The Rhizobium leguminosarum bv. trifolii pssB gene product is an inositol monophosphatase that influences exopolysaccharide synthesis

2001 ◽  
Vol 175 (2) ◽  
pp. 143-151 ◽  
Author(s):  
Monika Janczarek ◽  
Anna Skorupska
1990 ◽  
Vol 172 (9) ◽  
pp. 5486-5489 ◽  
Author(s):  
H R Schlaman ◽  
R J Okker ◽  
B J Lugtenberg

1989 ◽  
Vol 171 (9) ◽  
pp. 4686-4693 ◽  
Author(s):  
H R Schlaman ◽  
H P Spaink ◽  
R J Okker ◽  
B J Lugtenberg

1998 ◽  
Vol 64 (7) ◽  
pp. 2609-2615 ◽  
Author(s):  
Liangjing Chen ◽  
Mary F. Roberts

ABSTRACT Inositol monophosphatase (EC 3.1.3.25 ) plays a pivotal role in the biosynthesis of di-myo-inositol-1,1′-phosphate, an osmolyte found in hyperthermophilic archaea. Given the sequence homology between the MJ109 gene product of Methanococcus jannaschii and human inositol monophosphatase, the MJ109 gene was cloned and expressed in Escherichia coli and examined for inositol monophosphatase activity. The purified MJ109 gene product showed inositol monophosphatase activity with kinetic parameters (Km = 0.091 ± 0.016 mM;V max = 9.3 ± 0.45 μmol of Pi min−1 mg of protein−1) comparable to those of mammalian and E. coli enzymes. Its substrate specificity, Mg2+ requirement, Li+inhibition, subunit association (dimerization), and heat stability were studied and compared to those of other inositol monophosphatases. The lack of inhibition by low concentrations of Li+ and high concentrations of Mg2+ and the high rates of hydrolysis of glucose-1-phosphate and p-nitrophenylphosphate are the most pronounced differences between the archaeal inositol monophosphatase and those from other sources. The possible causes of these kinetic differences are discussed, based on the active site sequence alignment between M. jannaschii and human inositol monophosphatase and the crystal structure of the mammalian enzyme.


1999 ◽  
Vol 12 (11) ◽  
pp. 994-999 ◽  
Author(s):  
Kay H. Yeoman ◽  
Alex G. May ◽  
Nicola G. deLuca ◽  
Daniel B. Stuckey ◽  
Andrew W. B. Johnston

A cloned Rhizobium leguminosarum gene, termed rpoI, when transferred to wild-type strains, caused overproduction of the siderophore vicibactin. An rpoI mutant was defective in Fe uptake but was unaffected in symbiotic N2 fixation. The RpoI gene product was similar in sequence to extra-cytoplasmic σ factors of RNA polymerase. Transcription of rpoI was reduced in cells grown in medium that was replete with Fe.


1995 ◽  
Vol 177 (1) ◽  
pp. 200-205 ◽  
Author(s):  
A Matsuhisa ◽  
N Suzuki ◽  
T Noda ◽  
K Shiba

2006 ◽  
Vol 339 (3) ◽  
pp. 897-904 ◽  
Author(s):  
Xiaoling Gu ◽  
Mao Chen ◽  
Hongbo Shen ◽  
Xin Jiang ◽  
Yishu Huang ◽  
...  

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