Literature DB >> 28309917

Responses of amino acid metabolizing enzymes from plants differing in salt tolerance to NaCl.

A Priebe1, H-J Jäger1.   

Abstract

This paper reports the effects of NaCl on the in vivo activity of glutamate dehydrogenase (GDH) and glutamic-oxaloacetic transaminase (GOT) and on the in vitro activity of GDH, both enzymes having been isolated from plants differing in salt tolerance. The plants investigated were Vicia faba (salt-sensitive), Atriplex nitens and Atriplex calotheca (more or less salt-tolerant), and Atriplex halimus (halophyte) grown at various NaCl concentrations. GDH and GOT isolated from various salt-tolerant plants grown at low NaCl concentrations were inhibited in a similar way. At high NaCl concentrations, the enzyme activities remain at constant values only in the Atriplex species. GOT was more impaired by NaCl than GDH. In the case of GOT, the double reciprocal plot indicated the type of a noncompetitive inhibition. The in vitro effect of NaCl on the activity of GDH from the differentially salt-tolerant plants was of a different kind, i.e. GDH isolated from V. faba was clearly inhibited by NaCl, whereas NaCl stimulated the activity of GDH from all Atriplex species investigated. Kinetic analysis showed that substrate inhibition of GDH from A. nitens and A. calotheca grown at non-saline conditions could be removed by NaCl. Inhibition by high NaCl concentrations at low substrate concentrations was removable by increasing substrate concentrations. Moreover, the inhibition at low substrate concentrations was shown to be competitive. GDH lost this regulatory property when the plants were pretreated with 500 mM NaCl. GDH from A. halimus also possessed this control, but in contrast to A. nitens and A. calotheca, activity and control of GDH isolated from A. halimus were stimulated by pretreating the plants with 500 mM NaCl. The results showed that DDH isolated from the salt-tolerant Atriplex species was adapted to high NaCl concentrations of the tissue. Possible mechanisms of the interactions between GDH from salt-tolerant Atriplex species and NaCl are discussed.

Entities:  

Year:  1978        PMID: 28309917     DOI: 10.1007/BF00348056

Source DB:  PubMed          Journal:  Oecologia        ISSN: 0029-8549            Impact factor:   3.225


  13 in total

1.  Studies of glutamate dehydrogenase. Regulation of glutamate dehydrogenase from Candida utilis by a pH and temperature-dependent conformational transition.

Authors:  P Neumann; K Markau; H Sund
Journal:  Eur J Biochem       Date:  1976-06-01

2.  Sodium as an Essential Micronutrient Element for a Higher Plant (A triplex vesicaria).

Authors:  P F Brownell
Journal:  Plant Physiol       Date:  1965-05       Impact factor: 8.340

3.  [Allosteric regulation of the activity of glutamate dehydrogenase from pea seedlings by the substrate α-ketoglutarate].

Authors:  E Pahlich
Journal:  Planta       Date:  1971-09       Impact factor: 4.116

4.  The role of proline accumulation in halophytes.

Authors:  G R Stewart; J A Lee
Journal:  Planta       Date:  1974-01       Impact factor: 4.116

5.  The effect of neutral salt anions on the oxidative deamination activity of plant glutamate dehydrogenase.

Authors:  E Pahlich; B Gelleri; R Kindt
Journal:  Planta       Date:  1978-01       Impact factor: 4.116

6.  Effect of water stress on growth and proline metabolism of Phaseolus vulgaris L.

Authors:  H -J Jäger; H R Meyer
Journal:  Oecologia       Date:  1977-03       Impact factor: 3.225

7.  [Effect of sodium chloride on respiration and the activity of malate dehydrogenase in some halophytes and glycophytes].

Authors:  Dieter Joachim von Willert
Journal:  Oecologia       Date:  1974-03       Impact factor: 3.225

8.  Malic dehydrogenase from tamarix roots: effects of sodium chloride in vivo and in vitro.

Authors:  A Kalir; A Poljakoff-Mayber
Journal:  Plant Physiol       Date:  1975-02       Impact factor: 8.340

9.  Salt responses of enzymes from species differing in salt tolerance.

Authors:  H Greenway
Journal:  Plant Physiol       Date:  1972-02       Impact factor: 8.340

10.  Salt responses of carboxylation enzymes from species differing in salt tolerance.

Authors:  C B Osmond
Journal:  Plant Physiol       Date:  1972-02       Impact factor: 8.340

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