scholarly journals PHOSPHOMANNOSE ISOMERASE

1950 ◽  
Vol 186 (2) ◽  
pp. 753-761 ◽  
Author(s):  
Milton W. Slein
2007 ◽  
Vol 353 (1) ◽  
pp. 200-206 ◽  
Author(s):  
Sílvia A. Sousa ◽  
Leonilde M. Moreira ◽  
Julia Wopperer ◽  
Leo Eberl ◽  
Isabel Sá-Correia ◽  
...  

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Susumu Mochizuki ◽  
Takeshi Fukumoto ◽  
Toshiaki Ohara ◽  
Kouhei Ohtani ◽  
Akihide Yoshihara ◽  
...  

AbstractThe rare sugar d-tagatose is a safe natural product used as a commercial food ingredient. Here, we show that d-tagatose controls a wide range of plant diseases and focus on downy mildews to analyze its mode of action. It likely acts directly on the pathogen, rather than as a plant defense activator. Synthesis of mannan and related products of d-mannose metabolism are essential for development of fungi and oomycetes; d-tagatose inhibits the first step of mannose metabolism, the phosphorylation of d-fructose to d-fructose 6-phosphate by fructokinase, and also produces d-tagatose 6-phosphate. d-Tagatose 6-phosphate sequentially inhibits phosphomannose isomerase, causing a reduction in d-glucose 6-phosphate and d-fructose 6-phosphate, common substrates for glycolysis, and in d-mannose 6-phosphate, needed to synthesize mannan and related products. These chain-inhibitory effects on metabolic steps are significant enough to block initial infection and structural development needed for reproduction such as conidiophore and conidiospore formation of downy mildew.


1991 ◽  
Vol 173 (6) ◽  
pp. 2006-2010 ◽  
Author(s):  
M A Payton ◽  
M Rheinnecker ◽  
L S Klig ◽  
M DeTiani ◽  
E Bowden

1996 ◽  
Vol 318 (2) ◽  
pp. 437-442 ◽  
Author(s):  
Amanda E. I. PROUDFOOT ◽  
Laurence GOFFIN ◽  
Mark A PAYTON ◽  
Timothy N. C. WELLS ◽  
Alain R BERNARD

Phosphomannose isomerase (PMI) catalyses the interconversion of mannose 6-phosphate and fructose 6-phosphate in prokaryotic and eukaryotic cells. The enzyme is a metalloenzyme which contains 1 mol of zinc per mol of enzyme. Heterologous expression of the cDNA coding for the Candida albicans enzyme in the prokaryotic host Escherichia coli results in an expression level of up to 30% of total E. coli protein. Ten percent of recombinant PMI is expressed in the soluble fraction and 90% in inclusion bodies. Inclusion of a high level of zinc in the fermentation medium resulted in a fourfold increase in soluble protein. Co-expression of the bacterial chaperones, GroES and GroEL, resulted in a proportional twofold increase in soluble PMI while causing an overall decrease in the PMI expression level. Folding denatured PMI in vitro required reductant and zinc ions. The yield of renatured protein was increased by folding in the presence of GroEL and DnaK in an ATP-independent manner. The refolding yield of denatured soluble enzyme from a guanidine solution was threefold higher than that of folding monomerized inclusion body protein solubilized in guanidine hydrochloride. This suggests that a proportion of recombinant protein expressed in E. coli inclusion bodies may be irreversibly denatured.


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