Interface Mutants of Glyoxasomal Malate Dehydrogenase
نویسندگان
چکیده
منابع مشابه
THE EFFECT OF SALT STRESS ON MALATE DEHYDROGENASE IN WHEAT
Effect of various NaCI treatments (0, 50, 100, 200 and 300 mM) at different growth and development stages (tillering, boot swollen, flowering and anthesis) of two wheat cultivars on the kinetic activity and PAGE electrophoretic pattern of leaf malate dehydrogenase was studied under greenhouse conditions. Ghods was salt-sensitive and Boolani was salt-tolerant. In general, in response to salinti...
متن کاملRegulation of Mitochondrial Malate Dehydrogenase
The effect of citrate on the structure and function of porcine heart mitochondrial malate dehydrogenase (EC 1.1.1.37) has been characterized. The native dimeric form of this enzyme is specifically activated by citrate in the NAD’ -+ NADH direction and inhibited by citrate in the NADH -+ NAD’ direction. It is proposed that citrate is bound at a regulatory site that is distinct from the catalytic...
متن کاملIndependent spontaneous mitochondrial malate dehydrogenase null mutants in soybean are the result of deletions.
The mitochondrial malate dehydrogenase-1 (Mdh1) gene of soybean [Glycine max (L.) Merr.] spontaneously mutates to a null phenotype at a relatively high rate. To determine the molecular basis for the instability of the Mdh1 gene, the gene was cloned and sequenced. The null phenotype correlated with the deletion of specific genomic restriction fragments that encode the Mdh1 gene. The composition ...
متن کاملConvergent evolution of Trichomonas vaginalis lactate dehydrogenase from malate dehydrogenase.
Lactate dehydrogenase (LDH) is present in the amitochondriate parasitic protist Trichomonas vaginalis and some but not all other trichomonad species. The derived amino acid sequence of T. vaginalis LDH (TvLDH) was found to be more closely related to the cytosolic malate dehydrogenase (MDH) of the same species than to any other LDH. A key difference between the two T. vaginalis sequences was tha...
متن کاملInterface Matters: The Stiffness Route to Stability of a Thermophilic Tetrameric Malate Dehydrogenase
In this work we investigate by computational means the behavior of two orthologous bacterial proteins, a mesophilic and a thermophilic tetrameric malate dehydrogenase (MalDH), at different temperatures. Namely, we quantify how protein mechanical rigidity at different length- and time-scales correlates to protein thermophilicity as commonly believed. In particular by using a clustering analysis ...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2006
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.20.4.a54-a