Synthesis of photoaffinity probes [2′-iodo-4′-(3′′-trifluoromethyldiazirinyl)phenoxy]-d-glucopyranoside and [(4′-benzoyl)phenoxy]-d-glucopyranoside for the identification of sugar-binding and phlorizin-binding sites in the sodium/d-glucose cotransporter protein

2003 ◽  
Vol 323 (1) ◽  
pp. 74-83 ◽  
Author(s):  
Navneet Kumar Tyagi ◽  
Rolf K.H Kinne
2004 ◽  
Vol 23 (10) ◽  
pp. 2019-2028 ◽  
Author(s):  
Linda J Olson ◽  
Rama D Yammani ◽  
Nancy M Dahms ◽  
Jung-Ja P Kim

Biochemistry ◽  
2000 ◽  
Vol 39 (15) ◽  
pp. 4493-4499 ◽  
Author(s):  
Emmanuelle Cordat ◽  
Gérard Leblanc ◽  
Isabelle Mus-Veteau
Keyword(s):  

2013 ◽  
Vol 9 ◽  
pp. P151-P151
Author(s):  
Doug Johnson ◽  
Kelly Bales ◽  
Nikolay Pozdnyakov ◽  
Heather Murrey ◽  
Martin Pettersson ◽  
...  

1993 ◽  
Vol 294 (3) ◽  
pp. 753-760 ◽  
Author(s):  
C A Colville ◽  
M J Seatter ◽  
G W Gould

We have expressed the liver (GLUT 2), brain (GLUT 3) and insulin-responsive (GLUT 4) glucose transporters in oocytes from Xenopus laevis by microinjection of in vitro-transcribed mRNA. Using a range of halogeno- and deoxy-glucose analogues, and other hexoses, we have studied the structural basis of sugar binding to these different isoforms. We show that a hydrogen bond to the C-3 position is involved in sugar binding for all three isoforms, but that the direction of this hydrogen bond is different in GLUT 2 from either GLUT 1, 3 or 4. Hydrogen-bonding at the C-4 position is also involved in sugar recognition by all three isoforms, but we propose that in GLUT 3 this hydrogen bond plays a less significant role than in GLUT 2 and 4. In all transporters we propose that the C-4 position is directed out of the sugar-binding pocket. The role of the C-6 position is also discussed. In addition, we have analysed the ability of fructopyranose and fructofuranose analogues to inhibit the transport mediated by GLUT2. We show that fructofuranose analogues, but not fructopyranose analogues, are efficient inhibitors of transport mediated by GLUT 2, and therefore suggest that GLUT 2 accommodates D-glucose as a pyranose ring, but D-fructose as a furanose ring. Models for the binding sites of GLUT 2, 3 and 4 are presented.


1985 ◽  
Vol 55 (1-2) ◽  
pp. 15-20 ◽  
Author(s):  
J. Hubert ◽  
A. P. Seve ◽  
D. Bouvier ◽  
C. Masson ◽  
M. Bouteille ◽  
...  

Biochemistry ◽  
1995 ◽  
Vol 34 (47) ◽  
pp. 15395-15406 ◽  
Author(s):  
Erin K. Cloherty ◽  
Lisa A. Sultzman ◽  
Ralph J. Zottola ◽  
Anthony Carruthers

Author(s):  
Xiaojie Yao ◽  
Rebecca Mauldin ◽  
Larry Byers
Keyword(s):  

1999 ◽  
Vol 181 (13) ◽  
pp. 3949-3955 ◽  
Author(s):  
Eva Karpati ◽  
Peter Kiss ◽  
Tamas Ponyi ◽  
Istvan Fendrik ◽  
Miklos de Zamaroczy ◽  
...  

ABSTRACT In vitro, the nitrogen fixation capability of A. lipoferum is efficiently increased in the presence of wheat germ agglutinin (WGA). A putative WGA-binding receptor, a 32-kDa protein, was detected in the cell capsule. The stimulatory effect requiredN-acetyl-d-glucosamine dimer (GlcNAcdi) terminated sugar side chains of the receptor and was dependent on the number of GlcNAcdi links involved in receptor-WGA interface. Binding to the primary sugar binding sites on WGA had a larger stimulatory effect than binding to the secondary sites. The WGA-receptor complex generated stimulus led to elevated transcription of the nifH and nifA genes and of the glnBA gene cluster but not of the glnA gene from its own promoter. There may well be a signalling cascade contributing to the regulation of nitrogen fixation.


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