2024-03-29T05:21:25Z
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2021-12-31T03:51:46Z
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Crystallization of 3-hexulose-6-phosphate synthase
Delfi, Masoud
Mahdavian, Leila
Sattarifar, Mohammad
Hakulinen, Nina
Rouvinen, Juha
Protein crystallization
Formaldehyde fixation
Methylotrophic bacteria
Methylomonas aminofaciens 77a
3-Hexulose-6-phosphate synthase
Ribulose monophosphate pathway
The crystal structures can reveal detailed information about the overall structure, active site structure, and functional mechanism of enzymes. This study focused on the crystallization of 3-hexulose-6-phosphate synthase from Methylomonas aminofaciens 77a, to produce higher resolution crystals for precise structural characterization. 3-Hexulose-6-phosphate synthase is from Methylomonas aminofaciens 77a (EC 4.1.2.43). It belongs to the orotidine 5'-monophosphate decarboxylase superfamily, and acts as a key enzyme for a ribulose-monophosphate cycle of formaldehyde fixation and detoxification. 3-Hexulose-6-phosphate synthase catalyzes the aldol condensation of formaldehyde with D-ribulose-5-phosphate. For the maximum activity, 3-hexulose-6-phosphate synthase requires Mg2+ or Mn2+ as ligands. MaHPS crystallized at the concentration of 7 mg/mL and conditions consisting of 0.2 M MgCl2, 18% PEG 3350 at pH = 7.0.
Atlanta Publishing House LLC
2021-09-30
info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
application/pdf
https://www.eurjchem.com/index.php/eurjchem/article/view/2072
10.5155/eurjchem.12.3.299-303.2072
European Journal of Chemistry; Vol. 12 No. 3 (2021): September 2021; 299-303
2153-2257
2153-2249
eng
https://www.eurjchem.com/index.php/eurjchem/article/view/2072/pdf_2072
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