated that on the ninth day of growth of Gardner lymphosarcoma these tissues were invaded with tumor cells. The weights of mice with advanced tumors increased. Yet the deterioration of health status of mice is characterized by decreased food and water consumption, as well as by lower concentrations of proteins in mouse sera and plasma. The albumin fraction shows a remarkable drop. These changes could not be detected in tumor free mice following LDH-virus infection. The treatment with L-asparaginase influenced the manifestations of tumor growth, but not the effectivity of LDH-virus contaminating the tumor as demonstrated by the increased activity of lactate-dehydrogenase in the mouse sera.
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PMID:Changes in hemopoiesis of mice of the C3H strain following transplantation of Gardner lymphosarcoma and infection with LDH-virus. III. Blood proteins. 689 6


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