Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026918 (Mycobacterium)
 52,428 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Binding studies of various nucleotides to the purified coupling factor-latent ATPase from Mycobacterium phlei have been carried out using gel filtration, equilibrium dialysis, and ultrafiltration methods. The purified latent ATPase binds 3 mol of ADP per mol of the enzyme with an apparent dissociation constant of 68 muM. Binding of nucleotides occurred in the decreasing order: ADP, epsilon-ATP, epsilon-ADP, UDP, adenyl-5'-yl imidodiphosphate (AMP-P(NH)P), IDP, and adenosine 5'-(alpha,beta-methylene)diphosphate (AdoP(CH2)P). AMP-P(NH)P inhibits both soluble (Ki = 77 muM) and membrane-bound latent ATPase activity. However, AMP-P(NH)P does not affect oxidative phosphorylation in membrane vesicles of M. phlei. AMP-P(NH)P exhibits one binding site per molecule of the enzyme with a dissociation constant of 71 muM. After trypsin treatment of the enzyme, the binding of ADP decreases 35%, while AMP-P(NH)P binding remains unchanged. Moreover, AMP-P(NH)P binding was not displaced by ADP. Studies with sulfhydryl agents showed that, in contrast to AMP-P(NH)P, binding of at least 1 mol of ADP requires the participation of sulfhydryl groups. The results indicate that AMP-P(NH)P and ADP do not share a common binding site and that the latent ATPase enzyme has separate sites for ATP hydrolysis and ATP synthesis.
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PMID:Binding of nucleotides to purified coupling factor-latent ATPase from Mycobacterium phlei. 1 31

Inbred rats were immunized with Freund's Adjuvant containing proteins of Mycogacterium tuberculosis, Mycobacterium butyrium, or dinitrochlorobenzene (DNCB). Native arterial blood was then passed over glass beads coated with those antigens. The platelet retention on the glass beads was measured. Rats immunized with Complete Freund's Adjuvant developed accelerated platelet retention on beads coated with protein derivatives of tuberculosis (PPD) after just 18 seconds of blood flow. Rats immunized twice maintained selective retention longer than those immunized once. The test animals developed no cutaneous hypersensitivity nor precipitin lines on Ouchterlong gels against PPD. Rats sensitized to DNCB had accelerated platelet retention on DNCB-coated beads. Results were temperature and complement dependent, and antigen-specific. Heparin caused a dose-dependent inhibition of the accelerated retention. PPD potentiated the ADP-induced aggregation of plateletrich plasma (PRP) from immunized rats. These experiments suggest that platelets react selectively to antigens in the intravascular spaces in immune reactions.
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PMID:Selective platelet immune retention. 9 7

The membrane-bound coupling factor from Mycobacterium phlei was solubilized from membrane vesicles by washing with low ionic strength buffer or 0.25 M sucrose. The solubilized enzyme exhibited coupling factor, latent ATPase, and succinate oxidation-stimulating activity. Purification by affinity chromatography using Sepharose coupled to ADP yielded a homogeneous preparation of latent ATPase which was purified about 200-fold with an 84% yield in a single step. Purified latent ATPase exhibited coupling factor activity but no succinate oxidation-stimulating activity. The molecular weight of latent ATPase was determined to be 250,000 +/- 10,000 by Sephadex G-200 chromatography. The ATPase was unmasked by trypsin treatment and activated by Mg2+ ion. However, trypsin treatment inactivated the coupling factor activity in the purified enzyme, indicating that the catalytic sites for ATPase and coupling activity are different. Unlike mitochondrial ATPase, latent ATPase from M. phlei was not cold-labile. Of the nucleoside triphosphates, UTP, ITP, and epsilon-ATP (1-N6-ethenoadenosine triphosphate) were hydrolyzed to a lesser extent compared to ATP. Kinetic data showed that ADP acted as a competitive inhibitor of latent ATPase activity with a Ki of 5 x 10(-3) M. Uncouplers of oxidative phosphorylation and respiratory inhibitors did not affect the latent ATPase activity, while sodium azide (0.1 mM) inhibited the latent ATPase activity.
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PMID:Energy-transducing membrane-bound coupling factor-ATPase from Mycobacterium phlei. I. Purification, homogeneity, and properties. 12 54

The membrane bound coupling factor-latent ATPase was solubilized from the membrane vesicles of Mycobacterium phlei by using 0.25 M sucrose or low ionic strength buffer. Purification of the solubilized enzyme by use of Sepharose-ADP conjugate gel yielded a homogenous preparation of latent ATPase which was purified about 216-fold in a single step with an 84% yield. The enzyme exhibits a specific activity of 39 mumoles of ATP hydrolyzed per min per mg protein. The purified enzyme exhibits coupling factor activity. Electrophoresis in two dissociating solvent systems indicates that the enzyme contains at least three major polypeptides of molecular weights 56,000, 51,000, and 46,000 daltons, and two minor polypeptides of 30,000 and 17,000 daltons. Equilibrium binding studies of ADP with purified coupling factor-latent ATPase reveal the presence of two nucleotide binding sites per molecule with an apparent Ka of 8.1 X 10(-5) M. By use of affinity chromatography, another latent ATPase has been isolated from the solubilized enzyme, which does not exhibit coupling factor activity.
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PMID:Purification and properties of membrane-bound coupling factor-latent ATPase from Mycobacterium phlei. 12 86

The N,N'-dicyclohexylcarbodiimide (DCCD)-sensitive latent adenosinetriphosphatase (ATPase) (EC 3.6.1.3; ATP phosphohydrolase) from Mycobacterium phlei has been purified to homogeneity and used to resotre oxidative phosphorylation to detergent-extracted membranes. The phosphorylation was inhibited by DCCD any by tetraphenylboron and valinomycin. The enzyme was solubilized from the membrane vesicles by treatment with cholate followed by extraction with Triton X-100. After partial purification on a sucrose gradient, the enzyme was purified to homogeneity by affinity chromatography on Sepharose coupled to ADP. The DCCD-sensitive latent ATPase of coupling factor from M. phlei consists of two components, the latent ATPase (Bcf4), which is insensitive to DCCD, and an intrinsic membrane component, BCF0. This hydrophobic portion of the DCCD-sensitive ATPase was partially purified on a sucrose gradient after solubilization with detergents from membrane vesicles that had been first depleted of the BCF4 by washing with 0.25 M sucrose. When BCF0 was combined with purified BCF4, the latent ATPase of the resulting complex was sensitive to DCCD. Moreover, like the purified DCCD-sensitive latent ATPase, the combined BCF4 and BCF0 restored coupled phosphorylation to detergent-extracted membranes.
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PMID:Restoration of oxidative phosphorylation by purified N,N'-dicyclohexylcarbodiimide-sensitive latent adenosinetriphosphatase from Mycobacterium phlei. 13 58

It is not known how Mycobacterium leprae obtains energy for survival and growth in the host tissues; the organism does not grow in vitro. In the studies reported here, M. leprae incorporated labelled ATP, which was blocked by cyanide, unlabelled ATP or ADP, but not by adenosine or Pi. It seems that the organism takes up unhydrolysed ATP by an active transport process. The bacterium contained a membrane-bound, vanadate-sensitive E1 E2-ATPase (which creates a transmembrane potential driving transport of solutes into cells). The enzyme was not inhibited by N-ethylmaleimide, suggesting that it is not an F0F1-ATPase which catalyses ATP synthesis. Apparently, M. leprae derives energy-rich compounds from the host cell.
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PMID:Active transport of ATP and presence of a vanadate-sensitive membrane-bound ATPase in Mycobacterium leprae. 183 12

Adenylate kinase (ATP:AMP phosphotransferase, EC 2.7.4.3) was detected in partially purified preparations of cell-free extracts of Mycobacterium leprae. The apparent Km values of M. leprae adenylate kinase for ADP and Mg2+ were 1 X 10(-4) M, respectively. The enzyme was heat-labile: loss of activity by 80% at 45 degrees C and over 90% at 60 degrees C occurred within 5 min. M. leprae adenylate kinase was distinct from armadillo adenylate kinase in respect of affinity for substrate and heat-sensitivity.
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PMID:Adenylate kinase activity in Mycobacterium leprae. 301 66

Crude extracts of Mycobacterium smegmatis catalyzed the synthesis of adenosine diphosphate-glucose (ADP-Glc), cytidine diphosphate-glucose, guanosine diphosphate-glucose (GDP-Glc), thymidine diphosphate-glucose (TDP-Glc), and uridine diphosphate-glucose (UDP-Glc). In these crude enzyme fractions, high concentrations of trehalose-P inhibited the ADP-Glc and GDP-Glc pyrophosphorylases but did not effect the UDP-Glc or TDP-Glc pyrophosphorylases. Both the ADP-Glc pyrophosphorylase and the UDP-Glc pyrophosphorylase were partially purified (about 140-fold and 60-fold, respectively), and their properties were compared. For the ADP-Glc pyrophosphorylase, the K(m) for adenosine triphosphate was 6 x 10(-4)m, whereas that for glucose-1-P was 8 x 10(-4)m. The optimal concentration of Mg(2+) was 1 x 10(-3)m, and the pH optimum was 8.5. For the UDP-Glc pyrophosphorylase, the K(m) for uridine triphosphate was 1 x 10(-3)m and for glucose-1-P was 2 x 10(-3)m. The optimal Mg(2+) concentration was 1 x 10(-3)m, and the pH optimum was about 8.0. The purified ADP-Glc pyrophosphorylase was inhibited by fructose-6-P, fructose-1, 6-diphosphate, glucose-6-P, and phosphoenolpyruvate. On the other hand, trehalose, trehalose diphosphate, sodium pyruvate, and ribose-5-P did not effect the ADP-Glc pyrophosphorylase. None of these compounds, including trehalose-P, had any effect on the UDP-Glc pyrophosphorylase.
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PMID:Purification and properties of the adenosine diphosphate-glucose and uridine diphosphate-glucose pyrophosphorylases of Mycobacterium smegmatis: inhibition and activation of the adenosine diphosphate-glucose pyrophosphorylase. 507 67

Two natural arabinolipids from the cell wall of Mycobacterium tuberculosis (5-mycoloyl-D-arabinose and 5-mycoloyldiarabinoside) and two synthetic arabinolipids (5-mycoloyl-L-arabinose and 5-mycoloyl(2'-hydroxyethyl)L-arabinoside) were tested on rat liver mitochondria. 5-Mycoloyl D- and L-rabinose had the same low activity, while 5-mycoloyldiarabinoside efficiently lowered the ADP/O ratio, inhibited active respiration and increased controlled respiration. The synthetic 5-mycoloyl(2'-hydroxyethyl)arabinoside had an intermediate efficiency. Due to their activity on mitochondria, the arabinolipids of the mycobacterial cell wall can be considered as potential endotoxins.
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PMID:Mycobacteria arabinolipids as potential endotoxins: their activity on mitochondrial oxidative phosphorylation. 641 50

Pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40) from Mycobacterium smegmatis has been purified to homogeneity through a seven-step procedure with a yield of 16% and specific activity of 220 units/mg protein. The purified enzyme had a molecular weight of 230,700 and was composed of four subunits with identical molecular weights of 57,540. Analysis of amino acid composition revealed a low content of aromatic amino acids. The enzyme exhibited sigmoidal kinetics of varying concentrations of phosphoenolpyruvate, the degree of cooperativity and S0.5v value for phosphoenolpyruvate being strongly dependent on the pH of the reaction mixture. Among the nucleoside diphosphates acting as substrate for pyruvate kinase, ADP was the best phosphate acceptor, as judged by its lowest Km value. The enzyme showed an absolute requirement for divalent cations (either Mg2+ or Mn2+), but monovalent cations were not necessary for activity. Other divalent cations inhibited the Mg2+-activated enzyme to varying degrees (Ni2+ greater than Zn2+ greater than Cu2+ greater than Ca2+ greater than Ba2+). The differences in the kinetic responses of the enzyme to Mg2+ and Mn2+ are discussed.
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PMID:Purification and properties of pyruvate kinase from Mycobacterium smegmatis. 661 24


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