Amino acid residues that determine functional specificity of NADP- and NAD-dependent isocitrate and isopropylmalate dehydrogenases

Olga V. Kalinina, Mikhail S. Gelfand

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

Isocitrate and isopropylmalalte dehydrogenases are homologous enzymes important for the cell metabolism. They oxidize their substrates using NAD or NADP as cofactors. Thus, they have two specificities, towards the substrate and the cofactor, appearing in three combinations. Although many three-dimensional (3D) structures are resolved, identification of amino acids determining these specificities remains a challenge. We present computational identification and analysis of specificity-determining positions (SDPs). Besides many experimentally proven SDPs, we predict new SDPs, for example, four substrate-specific positions (103Leu, 105Thr, 337Ala, and 341Thr in IDH from E. coli) that contact the cofactor and may play a role in the recognition process.

Original languageEnglish
Pages (from-to)1001-1009
Number of pages9
JournalProteins: Structure, Function and Genetics
Volume64
Issue number4
DOIs
Publication statusPublished - 1 Sep 2006
Externally publishedYes

Keywords

  • Isocitrate dehydrogenase
  • Protein function
  • Specificity determinants
  • Specificity-determining positions (SDP)

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