Molecules and Cells

  • 제37권10호
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  • Pages.719-726
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  • 2014
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  • 1016-8478(pISSN)
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  • 0219-1032(eISSN)
한국분자세포생물학회 (Korean Society for Molecular and Cellular Biology)
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Kinetic and Structural Characterization for Cofactor Preference of Succinic Semialdehyde Dehydrogenase from Streptococcus pyogenes

  • Jang, Eun Hyuk (Department of Biosystems and Biotechnology, College of Life Sciences and Biotechnology, Korea University) ;
  • Park, Seong Ah (Department of Clinical Laboratory Science, College of Health Sciences, Catholic University of Pusan) ;
  • Chi, Young Min (Department of Biosystems and Biotechnology, College of Life Sciences and Biotechnology, Korea University) ;
  • Lee, Ki Seog (Department of Clinical Laboratory Science, College of Health Sciences, Catholic University of Pusan)
  • 투고 : 2014.06.10
  • 심사 : 2014.09.02
  • 발행 : 2014.10.31
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초록

The ${\gamma}$-Aminobutyric acid (GABA) that is found in prokaryotic and eukaryotic organisms has been used in various ways as a signaling molecule or a significant component generating metabolic energy under conditions of nutrient limitation or stress, through GABA catabolism. Succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde to succinic acid in the final step of GABA catabolism. Here, we report the catalytic properties and two crystal structures of SSADH from Streptococcus pyogenes (SpSSADH) regarding its cofactor preference. Kinetic analysis showed that SpSSADH prefers $NADP^+$ over $NAD^+$ as a hydride acceptor. Moreover, the structures of SpSSADH were determined in an apo-form and in a binary complex with $NADP^+$ at $1.6{\AA}$ and $2.1{\AA}$ resolutions, respectively. Both structures of SpSSADH showed dimeric conformation, containing a single cysteine residue in the catalytic loop of each subunit. Further structural analysis and sequence comparison of SpSSADH with other SSADHs revealed that Ser158 and Tyr188 in SpSSADH participate in the stabilization of the 2'-phosphate group of adenine-side ribose in $NADP^+$. Our results provide structural insights into the cofactor preference of SpSSADH as the gram-positive bacterial SSADH.

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참고문헌

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  1. Residues that influence coenzyme preference in the aldehyde dehydrogenases vol.234, 2015, https://doi.org/10.1016/j.cbi.2014.12.039
  2. Structural insight into the substrate inhibition mechanism of NADP+-dependent succinic semialdehyde dehydrogenase from Streptococcus pyogenes vol.461, pp.3, 2015, https://doi.org/10.1016/j.bbrc.2015.04.047
  3. The ALDH21 gene found in lower plants and some vascular plants codes for a NADP+ -dependent succinic semialdehyde dehydrogenase 2017, https://doi.org/10.1111/tpj.13648
  4. A QM/MM study of the catalytic mechanism of succinic semialdehyde dehydrogenase from Synechococcus sp. PCC 7002 and Salmonella typhimurium vol.5, pp.123, 2015, https://doi.org/10.1039/C5RA21535H
  5. using burst kinetics and enzyme adduct formation vol.285, pp.13, 2018, https://doi.org/10.1111/febs.14497
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  7. Kinetic and structural insights into enzymatic mechanism of succinic semialdehyde dehydrogenase from Cyanothece sp. ATCC51142 vol.15, pp.9, 2020, https://doi.org/10.1371/journal.pone.0239372