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Amino acid residues that determine functional specificity of NADP- and NAD-dependent isocitrate and isopropylmalate dehydrogenases.
Proteins. 2006 Sep 01; 64(4):1001-9.P

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.

Authors+Show Affiliations

Department of Bioengineering and Bioinformatics, Moscow State University, Moscow, Russia.No affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

16767773

Citation

Kalinina, Olga V., and Mikhail S. Gelfand. "Amino Acid Residues That Determine Functional Specificity of NADP- and NAD-dependent Isocitrate and Isopropylmalate Dehydrogenases." Proteins, vol. 64, no. 4, 2006, pp. 1001-9.
Kalinina OV, Gelfand MS. Amino acid residues that determine functional specificity of NADP- and NAD-dependent isocitrate and isopropylmalate dehydrogenases. Proteins. 2006;64(4):1001-9.
Kalinina, O. V., & Gelfand, M. S. (2006). Amino acid residues that determine functional specificity of NADP- and NAD-dependent isocitrate and isopropylmalate dehydrogenases. Proteins, 64(4), 1001-9.
Kalinina OV, Gelfand MS. Amino Acid Residues That Determine Functional Specificity of NADP- and NAD-dependent Isocitrate and Isopropylmalate Dehydrogenases. Proteins. 2006 Sep 1;64(4):1001-9. PubMed PMID: 16767773.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Amino acid residues that determine functional specificity of NADP- and NAD-dependent isocitrate and isopropylmalate dehydrogenases. AU - Kalinina,Olga V, AU - Gelfand,Mikhail S, PY - 2006/6/13/pubmed PY - 2006/9/13/medline PY - 2006/6/13/entrez SP - 1001 EP - 9 JF - Proteins JO - Proteins VL - 64 IS - 4 N2 - 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. SN - 1097-0134 UR - https://www.unboundmedicine.com/medline/citation/16767773/Amino_acid_residues_that_determine_functional_specificity_of_NADP__and_NAD_dependent_isocitrate_and_isopropylmalate_dehydrogenases_ L2 - https://doi.org/10.1002/prot.21027 DB - PRIME DP - Unbound Medicine ER -