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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Specific antibody to a fragment [CBb(2-56)] of porcine muscle adenylate kinase was purified from goat antiserum against adenylate kinase on an immunoadsorbent column. This anti-CBb antibody cross-reacted in solid phase radioimmunoassay with two other CNBr-fragments of adenylate kinase, CBfN(81-125) and CBfC(126-194). This cross-reactivity explained their high inhibition activities in quantitative precipitin reaction between adenylate kinase and goat antiserum shown in the previous work. Cysteinyl residues of the enzyme (positions 25 and 187) were S-cyanylated with 2-nitro-5-thiocyanobenzoic acid and the enzyme was cleaved at these residues. Fragment 1-24 thus obtained was purified. The fragment 1-24, composing the N-terminal half of CBb(2-56), accounted for full activity of CBb to anti-CBb in radioimmunoassay. Hence antigenic region(s) of CBb(2-56) exist in its N-terminal half, 2-24, and this determinant(s) may be closely related to the cross-reactivity among CB-fragments. CBfN also bound to the antibody fraction which had not been adsorbed to CBb-Sepharose (non-anti-CBb). CBfN carried additional antigenic regions. In conclusion, we propose that the antigenic reactive region(s) of adenylate kinase responsible for the cross-reactivity of the CB-fragments are as follows: -Glu-Glu-Lys-Leu-Lys-Lys- (2-7), -Glu-Glu-Phe-Lys-Arg-Lys- (103-108), -Glu-Glu-Thr-Ile-Lys-Lys- (143-148).
Mol Immunol 1983 Aug
PMID:Antigenic structure of adenylate kinase from porcine skeletal muscle--II. Immunochemical cross-reactivity of fragments from adenylate kinase. 619 28

A dnaW mutant, isolated on the basis of inability to effect conjugal DNA transfer at high temperature, has been shown by complementation and enzyme assay to be defective in the adk (adenylate kinase; EC 2.7.4.3) locus. The adk mutant, known to have reduced ATP concentration at the nonpermissive temperature (Cousin and Belaich 1966), was used to demonstrate a donor energy requirement for stable aggregate formation and for chromosome transfer in conjugation.
Mol Gen Genet 1982
PMID:The Escherichia coli dnaW mutation is an allele of the adk gene. 629 Aug 47

Human muscle adenylate kinase (ATP:AMP phosphotransferase, EC 2.7.4.3.) was studied by 1H-nuclear magnetic resonance spectroscopy. The C-2 and C-4 proton resonances of the active-center histidine His-36 could be identified; the pK of His-36 was determined as 6.1. The pK of His-189 is very low (4.9) although it is located at the surface of the protein. Other resonance lines are discussed in comparison with NMR spectra of porcine adenylate kinase [McDonald et al. (1975) J. Biol. Chem. 250, 6947-6954]. A pH-dependent structural isomerization as shown by X-ray crystallography in the pig enzyme [Pai et al. (1977) J. Mol. Biol. 114, 37-45] was not observed for human adenylate kinase in solution. However, the binding of adenosine(5')pentaphospho(5')adenosine (Ap5A), a bisubstrate inhibitor, to adenylate kinase causes an overall change of the NMR spectrum indicative of a large conformational change of the enzyme. The exchange rate (koff) for Ap5A was estimated as 10 s-1 and decreases by addition of Mg2+. On the basis of these values and the known dissociation constant it is likely that the binding of Ap5A is a diffusion-controlled process kon being 10(8) M-1 s-1. In conclusion, the system Ap5A/Mg2+/human adenylate kinase, which has been studied by NMR spectroscopy and X-ray diffraction in parallel, is suitable for analyzing the induced fit postulated by Jencks for all kinase-catalyzed reactions.
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PMID:The structural isomerisation of human-muscle adenylate kinase as studied by 1H-nuclear magnetic resonance. 629 31

The alpha, beta, gamma-tridentate complex of CrATP, a paramagnetic competitive inhibitor of porcine adenylate kinase, increases the longitudinal [1/(fT1p)] and transverse [1/(fT2p)] relaxation rates of a resonance of the enzyme previously assigned by McDonald et al. [McDonald, G.G., Cohn, M., & Noda, L. (1975) J. Biol. Chem. 250, 6947-6954] to the C2 proton of histidine-36. These paramagnetic effects are diminished upon the addition of the substrate MgATP by an amount consistent with the simple displacement of CrATP. The 1/(fT2p) value sets a lower limit of 400 s-1 on the rate constant for dissociation of CrATP from the enzyme. The 1/(fT1p) value at 250 MHz and the correlation time for water protons in the same complex are used to calculate a distance of 12.9 +/- 1.0 A from Cr(III) to the C2 proton of histidine-36. A primary, negative nuclear Overhauser effect is detected on the adenine H2 resonance of enzyme-bound MgATP upon preirradiation of the C2 proton of histidine-36, indicating that these protons are approximately less than 5 A apart. These distances and negative intramolecular Overhauser effects from the ribose protons to adenine H8 of MgATP indicate an extended structure for bound MgATP with an anti conformation about the glycosidic bond. These findings require a different orientation or location of the bound metal-ATP substrate from that proposed based on X-ray studies of the binding of salicylate [Pai, E. F., Sachsenheimer, W., & Schirmer, R.H. (1977) J. Mol. Biol. 114, 37-45]. Other nuclear Overhauser effects from resonances of the protein at 1.8 and 0.9 ppm to both adenine H2 and ribose H1' of bound MgATP indicate the proximity to the substrate of at least one Arg C beta proton (at 1.8 ppm), C gamma proton (at 1.7 ppm), Lys C delta proton (at 1.7 ppm), or Leu C beta proton (at 1.6 ppm) and one or more Leu, Ile, or Val methyl groups (at 0.9 ppm). Entirely different Overhauser effects are observed from the enzyme to the adenine protons of AMP consistent with a distinct site for the other substrate.
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PMID:Nuclear magnetic resonance studies of the nucleotide binding sites of porcine adenylate kinase. 629 55

Selective inactivation of the multiple forms of mitochondrial monoamine oxidase (MAO) by proteases in intact and hypotonically disrupted rat liver mitochondria has been used to examine the question of differential membrane orientations of the A and B enzymes. Proteases used as probes included trypsin, beta-chymotrypsin, and the extracellular protease of Staphylococcus aureus, chosen for their different amino acid specificities. With all three proteases, no changes in the relative rates of MAO-A and MAO-B inactivation were observed after disruption of the mitochondria. Trypsin and beta-chymotrypsin gave much faster rates of MAO-A inactivation in both intact and disrupted mitochondria. The selective effect of trypsin on MAO-A was also confirmed in human placental mitochondria, which possess only A-type activity. The effectiveness of hypotonicity in disrupting the outer membrane of the mitochondria was shown by rapid protease inactivation of an intermembrane space marker enzyme, adenylate kinase (EC 2.7.4.3). Contrary to some recent reports in the literature, these findings strongly suggest that the MAO-A and MAO-B multiple-form catalytic activities do not reside on opposite faces of the membrane.
Mol Pharmacol 1984 Jan
PMID:Proteases as probes of mitochondrial monoamine oxidase topography in situ. 636 8

Evidence is presented for the occurrence of glycosomes (organelles resembling peroxisomes) in four major species of Leishmania (viz. L. major, L.m. mexicana, L. b. braziliensis and L. donovani), based on latency as well as differential and isopycnic centrifugation studies. The enzymes involved in glycolysis; (hexokinase, phosphoglucose isomerase, phosphofructokinase, fructose-1,6-bisphosphate aldolase, triosephosphate isomerase, glyceraldehyde-phosphate dehydrogenase and phosphoglycerate kinase); glycerol metabolism (sn-glycerol-3-phosphate dehydrogenase and glycerol kinase); carbon dioxide fixation (phosphoenolpyruvate carboxykinase and possibly malate dehydrogenase); together with an enzyme involved in the beta-oxidation of fatty acids (3-beta-hydroxybutyryl coenzyme A dehydrogenase); a key enzyme in the synthesis of ether lipids (dihydroxyacetone phosphate acyltransferase) as well as the ADP utilising enzyme adenylate kinase, were all found associated, at least in part, with a subcellular organelle which had a buoyant density in sucrose gradients of 1.21 to 1.24 g cm-3. Little variance in enzyme composition was found between the different species of Leishmania or in comparison with other members of the Trypanosomatidae, supporting the unifying principle that glycosomes are a unique characteristic of this family. The occurrence of important catabolic, anabolic and anaplerotic pathways in the glycosomes of Leishmania renders them prime targets for chemotherapy.
Mol Biochem Parasitol 1984 Oct
PMID:The occurrence of glycosomes (microbodies) in the promastigote stage of four major Leishmania species. 644 18

Highly purified glycosomes were isolated from Trypanosoma brucei bloodstream forms and cultured procyclic trypomastigotes. A comparison of the specific activities of glycosomal enzymes revealed that glycosomes from insect stages had decreased levels of hexokinase, phosphoglucose isomerase, phospho-fructokinase, fructose-bisphosphate aldolase, glyceraldehyde-phosphate dehydrogenase and phosphoglycerate kinase, but contained increased levels of adenylate kinase, malate dehydrogenase and phosphoenolpyruvate carboxykinase. Glycosomes from bloodstream forms were almost totally devoid of the latter two activities. Comparison of the two types of glycosomes by sodium dodecylsulphate-polyacrylamide gel electrophoresis revealed that bloodstream form glycosomes contained 3 prominent polypeptides (64, 46 and 40 kDa) which were hardly detectable in insect stage glycosomes, whereas the latter contained 3 insect stage specific bands with molecular weight of 34 000, 61 000 and 77 000 and 4 additional bands with molecular weights between 94 000 and 110 000. Both types of glycosome contained the phospholipids phosphatidylcholine and phosphatidylethanolamine. Insect stage glycosomes contained in addition also phosphatidylinositol and some phosphatidylserine.
Mol Biochem Parasitol 1984 May
PMID:A comparison of the glycosomes (microbodies) isolated from Trypanosoma brucei bloodstream form and cultured procyclic trypomastigotes. 674 87

Procyclic culture forms of Trypanosoma brucei stock 427 have been screened for the presence of enzymes involved in glycolysis, mitochondrial energy metabolism and threonine degradation. The enzyme activities in the procyclics were compared with those of the blood stream forms. The specific activities of glycolytic enzymes represented 30-70% of the respective levels in the blood stream form, except for hexokinase which was 25-fold reduced. Cell fractionation showed that the enzymes involved in the early sequence of the glycolytic pathway, i.e. from hexokinase to phosphoglycerate kinase, and the enzymes NAD+-linked glycerol-3-phosphate dehydrogenase and glycerol kinase were all present in glycosomes equilibrating at a density of 1.23 g/cm3 in sucrose gradients. Malate dehydrogenase was 8-fold more active in procyclics than in bloodstream forms. This increase in activity was the result of the appearance of malate dehydrogenase in the glycosomes of the procyclics, in addition to mitochondrial and cell-sap activities which were present in both stages of the life cycle. Glycosomes contained part of the adenylate kinase activity, which was also associated with the mitochondrion. Succinate dehydrogenase and sn-glycerol-3-phosphate dehydrogenase, together with oligomycin-sensitive ATPase, were located in the mitochondrion which had a density in sucrose ranging from 1.16 to 1.18 g/cm3. This organelle also contained L-threonine 3-dehydrogenase and carnitine acetyltransferase, two enzymes involved in threonine catabolism. The latter two enzymes had activities which were, respectively, 15-and 13-fold higher in the procyclics than in the bloodstream form. Mitochondrial sn-glycerol-3-phosphate dehydrogenase was decreased 4-fold.
Mol Biochem Parasitol 1981 Dec 31
PMID:Localization of malate dehydrogenase, adenylate kinase and glycolytic enzymes in glycosomes and the threonine pathway in the mitochondrion of cultured procyclic trypomastigotes of Trypanosoma brucei. 680 9

The current problems of regulation of myocardial energy metabolism and oxidative phosphorylation in vivo are considered. With this purpose, retarded diffusion of ADP in cardiomyocytes was studied by analysis of elevated apparent Km for this substrate in regulation of respiration of saponin-skinned cardiac fibers, as compared to isolated mitochondria. Recently published data showing the importance of the outer mitochondrial membrane were compared with new experimental results on the proteolysis of skinned fibers and tissue homogenates. In both cases 10 min incubation and 0.125 mg/ml of trypsin resulted in a decrease of apparent Km for ADP from 297 +/- 35 and 228 +/- 16 to 109 +/- 2 and 36 +/- 16, respectively. Thus, the permeability of the outer mitochondrial membrane for ADP may be controlled by some unknown cytoplasmic protein(s), probably related to the cytoskeleton, which are separated from mitochondria during their isolation. The extent of expression of this protein(s) depends on the energy state and type of muscle. Activation of mitochondrial creatine kinase reaction coupled to oxidative phosphorylation overcomes the diffusion difficulties of ADP by amplifying the stimulatory effect of ADP on respiration. It is concluded that both cytoplasmic and mitochondrial creatine kinases, adenylate kinase and cytoplasmic factor controlling outer membrane permeability may participate in metabolic feedback regulation of respiration in muscle cells.
J Mol Cell Cardiol 1995 Jan
PMID:Control of cellular respiration in vivo by mitochondrial outer membrane and by creatine kinase. A new speculative hypothesis: possible involvement of mitochondrial-cytoskeleton interactions. 776 Mar 82

Previously, we characterized nucleotide sequences of two cDNAs encoding adenylate kinase from rice plants (Oryza sativa L.). Each cDNA (Adk-a or Adk-b) was cloned into the expression vector pET 11d-GST to produce GST-AK fusion proteins in Escherichia coli. Recombinant proteins were cleaved by thrombin, and GST-free adenylate kinase proteins were obtained. Enzyme activity profiles of different pH and inhibition effects to the enzyme by Ap5A (adenosine-5'-pentaphospho-5'-adenosine) indicates that both adenylate kinase proteins have similar biochemical characteristics. Among the nucleoside monophosphates (AMP, CMP, GMP and UMP) investigated, only AMP reacted with ATP. Furthermore, using the antiserum against the rice adenylate kinase proteins, the cellular location of adenylate kinase proteins was examined by immunomicroscopic analysis in combination with a subcellular fractionation method. The results indicated that adenylate kinase proteins were distributed largely in cytosol of rice cells.
Plant Mol Biol 1995 Mar
PMID:Biochemical properties of rice adenylate kinase and subcellular location in plant cells. 776 84


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