Effect of Interactions Between Amino Acid Residues 43 and 61 on Thermal Stability of Bacterial Formate Dehydrogenases View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-10

AUTHORS

V. V. Fedorchuk, A. G. Galkin, I. E. Yasny, L. B. Kulakova, A. M. Rojkova, A. A. Filippova, V. I. Tishkov

ABSTRACT

NAD+-dependent formate dehydrogenases (EC 1.2.1.2, FDH) of methylotrophic bacteria Pseudomonas sp. 101 (PseFDH) and Mycobacterium vaccae N10 (MycFDH) exhibit high homology. They differ in two amino acid residues only among a total of 400, i.e., Ile35 and Glu61 in MycFDH substitute for Thr35 and Lys61 as in PseFDH. However, the rate constant for MycFDH thermal inactivation in the temperature range of 54-65 degrees C is 4-6-times higher than the corresponding rate constant for the enzyme from Pseudomonas sp. 101. To clarify the role of these residues in FDH stability the dependence of the apparent rate constant for enzyme inactivation on phosphate concentration was studied. Kinetic and thermodynamic parameters for thermal inactivation were obtained for both recombinant wild-type and mutant forms, i.e., MycFDH Glu61Gln, Glu61Pro, Glu61Lys and PseFDH Lys61Arg. It has been shown that the lower stability of MycFDH compared to that of PseFDH is caused mainly by electrostatic repulsion between Asp43 and Glu61 residues. Replacement of Lys61 with an Arg residue in the PseFDH molecule does not result in an increase in stability. More... »

PAGES

1145-1151

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1020915324159

DOI

http://dx.doi.org/10.1023/a:1020915324159

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031777334

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12460112


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