scholarly journals Esters of Glucose-2-Phosphate: Occurrence and Chemistry

Molecules ◽  
2020 ◽  
Vol 25 (12) ◽  
pp. 2829
Author(s):  
Qiang Zhang ◽  
Si-Zhe Li ◽  
Mohammed Ahmar ◽  
Laurent Soulère ◽  
Yves Queneau
Keyword(s):  
Biocontrol Agent ◽  
Binding Protein ◽  
Building Blocks ◽  
Natural Compounds ◽  
Phosphate Esters ◽  
Agrobacterium Radiobacter ◽  
Periplasmic Binding Protein ◽  
Repressor Protein ◽  
Coupling Methods ◽  
Structural Signature

Phosphodiesters of glucose-2-phosphate (G2P) are found only in few natural compounds such as agrocinopine D and agrocin 84. Agrocinopine D is a G2P phosphodiester produced by plants infected by Agrobacterium fabrum C58 and recognized by the bacterial periplasmic binding protein AccA for being transported into the bacteria before cleavage by the phosphodiesterase AccF, releasing G2P, which promotes virulence by binding the repressor protein AccR. The G2P amide agrocin 84 is a natural antibiotic produced by the non-pathogenic Agrobacterium radiobacter K84 strain used as a biocontrol agent by competing with Agrobacterium fabrum C58. G2P esters are also found in irregular glycogen structures. The rare glucopyranosyl-2-phophoryl moiety found in agrocin 84 is the key structural signature enabling its action as a natural antibiotic. Likewise, G2P and G2P esters can also dupe the Agrobacterium agrocinopine catabolism cascade. Such observations illustrate the importance of G2P esters on which we have recently focused our interest. After a brief review of the reported phosphorylation coupling methods and the choice of carbohydrate building blocks used in G2P chemistry, a flexible access to glucose-2-phosphate esters using the phosphoramidite route is proposed.

scholarly journals Periplasmic binding protein dependent transport system for maltose and maltodextrins: some recent studies

1989 ◽  
Vol 63 (1-2) ◽  
pp. 53-60
Author(s):  
W. Saurin ◽  
E. Francoz ◽  
P. Martineau ◽  
A. Charbit ◽  
E. Dassa ◽  
...  
Keyword(s):  
Transport System ◽  
Binding Protein ◽  
Periplasmic Binding Protein ◽  
Dependent Transport

Detailed analysis of the atrial natriuretic factor receptor hormone-binding domain crystal structure

2001 ◽  
Vol 79 (8) ◽  
pp. 692-704 ◽  
Author(s):  
Focco van den Akker
Keyword(s):  
Crystal Structure ◽  
Atrial Natriuretic Factor ◽  
Binding Protein ◽  
Chloride Ion ◽  
Binding Domain ◽  
Protein Fold ◽  
Hormone Binding ◽  
Periplasmic Binding Protein ◽  
Natriuretic Factor ◽  
Hormone Binding Domain

The X-ray crystal structure of the dimerized atrial natriuretic factor (ANF) receptor hormone-binding domain has provided a first structural view of this anti-hypertensive receptor. The structure reveals a surprising evolutionary link to the periplasmic-binding protein fold family. Furthermore, the presence of a chloride ion in the membrane distal domain and the presence of a second putative effector pocket suggests that the extracellular domain of this receptor is allosterically regulated. The scope of this article is to extensively review the data published on this receptor and to correlate it with the hormone-binding domain structure. In addition, a more detailed description is provided of the important features of this structure including the different binding sites for the ANF hormone, chloride ion, putative effector pocket, glycosylation sites, and dimer interface.Key words: crystal structure, periplasmic-binding protein fold, guanylyl cyclase, hormone receptor.

Study on the mechanism of the BtuF periplasmic-binding protein for vitamin B12

2008 ◽  
Vol 135 (1-3) ◽  
pp. 19-24 ◽  
Author(s):  
Ming Liu ◽  
TingGuang Sun ◽  
JianPing Hu ◽  
WeiZu Chen ◽  
CunXin Wang
Keyword(s):  
Vitamin B12 ◽  
Binding Protein ◽  
Periplasmic Binding Protein

scholarly journals Trapping open and closed forms of FitE-A group III periplasmic binding protein

2009 ◽  
Vol 75 (3) ◽  
pp. 598-609 ◽  
Author(s):  
Rong Shi ◽  
Ariane Proteau ◽  
John Wagner ◽  
Qizhi Cui ◽  
Enrico O. Purisima ◽  
...  
Keyword(s):  
Binding Protein ◽  
Periplasmic Binding Protein ◽  
Group Iii

A Building Block Approach to Monofluorinated Organic Compounds

2008 ◽  
Vol 73 (12) ◽  
pp. 1553-1611 ◽  
Author(s):  
Alexander S. Konev ◽  
Alexander F. Khlebnikov
Keyword(s):  
Organic Compounds ◽  
Building Block ◽  
Building Blocks ◽  
Natural Compounds ◽  
Pericyclic Reactions ◽  
Fluoroacetic Acid ◽  
Phosphorus Containing ◽  
Block Approach

Building blocks for the synthesis of monofluorinated organic compounds are reviewed. The synthetic potential of polyhalomethanes, sulfur- and phosphorus-containing building blocks, difluoroethene, polyhaloethanes, fluoroacetic acid derivatives, and other compounds are described. Pericyclic reactions involving fluorinated compounds and application of the methodology of building blocks to the synthesis of monofluorinated pharmaceuticals and analogs of natural compounds are considered. The review with 317 references covers mainly the literature from 1996 through 2007.

scholarly journals Characterization of a Sinorhizobium melilotiATP-Binding Cassette Histidine Transporter Also Involved in Betaine and Proline Uptake

2000 ◽  
Vol 182 (13) ◽  
pp. 3717-3725 ◽  
Author(s):  
Eric Boncompagni ◽  
Laurence Dupont ◽  
Tam Mignot ◽  
Magne Østeräs ◽  
Annie Lambert ◽  
...  
Keyword(s):  
Glycine Betaine ◽  
Sinorhizobium Meliloti ◽  
Binding Protein ◽  
Compatible Solutes ◽  
Site Directed Mutagenesis ◽  
Uptake System ◽  
Periplasmic Binding Protein ◽  
Gene Encoding ◽  
Inhibition Of Growth

ABSTRACT The symbiotic soil bacterium Sinorhizobium melilotiuses the compatible solutes glycine betaine and proline betaine for both protection against osmotic stress and, at low osmolarities, as an energy source. A PCR strategy based on conserved domains in components of the glycine betaine uptake systems from Escherichia coli(ProU) and Bacillus subtilis (OpuA and OpuC) allowed us to identify a highly homologous ATP-binding cassette (ABC) binding protein-dependent transporter in S. meliloti. This system was encoded by three genes (hutXWV) of an operon which also contained a fourth gene (hutH2) encoding a putative histidase, which is an enzyme involved in the first step of histidine catabolism. Site-directed mutagenesis of the gene encoding the periplasmic binding protein (hutX) and of the gene encoding the cytoplasmic ATPase (hutV) was done to study the substrate specificity of this transporter and its contribution in betaine uptake. These mutants showed a 50% reduction in high-affinity uptake of histidine, proline, and proline betaine and about a 30% reduction in low-affinity glycine betaine transport. When histidine was used as a nitrogen source, a 30% inhibition of growth was observed inhut mutants (hutX and hutH2). Expression analysis of the hut operon determined using ahutX-lacZ fusion revealed induction by histidine, but not by salt stress, suggesting this uptake system has a catabolic role rather than being involved in osmoprotection. To our knowledge, Hut is the first characterized histidine ABC transporter also involved in proline and betaine uptake.

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