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
Query: EC:1.4.1.2 (
glutamate dehydrogenase
)
4,380
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
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.
...
PMID:Responses of amino acid metabolizing enzymes from plants differing in salt tolerance to NaCl. 2830 17
