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Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity.
J Biol Chem. 1986 Oct 25; 261(30):14178-83.JB

Abstract

The nucleotide sequence of the malate dehydrogenase (mdh) gene from a thermophilic bacterium, Thermus flavus, was determined. The amino acid sequence of the Thermus malate dehydrogenase resembled that of the porcine heart cytoplasmic enzyme to a certain extent, and Asp-159 and His-187 were identified as possible essential residues for the catalytic function. The mutated mdh gene was also cloned from a spontaneous mutant of T. flavus containing a higher activity of the enzyme. Its mutation point was determined to be a single nucleotide exchange from C to T which caused Thr-190 to be substituted by isoleucine. The mutated enzyme showed resistance to substrate inhibition, an increase in both kcat and Km, and a shift toward a more acid optimum pH for the enzyme reaction.

Authors

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Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

3771528

Citation

Nishiyama, M, et al. "Nucleotide Sequence of the Malate Dehydrogenase Gene of Thermus Flavus and Its Mutation Directing an Increase in Enzyme Activity." The Journal of Biological Chemistry, vol. 261, no. 30, 1986, pp. 14178-83.
Nishiyama M, Matsubara N, Yamamoto K, et al. Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity. J Biol Chem. 1986;261(30):14178-83.
Nishiyama, M., Matsubara, N., Yamamoto, K., Iijima, S., Uozumi, T., & Beppu, T. (1986). Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity. The Journal of Biological Chemistry, 261(30), 14178-83.
Nishiyama M, et al. Nucleotide Sequence of the Malate Dehydrogenase Gene of Thermus Flavus and Its Mutation Directing an Increase in Enzyme Activity. J Biol Chem. 1986 Oct 25;261(30):14178-83. PubMed PMID: 3771528.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity. AU - Nishiyama,M, AU - Matsubara,N, AU - Yamamoto,K, AU - Iijima,S, AU - Uozumi,T, AU - Beppu,T, PY - 1986/10/25/pubmed PY - 1986/10/25/medline PY - 1986/10/25/entrez SP - 14178 EP - 83 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 261 IS - 30 N2 - The nucleotide sequence of the malate dehydrogenase (mdh) gene from a thermophilic bacterium, Thermus flavus, was determined. The amino acid sequence of the Thermus malate dehydrogenase resembled that of the porcine heart cytoplasmic enzyme to a certain extent, and Asp-159 and His-187 were identified as possible essential residues for the catalytic function. The mutated mdh gene was also cloned from a spontaneous mutant of T. flavus containing a higher activity of the enzyme. Its mutation point was determined to be a single nucleotide exchange from C to T which caused Thr-190 to be substituted by isoleucine. The mutated enzyme showed resistance to substrate inhibition, an increase in both kcat and Km, and a shift toward a more acid optimum pH for the enzyme reaction. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/3771528/Nucleotide_sequence_of_the_malate_dehydrogenase_gene_of_Thermus_flavus_and_its_mutation_directing_an_increase_in_enzyme_activity_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=3771528 DB - PRIME DP - Unbound Medicine ER -