This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fernandes, C.
Right arrow Articles by da Costa, M. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fernandes, C.
Right arrow Articles by da Costa, M. S.

 Previous Article  |  Next Article 

Journal of Bacteriology, June 2007, p. 4014-4019, Vol. 189, No. 11
0021-9193/07/$08.00+0     doi:10.1128/JB.00075-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Single-Step Pathway for Synthesis of Glucosylglycerate in Persephonella marina{triangledown}

Chantal Fernandes,1 Nuno Empadinhas,1 and Milton S. da Costa2*

Centro de Neurociências e Biologia Celular, Universidade de Coimbra, 3004-517 Coimbra, Portugal,1 Departamento de Bioquímica, Universidade de Coimbra, 3001-401 Coimbra, Portugal2

Received 15 January 2007/ Accepted 9 March 2007

A single-step pathway for the synthesis of the compatible solute glucosylglycerate (GG) is proposed based on the activity of a recombinant glucosylglycerate synthase (Ggs) from Persephonella marina. The corresponding gene encoded a putative glycosyltransferase that was part of an operon-like structure which also contained the genes for glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP), the enzymes that lead to the synthesis of GG through the formation of glucosyl-3-phosphoglycerate. The putative glucosyltransferase gene was expressed in Escherichia coli, and the recombinant product catalyzed the synthesis of GG in one step from ADP-glucose and D-glycerate, with Km values at 70°C of 1.5 and 2.2 mM, respectively. This glucosylglycerate synthase (Ggs) was also able to use GDP- and UDP-glucose as donors to form GG, but the efficiencies were lower. Maximal activity was observed at temperatures between 80 and 85°C, and Mg2+ or Ca2+ was required for catalysis. Ggs activity was maximal and remained nearly constant at pH values between 5.5 and pH 8.0, and the half-lives for inactivation were 74 h at 85°C and 8 min at 100°C. This is the first report of an enzyme catalyzing the synthesis of GG in one step and of the existence of two pathways for GG synthesis in the same organism.

* Corresponding author. Mailing address: Departamento de Bioquímica, Universidade de Coimbra, 3001-401 Coimbra, Portugal. Phone: 351-239824024. Fax: 351-239855789. E-mail: milton{at}ci.uc.pt

{triangledown} Published ahead of print on 16 March 2007.

Journal of Bacteriology, June 2007, p. 4014-4019, Vol. 189, No. 11
0021-9193/07/$08.00+0     doi:10.1128/JB.00075-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Jackson, M., Brennan, P. J. (2009). Polymethylated Polysaccharides from Mycobacterium Species Revisited. J. Biol. Chem. 284: 1949-1953 [Abstract] [Full Text]  
  • Nobre, A., Alarico, S., Fernandes, C., Empadinhas, N., da Costa, M. S. (2008). A Unique Combination of Genetic Systems for the Synthesis of Trehalose in Rubrobacter xylanophilus: Properties of a Rare Actinobacterial TreT. J. Bacteriol. 190: 7939-7946 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»