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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Arum

 
 
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High impact information on Arum

  • The subcellular location of the two porphyrin-synthesis enzymes 5-aminolaevulinate dehydratase (ALAD) and porphobilinogen deaminase (PBGD) was investigated in Pisum sativum (pea) leaves and spadices of Arum (cuckoo-pint) [1].
  • Throughout the tissue-fractionation procedures the distribution of the two enzymes paralleled that of the plastid marker enzyme (ADP-glucose pyrophosphorylase), even in Arum, a tissue where the synthesis of non-plastid haem is predominant [1].
  • 1. Mitochondria isolated from the thermogenic spadices of Arum maculatum and Sauromatum guttatum plants oxidized external NADH, succinate, citrate, malate, 2-oxoglutarate and pyruvate without the need to add exogenous cofactors [2].
  • These plots were linear in the absence of an activating anion, which may indicate that the catalytic and/or regulatory mechanism of Arum maculatum adenosine triphosphatase is different from that of other enzyme preparations [3].
  • Inhibitor-sensitivities and water-forming DQH2 (tetramethyl-p-hydroquinone, reduced form): O2 stoichiometry were the same for the alternative oxidase of intact Arum mitochondria [4].
 

Anatomical context of Arum

 

Associations of Arum with chemical compounds

 

Gene context of Arum

  • Depending on the fungal species, wild-type tomato forms both major morphological AM types, Arum and Paris. The mutant rmc blocks the penetration of the root surface or invasion of the root cortex by most species of AM fungi, but one fungus has been shown to develop normal mycorrhizas [11].
  • We have purified plant alternative oxidase (AOX) protein from the spadices of thermogenic Arum maculatum (cuckoo pint) to virtual homogeneity [12].

References

  1. Subcellular localization of two porphyrin-synthesis enzymes in Pisum sativum (pea) and Arum (cuckoo-pint) species. Smith, A.G. Biochem. J. (1988) [Pubmed]
  2. Pyruvate transport by thermogenic-tissue mitochondria. Proudlove, M.O., Beechey, R.B., Moore, A.L. Biochem. J. (1987) [Pubmed]
  3. Characterization of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatases. Dunn, P.P., Slabas, A.R., Moore, A.L. Biochem. J. (1986) [Pubmed]
  4. Solubilization of the alternative oxidase of cuckoo-pint (Arum maculatum) mitochondria. Stimulation by high concentrations of ions and effects of specific inhibitors. Kay, C.J., Palmer, J.M. Biochem. J. (1985) [Pubmed]
  5. ESEEM studies of the iron-sulphur clusters of succinate dehydrogenase in Arum maculatum spadix mitochondrial membranes. Shergill, J.K., Cammack, R. Biochim. Biophys. Acta (1994) [Pubmed]
  6. Characterization of iron-sulphur centres of plant mitochondria by microwave power saturation. Rupp, H., Moore, A.L. Biochim. Biophys. Acta (1979) [Pubmed]
  7. 9-Aminoacridine as a fluorescent probe of the electrical diffuse layer associated with the membranes of plant mitochondria. Møller, I.M., Chow, W.S., Palmer, J.M., Barber, J. Biochem. J. (1981) [Pubmed]
  8. Pyrophosphate:fructose 6-phosphate 1-phosphotransferase and glycolysis in non-photosynthetic tissues of higher plants. ap Rees, T., Green, J.H., Wilson, P.M. Biochem. J. (1985) [Pubmed]
  9. New inhibitors of the ubiquinol oxidase of higher plant mitochondria. Hoefnagel, M.H., Wiskich, J.T., Madgwick, S.A., Patterson, Z., Oettmeier, W., Rich, P.R. Eur. J. Biochem. (1995) [Pubmed]
  10. Discrimination between duroquinol oxidase activity and the terminal oxidation step of the cyanide-resistant electron transport pathway of plant mitochondria. Rustin, P., Alin, M.F., Lance, C. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
  11. Expression patterns of defense-related genes in different types of arbuscular mycorrhizal development in wild-type and mycorrhiza-defective mutant tomato. Gao, L.L., Knogge, W., Delp, G., Smith, F.A., Smith, S.E. Mol. Plant Microbe Interact. (2004) [Pubmed]
  12. Purification of the plant alternative oxidase from Arum maculatum: measurement, stability and metal requirement. Affourtit, C., Moore, A.L. Biochim. Biophys. Acta (2004) [Pubmed]
 
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