

Crystallization of 3-hexulose-6-phosphate synthase
Masoud Delfi (1)





(1) Department of Chemistry, University of Eastern Finland, Joensuu Campus, Joensuu, FIN-80101 Finland
(2) Department of Chemistry, Doroud Branch, Islamic Azad University, P.O. Box: 133. Doroud. Iran
(3) Department of Chemistry, Doroud Branch, Islamic Azad University, P.O. Box: 133. Doroud. Iran
(4) Department of Chemistry, University of Eastern Finland, Joensuu Campus, Joensuu, FIN-80101 Finland
(5) Department of Chemistry, University of Eastern Finland, Joensuu Campus, Joensuu, FIN-80101 Finland
(*) Corresponding Author
Received: 18 Jan 2021 | Revised: 18 Jun 2021 | Accepted: 15 Jul 2021 | Published: 30 Sep 2021 | Issue Date: September 2021
Abstract
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.
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DOI: 10.5155/eurjchem.12.3.299-303.2072
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Department of Chemistry, University of Eastern Finland, Joensuu Campus, Joensuu, FIN-80101 Finland.
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DOI Link: https://doi.org/10.5155/eurjchem.12.3.299-303.2072

















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