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Characterization of two β-decarboxylating dehydrogenases from Sulfolobus acidocaldarius.
Extremophiles. 2016 Nov; 20(6):843-853.E

Abstract

Sulfolobus acidocaldarius, a hyperthermoacidophilic archaeon, possesses two β-decarboxylating dehydrogenase genes, saci_0600 and saci_2375, in its genome, which suggests that it uses these enzymes for three similar reactions in lysine biosynthesis through 2-aminoadipate, leucine biosynthesis, and the tricarboxylic acid cycle. To elucidate their roles, these two genes were expressed in Escherichia coli in the present study and their gene products were characterized. Saci_0600 recognized 3-isopropylmalate as a substrate, but exhibited slight and no activity for homoisocitrate and isocitrate, respectively. Saci_2375 exhibited distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. These results suggest that Saci_0600 is a 3-isopropylmalate dehydrogenase for leucine biosynthesis and Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase. The crystal structure of Saci_0600 was determined as a closed-form complex that binds 3-isopropylmalate and Mg2+, thereby revealing the structural basis for the extreme thermostability and novel-type recognition of the 3-isopropyl moiety of the substrate.

Authors+Show Affiliations

Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.Max Planck Institute for Terrestrial Microbiology, Marburg, Germany. Molecular Biology of Archaea, Institute of Biology II, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.Max Planck Institute for Terrestrial Microbiology, Marburg, Germany. Molecular Biology of Archaea, Institute of Biology II, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan. umanis@mail.ecc.u-tokyo.ac.jp.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

27590116

Citation

Takahashi, Kento, et al. "Characterization of Two Β-decarboxylating Dehydrogenases From Sulfolobus Acidocaldarius." Extremophiles : Life Under Extreme Conditions, vol. 20, no. 6, 2016, pp. 843-853.
Takahashi K, Nakanishi F, Tomita T, et al. Characterization of two β-decarboxylating dehydrogenases from Sulfolobus acidocaldarius. Extremophiles. 2016;20(6):843-853.
Takahashi, K., Nakanishi, F., Tomita, T., Akiyama, N., Lassak, K., Albers, S. V., Kuzuyama, T., & Nishiyama, M. (2016). Characterization of two β-decarboxylating dehydrogenases from Sulfolobus acidocaldarius. Extremophiles : Life Under Extreme Conditions, 20(6), 843-853.
Takahashi K, et al. Characterization of Two Β-decarboxylating Dehydrogenases From Sulfolobus Acidocaldarius. Extremophiles. 2016;20(6):843-853. PubMed PMID: 27590116.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of two β-decarboxylating dehydrogenases from Sulfolobus acidocaldarius. AU - Takahashi,Kento, AU - Nakanishi,Fumika, AU - Tomita,Takeo, AU - Akiyama,Nagisa, AU - Lassak,Kerstin, AU - Albers,Sonja-Verena, AU - Kuzuyama,Tomohisa, AU - Nishiyama,Makoto, Y1 - 2016/09/02/ PY - 2016/02/02/received PY - 2016/08/25/accepted PY - 2016/11/1/pubmed PY - 2017/2/24/medline PY - 2016/9/4/entrez KW - 3-Isopropylmalate dehydrogenase KW - Crystal structure KW - Homoisocitrate dehydrogenase KW - Isocitrate dehydrogenase KW - Sulfolobus acidocaldarius KW - β-Decarboxylating dehydrogenase SP - 843 EP - 853 JF - Extremophiles : life under extreme conditions JO - Extremophiles VL - 20 IS - 6 N2 - Sulfolobus acidocaldarius, a hyperthermoacidophilic archaeon, possesses two β-decarboxylating dehydrogenase genes, saci_0600 and saci_2375, in its genome, which suggests that it uses these enzymes for three similar reactions in lysine biosynthesis through 2-aminoadipate, leucine biosynthesis, and the tricarboxylic acid cycle. To elucidate their roles, these two genes were expressed in Escherichia coli in the present study and their gene products were characterized. Saci_0600 recognized 3-isopropylmalate as a substrate, but exhibited slight and no activity for homoisocitrate and isocitrate, respectively. Saci_2375 exhibited distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. These results suggest that Saci_0600 is a 3-isopropylmalate dehydrogenase for leucine biosynthesis and Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase. The crystal structure of Saci_0600 was determined as a closed-form complex that binds 3-isopropylmalate and Mg2+, thereby revealing the structural basis for the extreme thermostability and novel-type recognition of the 3-isopropyl moiety of the substrate. SN - 1433-4909 UR - https://www.unboundmedicine.com/medline/citation/27590116/Characterization_of_two_β_decarboxylating_dehydrogenases_from_Sulfolobus_acidocaldarius_ L2 - https://dx.doi.org/10.1007/s00792-016-0872-4 DB - PRIME DP - Unbound Medicine ER -