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:3.5.4.6 (AMP deaminase)
690 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

AMP deaminase (AMP aminohydrolase, EC 3.5.4.6) was found in extract of baker's yeast (Saccharomyces cerevisiae), and was purified to electrophoretic homogeneity using phosphocellulose adsorption chromatography and affinity elution by ATP. The enzyme shows cooperative binding of AMP (Hill coefficient, nH, 1.7) with an s0.5 value of 2.6 mM in the absence or presence of alkali metals. ATP acts as a positive effector, lowering nH to 1.0 and s0.5 to 0.02 mM. P1 inhibits the enzyme in an allosteric manner: s0.5 and nH values increase with increase in Pi concentration. In the physiological range of adenylate energy charge in yeast cells (0.5 to 0.9), the AMP deaminase activity increases sharply with decreasing energy charge, and the decrease in the size of adenylate pool causes a marked decrease in the rate of the deaminase reaction. AMP deaminase may act as a part of the system that protects against wide excursions of energy charge and adenylate pool size in yeast cells. These suggestions, based on the properties of the enzyme observed in vitro, are consistent with the results of experiments on baker's yeast in vivo reported by other workers.
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PMID:AMP deaminase from baker's yeast. Purification and some regulatory properties. 3 10

1. AMP-deaminase (EC 3.5.4.6) from skeletal muscle of frog and pikeperch was purified to homogeneity and compared with the homogeneous enzymes purified from rat, rabbit and hen skeletal muscle. 2. Their molecular weight was close to 280,000, every enzyme consisted of four identical subunits of molecular weight about 70,000. 3. All enzymes were found to contain about two atoms of zinc per molecule. 4. Minor differences of u.v.-absorption spectra between amphibian and fish muscle enzyme as compared with mammalian and bird muscle enzyme were found.
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PMID:Comparative studies on muscle AMP-deaminase--I. Purification, molecular weight, subunit structure and metal content of the enzymes from rat, rabbit, hen, frog and pikeperch. 4 53

Concentrations of key metabolites were determined in carp white muscle before exercise and after maximal activity. It was found that the concentration of ATP decreases by about 65%, ADP decreases slightly, and AMP remains unchanged. Consequently, the level of the free adenylate pool decreases. Simultaneously there is an increase in the concentration of IMP and NH4+. The increase in IMP level and the decrease in adenylate pool are essentially in 1:1 stoichiometry, a result showing that the adenylate pool is decreased by the reaction catalyzed by 5'-AMP deaminase (EC 3.5.4.6.). During exercise there is an increase in levels of glucose-6-phosphate, fructose 6-phosphate, and fructose 1,6-diphosphate that, along with the decrease in ATP levels, can account for the increase in glycolytic flux by activation of phosphofructokinase and pyruvate kinase.
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PMID:Control of energy metabolism in fish white muscle. 13 93

Purified rat muscle AMP deaminase (AMP aminohydrolase, EC 3.5.4.6) binds tightly to rat myosin. The binding is abolished in the presence of low concentrations of various ligands. Pyrophosphate and GTP at concentrations as low as 0.1 micrometer were effective in abolishing the interaction between two proteins. Other nucleoside triphosphates were less effective than GTP and the concentrations required for 50% inhibition were approximately 0.3 to 0.7 micrometer. ADP and AMP are effective in inhibiting the interaction between two proteins, but they are less effective than the nucleoside triphosphates; 50% inhibition occurred at 34 micrometer with ADP and at 1 mM with AMP. Creatine phosphate and inorganic phosphate showed 50% inhibition at 5 to 6 mM. All of the compounds, which affected AMP deaminase activity, were effective in abolishing the interaction of the enzyme with myosin; however, the interaction-abolishing effects of the compounds are not parallel with their inhibitory effects on the deaminase activity. Although there exist three parental isozymes of AMP deaminase in the rat, all three enzymes interacted with myosin.
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PMID:Effects of various ligands on interaction of AMP deaminase with myosin. 20 24

The problems of whether the kinetic and regulatory properties of AMP deaminase were modified by formation of a deaminase-myosin complex were investigated with an enzyme preparation from rat skeletal muscle. Results showed that AMP deaminase was activated by binding to myosin. Myosin-bound AMP deaminase showed a sigmoidal activity curve with respect to AMP concentration in the absence of ATP and ADP, but a hyperbolic curve in their presence. Addition of ATP and ADP doubled the V value, but did not affect the Km value. Myosin-bound AMP deaminase also gave a sigmoidal curve in the presence of alkali metal ions, whereas free AMP deaminase gave a hyperbolic curve. GTP abolished the activating effects of both myosin and ATP.
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PMID:Interaction of rat muscle AMP deaminase with myosin. II. Modification of the kinetic and regulatory properties of rat muscle AMP deaminase by myosin. 42 Aug 60

Deamination of AMP in skeletal muscle sarcoplasmic reticulum followed by an increase in pH from 6,5 up to 8,0 leads in a liberation of part of Ca2+ from the SR vesicles. This effect is enhanced by K+, which activate the deamination, and is suppressed by Mg2+, which inhibit the reaction. The activating effect of AMP on Ca2+ efflux from the vesicles markedly decreases after AMP deaminase dissociation from the vesicles and is restored after reconstitution of their deaminase activity. Substitution of IMP for AMP causes a decrease of Ca2+ efflux from the vesicles. The data obtained are in good agreement with the assumption that the ammonium formation from AMP can favour the release of Ca2+ from some vesicles of SR.
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PMID:[Efflux of Ca2+ from fragmented sarcoplasmic reticulum during AMP deamination]. 50 58

Kinetic studies with adenylate deaminase have been performed by stopped flow methods at 20 degrees C in 0.01 M imidazole/HCl, pH 6.5. The data were analyzed using either the whole time course of the reaction or the initial portion of the full time course. At low KCl concentrations, activation by the product IMP complicates any interpretation. In the presence of 0.15 M KCl, the results are interpreted in terms of three types of purine nucleotide binding sites: an active site, an inhibitory site which appears to be relatively specific for nucleoside triphosphates, and an activating site which shows relatively little specificity for nucleoside phosphates. Nucleotide binding to the activating site weakens binding to the inhibitory site. Sigmoidal kinetic data observed as a function of AMP in the presence of the inhibitor GTP are interpreted in terms of AMP binding to the activating site and weakening GTP binding. A fragment of myosin, subfragement-2, which has previously been shown to form a tight complex with adenylate deaminase (Ashby, B., and Frieden, C. (1977) J. Biol. Chem. 252, 1869--1875) activates the deaminase reaction only slightly. Complex formation, however, makes the reaction less susceptible to inhibition by GTP, although high levels of this nucleotide will disrupt the complex. In the presence of GTP or GTP plus subfragment-2, hysteretic effects are observed.
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PMID:Adenylate deaminase. Kinetic and binding studies on the rabbit muscle enzyme. 72 7

The regulatory properties of adenylate deaminase (EC 3.5.4.6) from Ehrlich ascites tumor cells suggest that the reaction catalyzed by this enzyme serves to protect the cell against sharp decreases in the adenylate energy charge by removing adenosine 5'-monophosphate generated when the rate of utilization of adenosine triphosphate is suddenly increased. The enzyme is effectively inhibited under normal physiological conditions of high energy charge (0.9) and 4 to 5 mM adenine nucleotide pool size. The reaction is sharply activated by a decrease in the energy charge in the physiological range (0.9 to 0.6). At low energy charge (0.6), decrease in the size of the pool causes a marked and nonlinear decrease in the rate of the deaminase reaction. This effect presumably serves to prevent excessive depletion of the adenine nucleotide pool. Calculations based on the kinetic data obtained in this study show that the AMP deaminase reaction can account for the well-established alteration of adenine nucleotide metabolism that is observed following addition of glucose or 2-deoxyglucose to intact ascites cells.
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PMID:Role of the adenylate deaminase reaction in regulation of adenine nucleotide metabolism in Ehrlich ascites tumor cells. 94 36

1. AMP-deaminase (AMP-aminohydrolase, EC 3.5.4.6) from rabbit skeletal muscle showed sigmoid-shaped plots of velocity versus substrate concentration at four temperatures tested between 15 degrees and 35 degrees C. In the presence of 20 mM-KCl, the plot was sigmoid only at 30 degrees C and became hyperbolic at the other temperatures tested. In the presence of 150 mM-KCl the plots were hyperbolic at all the temperatures applied. 2. The Km value depended on temperature and concentration of KCl, whereas Vmax was the same for the 20 mM- and 150 mM-KCl-activated enzyme. 3. The value of enthalpy of the enzyme-substrate complex formation was the same for both the 20 mM- and 150-mM-KCl-activated enzyme at lower temperature range (less than 38 degrees C), whereas at higher temperatures (greater than 38 degrees C) this value was much more negative in the presence of 20 mM-KCl than of 150 mM-KCl.
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PMID:Potassium-dependent thermal sensibility of AMP-deaminase from rabbit skeletal muscle. 97 34

Thick filaments in vertebrate striated muscles are composed of myosin heavy chain (MHC) and myosin light chains (MLCs) plus at least eight other proteins: C-protein, 86kD protein (birds) or H-protein (mammals), M-protein, myomesin, titin, MM-creatine kinase, skelemin, and AMP-deaminase. Except for CPK and AMP deaminase, none have well defined functions. Analysis of cDNA clones encoding chicken C-protein and 86kD protein has revealed a high degree of shared amino acid identity, particularly in the C-terminal 40kD. To identify functionally significant regions, the human counterpart of each protein was cloned, sequenced and analysed. Two human C-protein cDNAs were isolated with significant homology to chicken fast C-protein. Clone H75, with 69% identity to chicken fast C-protein, shows the same pattern of hybridization as the chicken fast C-protein in chicken muscles. The other clone, H8 with 60% identity, shows a pattern of hybridization in chicken muscles which is consistent with the expression of chicken slow C-protein. The human 86kD protein shares 66% DNA sequence identity with the chicken 86kD protein. Assuming that essential sequences would be conserved during evolution, we compared the chicken and human proteins using PALIGN. Chicken and human fast C-proteins possess 66% peptide identity over their deduced length plus 10% conservative substitutions. Human slow C-protein and chicken fast C-protein share 44% peptide sequence identity, plus 16% conservative substitutions. Chicken and human 86kD proteins are also very similar: 54% peptide identity plus 20% conservative substitutions. This high degree of sequence identity between chicken and human C- and 86kD proteins suggests selective pressure on the primary sequence. Recent primary sequence analyses of projectin and mini-titins from Drosophila, twitchin from C. elegans, C-protein, smMLCK, 86kD protein, and M-protein from the chicken, titin from the rabbit, and skelemin from the mouse reveals that all these proteins possess multiple internal repeats of approximately 100 amino acids. These repeating domains are of two types: one is homologous to the internal repeats which define the C-2 subset of the immunoglobulin superfamily, the other is related to the fibronectin type III repeat. Both human C-proteins possess comparable internal repeats and preliminary evidence suggests the presence of the same repeats in human 86kD. This duality of repeat structure is found in many extracellular proteins and is typified by the N-CAMs.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:cDNA cloning and sequence comparisons of human and chicken muscle C-protein and 86kD protein. 134 Oct 33


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