Molecules and Cells

Cited by CrossRef (10)

  1. . Polyamines in Fungi. .
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  2. Lilian González-Segura, Héctor Riveros-Rosas, Adriana Julián-Sánchez, Rosario A. Muñoz-Clares. Residues that influence coenzyme preference in the aldehyde dehydrogenases. Chemico-Biological Interactions 2015;234:59
    https://doi.org/10.1016/j.cbi.2014.12.039
  3. Congcong Xie, Zhi-Min Li, Fumei Bai, Ziwei Hu, Wei Zhang, Zhimin Li, Concepción Gonzalez-Bello. Kinetic and structural insights into enzymatic mechanism of succinic semialdehyde dehydrogenase from Cyanothece sp. ATCC51142. PLoS ONE 2020;15:e0239372
    https://doi.org/10.1371/journal.pone.0239372
  4. Eun Hyuk Jang, Seong Ah Park, Young Min Chi, Ki Seog Lee. Structural insight into the substrate inhibition mechanism of NADP+-dependent succinic semialdehyde dehydrogenase from Streptococcus pyogenes. Biochemical and Biophysical Research Communications 2015;461:487
    https://doi.org/10.1016/j.bbrc.2015.04.047
  5. Martina Kopečná, Armelle Vigouroux, Jan Vilím, Radka Končitíková, Pierre Briozzo, Eva Hájková, Lenka Jašková, Klaus von Schwartzenberg, Marek Šebela, Solange Moréra, David Kopečný. The ALDH21 gene found in lower plants and some vascular plants codes for a NADP+ -dependent succinic semialdehyde dehydrogenase. Plant J 2017;92:229
    https://doi.org/10.1111/tpj.13648
  6. Xiaoqin Wang, Chongde Lai, Guofeng Lei, Fei Wang, Haozhi Long, Xiaoyu Wu, Jinyin Chen, Guanghua Huo, Zhimin Li. Kinetic characterization and structural modeling of an NADP+-dependent succinic semialdehyde dehydrogenase from Anabaena sp. PCC7120. International Journal of Biological Macromolecules 2018;108:615
    https://doi.org/10.1016/j.ijbiomac.2017.12.059
  7. Shoki Ito, Takashi Osanai. Unconventional biochemical regulation of the oxidative pentose phosphate pathway in the model cyanobacterium Synechocystis sp. PCC 6803. 2020;477:1309
    https://doi.org/10.1042/BCJ20200038
  8. Jittima Phonbuppha, Somchart Maenpuen, Pobthum Munkajohnpong, Pimchai Chaiyen, Ruchanok Tinikul. Selective determination of the catalytic cysteinepKaof two‐cysteine succinic semialdehyde dehydrogenase fromAcinetobacter baumanniiusing burst kinetics and enzyme adduct formation. FEBS J 2018;285:2504
    https://doi.org/10.1111/febs.14497
  9. Jing Zhang, Yongjun Liu. A QM/MM study of the catalytic mechanism of succinic semialdehyde dehydrogenase from Synechococcus sp. PCC 7002 and Salmonella typhimurium. RSC Adv. 2015;5:101672
    https://doi.org/10.1039/C5RA21535H
  10. Tanakan Paladkong, Panu Pimviriyakul, Jittima Phonbuppha, Somchart Maenpuen, Pimchai Chaiyen, Ruchanok Tinikul. Mechanistic roles of the neighbouring cysteine in enhancing nucleophilicity of catalytic residue in a two‐cysteine succinic semialdehyde dehydrogenase. The FEBS Journal 2022
    https://doi.org/10.1111/febs.16640