European Journal of Chemistry

Crystallization of 3-hexulose-6-phosphate synthase

Crossmark


Main Article Content

Masoud Delfi
Leila Mahdavian
Mohammad Sattarifar
Nina Hakulinen
Juha Rouvinen

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.


icon graph This Abstract was viewed 427 times | icon graph Article PDF downloaded 161 times

How to Cite
(1)
Delfi, M.; Mahdavian, L.; Sattarifar, M.; Hakulinen, N.; Rouvinen, J. Crystallization of 3-Hexulose-6-Phosphate Synthase. Eur. J. Chem. 2021, 12, 299-303.

Article Details

Share
Crossref - Scopus - Google - European PMC
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

Most read articles by the same author(s)
TrendMD

Dimensions - Altmetric - scite_ - PlumX

Downloads and views

Downloads

Download data is not yet available.

Metrics

Metrics Loading ...
License Terms

License Terms

by-nc

Copyright © 2024 by Authors. This work is published and licensed by Atlanta Publishing House LLC, Atlanta, GA, USA. The full terms of this license are available at https://www.eurjchem.com/index.php/eurjchem/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 (https://www.eurjchem.com/index.php/eurjchem/terms) are administered by Atlanta Publishing House LLC (European Journal of Chemistry).