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Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant.
Biochem Biophys Res Commun. 2006 Aug 25; 347(2):502-8.BB

Abstract

To elucidate the structural basis for the alteration of coenzyme specificity from NADH toward NADPH in a malate dehydrogenase mutant EX7 from Thermus flavus, we determined the crystal structures at 2.0 A resolution of EX7 complexed with NADPH and NADH, respectively. In the EX7-NADPH complex, Ser42 and Ser45 form hydrogen bonds with the 2'-phosphate group of the adenine ribose of NADPH, although the adenine moiety is not seen in the electron density map. In contrast, although Ser42 and Ser45 occupy a similar position in the EX7-NADH complex structure, both the adenine and adenine ribose moieties of NADH are missing in the map. These results and kinetic analysis of site-directed mutant enzymes indicate (1) that the preference of EX7 for NADPH over NADH is ascribed to the recognition of the 2'-phosphate group by two Ser and Arg44, and (2) that the adenine moiety of NADPH is not recognized in this mutant.

Authors+Show Affiliations

Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Tokyo 113-8657, Japan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

16828705

Citation

Tomita, Takeo, et al. "Structural Basis for the Alteration of Coenzyme Specificity in a Malate Dehydrogenase Mutant." Biochemical and Biophysical Research Communications, vol. 347, no. 2, 2006, pp. 502-8.
Tomita T, Fushinobu S, Kuzuyama T, et al. Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant. Biochem Biophys Res Commun. 2006;347(2):502-8.
Tomita, T., Fushinobu, S., Kuzuyama, T., & Nishiyama, M. (2006). Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant. Biochemical and Biophysical Research Communications, 347(2), 502-8.
Tomita T, et al. Structural Basis for the Alteration of Coenzyme Specificity in a Malate Dehydrogenase Mutant. Biochem Biophys Res Commun. 2006 Aug 25;347(2):502-8. PubMed PMID: 16828705.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant. AU - Tomita,Takeo, AU - Fushinobu,Shinya, AU - Kuzuyama,Tomohisa, AU - Nishiyama,Makoto, Y1 - 2006/06/30/ PY - 2006/06/08/received PY - 2006/06/22/accepted PY - 2006/7/11/pubmed PY - 2006/9/22/medline PY - 2006/7/11/entrez SP - 502 EP - 8 JF - Biochemical and biophysical research communications JO - Biochem. Biophys. Res. Commun. VL - 347 IS - 2 N2 - To elucidate the structural basis for the alteration of coenzyme specificity from NADH toward NADPH in a malate dehydrogenase mutant EX7 from Thermus flavus, we determined the crystal structures at 2.0 A resolution of EX7 complexed with NADPH and NADH, respectively. In the EX7-NADPH complex, Ser42 and Ser45 form hydrogen bonds with the 2'-phosphate group of the adenine ribose of NADPH, although the adenine moiety is not seen in the electron density map. In contrast, although Ser42 and Ser45 occupy a similar position in the EX7-NADH complex structure, both the adenine and adenine ribose moieties of NADH are missing in the map. These results and kinetic analysis of site-directed mutant enzymes indicate (1) that the preference of EX7 for NADPH over NADH is ascribed to the recognition of the 2'-phosphate group by two Ser and Arg44, and (2) that the adenine moiety of NADPH is not recognized in this mutant. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/16828705/Structural_basis_for_the_alteration_of_coenzyme_specificity_in_a_malate_dehydrogenase_mutant_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(06)01445-8 DB - PRIME DP - Unbound Medicine ER -