European Journal of Chemistry 2021, 12(3), 299-303 | doi: https://doi.org/10.5155/eurjchem.12.3.299-303.2072 | Get rights and content

Issue cover




Crossmark

  Open Access OPEN ACCESS | Open Access PEER-REVIEWED | RESEARCH ARTICLE | DOWNLOAD PDF | VIEW FULL-TEXT PDF | TOTAL VIEWS

Crystallization of 3-hexulose-6-phosphate synthase


Masoud Delfi (1) orcid , Leila Mahdavian (2,*) orcid , Mohammad Sattarifar (3) orcid , Nina Hakulinen (4) orcid , Juha Rouvinen (5) orcid

(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.


Announcements


One of our sponsors will cover the article processing fee for all submissions made between May 17, 2023 and May 31, 2023 (Voucher code: SPONSOR2023).

Editor-in-Chief
European Journal of Chemistry

Keywords


Protein crystallization; Formaldehyde fixation; Methylotrophic bacteria; Methylomonas aminofaciens 77a; 3-Hexulose-6-phosphate synthase; Ribulose monophosphate pathway

Full Text:

PDF
PDF    Open Access

DOI: 10.5155/eurjchem.12.3.299-303.2072

Links for Article


| | | | | | |

| | | | | | |

| | | |

Related Articles




Article Metrics

icon graph This Abstract was viewed 328 times | icon graph PDF Article downloaded 111 times

Funding information


Department of Chemistry, University of Eastern Finland, Joensuu Campus, Joensuu, FIN-80101 Finland.

References


[1]. Stolzenberger, J.; Lindner, S. N.; Wendisch, V. F. Microbiology 2013, 159 (Pt 8), 1770-1781.
https://doi.org/10.1099/mic.0.067314-0

[2]. Kato, N.; Yurimoto, H.; Thauer, R. K. Biosci. Biotechnol. Biochem. 2006, 70 (1), 10-21.
https://doi.org/10.1271/bbb.70.10

[3]. Zhang, W.; Zhang, T.; Wu, S.; Wu, M.; Xin, F.; Dong, W.; Ma, J.; Zhang, M.; Jiang, M. RSC Adv. 2017, 7 (7), 4083-4091.
https://doi.org/10.1039/C6RA27038G

[4]. Park, Y.; Yoo, H.; Song, M.; Lee, D.-H.; Lee, S. Catalysts 2018, 8 (12), 582.
https://doi.org/10.3390/catal8120582

[5]. Orita, I.; Kita, A.; Yurimoto, H.; Kato, N.; Sakai, Y.; Miki, K. Proteins 2010, 78 (16), 3488-3492.
https://doi.org/10.1002/prot.22860

[6]. Rahman, M. M.; Andberg, M.; Koivula, A.; Rouvinen, J.; Hakulinen, N. Sci. Rep. 2018, 8 (1), 865.
https://doi.org/10.1038/s41598-018-19192-6

[7]. Witthoff, S.; Schmitz, K.; Niedenführ, S.; Nöh, K.; Noack, S.; Bott, M.; Marienhagen, J. Appl. Environ. Microbiol. 2015, 81 (6), 2215-2225.
https://doi.org/10.1128/AEM.03110-14

[8]. Lee, J. C.; Herman, P. Methods Enzymol. 2011, 488, 185-217.
https://doi.org/10.1016/B978-0-12-381268-1.00008-2

[9]. Kato, N.; Ohashi, H.; Hori, T.; Tani, Y.; Ogata, K. Agric. Biol. Chem. 1977, 41 (7), 1133-1140.
https://doi.org/10.1271/bbb1961.41.1133

[10]. Khurshid, S.; Saridakis, E.; Govada, L.; Chayen, N. E. Nat. Protoc. 2014, 9 (7), 1621-1633.
https://doi.org/10.1038/nprot.2014.109

[11]. Price, J. V.; Chen, L.; Whitaker, W. B.; Papoutsakis, E.; Chen, W. Proc. Natl. Acad. Sci. U. S. A. 2016, 113 (45), 12691-12696.
https://doi.org/10.1073/pnas.1601797113

[12]. Yew, W. S.; Wise, E. L.; Rayment, I.; Gerlt, J. A. Biochemistry 2004, 43 (21), 6427-6437.
https://doi.org/10.1021/bi049741t

[13]. Wise, E.; Yew, W. S.; Babbitt, P. C.; Gerlt, J. A.; Rayment, I. Biochemistry 2002, 41 (12), 3861-3869.
https://doi.org/10.1021/bi012174e

[14]. Yew, W. S.; Akana, J.; Wise, E. L.; Rayment, I.; Gerlt, J. A. Biochemistry 2005, 44 (6), 1807-1815.
https://doi.org/10.1021/bi047815v


How to cite


Delfi, M.; Mahdavian, L.; Sattarifar, M.; Hakulinen, N.; Rouvinen, J. Eur. J. Chem. 2021, 12(3), 299-303. doi:10.5155/eurjchem.12.3.299-303.2072
Delfi, M.; Mahdavian, L.; Sattarifar, M.; Hakulinen, N.; Rouvinen, J. Crystallization of 3-hexulose-6-phosphate synthase. Eur. J. Chem. 2021, 12(3), 299-303. doi:10.5155/eurjchem.12.3.299-303.2072
Delfi, M., Mahdavian, L., Sattarifar, M., Hakulinen, N., & Rouvinen, J. (2021). Crystallization of 3-hexulose-6-phosphate synthase. European Journal of Chemistry, 12(3), 299-303. doi:10.5155/eurjchem.12.3.299-303.2072
Delfi, Masoud, Leila Mahdavian, Mohammad Sattarifar, Nina Hakulinen, & Juha Rouvinen. "Crystallization of 3-hexulose-6-phosphate synthase." European Journal of Chemistry [Online], 12.3 (2021): 299-303. Web. 29 May. 2023
Delfi, Masoud, Mahdavian, Leila, Sattarifar, Mohammad, Hakulinen, Nina, AND Rouvinen, Juha. "Crystallization of 3-hexulose-6-phosphate synthase" European Journal of Chemistry [Online], Volume 12 Number 3 (30 September 2021)

The other citation formats (EndNote | Reference Manager | ProCite | BibTeX | RefWorks) for this article can be found online at: How to cite item



DOI Link: https://doi.org/10.5155/eurjchem.12.3.299-303.2072


CrossRef | Scilit | GrowKudos | Researchgate | Publons | ScienceGate | Scite | Lens | OUCI

WorldCat Paperbuzz | LibKey Citeas | Dimensions | Semanticscholar | Plumx | Kopernio | Zotero | Mendeley

ZoteroSave to Zotero MendeleySave to Mendeley



European Journal of Chemistry 2021, 12(3), 299-303 | doi: https://doi.org/10.5155/eurjchem.12.3.299-303.2072 | Get rights and content

Refbacks

  • There are currently no refbacks.




Copyright (c) 2021 Authors

Creative Commons License
This work is published and licensed by Atlanta Publishing House LLC, Atlanta, GA, USA. The full terms of this license are available at http://www.eurjchem.com/index.php/eurjchem/pages/view/terms and incorporate the Creative Commons Attribution-Non Commercial (CC BY NC) (International, v4.0) License (http://creativecommons.org/licenses/by-nc/4.0). By accessing the work, you hereby accept the Terms. This is an open access article distributed under the terms and conditions of the CC BY NC License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited without any further permission from Atlanta Publishing House LLC (European Journal of Chemistry). No use, distribution or reproduction is permitted which does not comply with these terms. Permissions for commercial use of this work beyond the scope of the License (http://www.eurjchem.com/index.php/eurjchem/pages/view/terms) are administered by Atlanta Publishing House LLC (European Journal of Chemistry).



© Copyright 2010 - 2023  Atlanta Publishing House LLC All Right Reserved.

The opinions expressed in all articles published in European Journal of Chemistry are those of the specific author(s), and do not necessarily reflect the views of Atlanta Publishing House LLC, or European Journal of Chemistry, or any of its employees.

Copyright 2010-2023 Atlanta Publishing House LLC. All rights reserved. This site is owned and operated by Atlanta Publishing House LLC whose registered office is 2850 Smith Ridge Trce Peachtree Cor GA 30071-2636, USA. Registered in USA.