scholarly journals Mapping of Bacillus subtilis riboflavin operon fragment coding for 3,4-dihydroxy-2-butanone-4-phosphate synthase

1996 ◽  
Vol 12 (1) ◽  
pp. 64-68
Author(s):  
N. I. Boretska ◽  
O. Ye. Liauta-Teglivets ◽  
A. Y. Voronovsky ◽  
J. R. Boretsky ◽  
G. M. Shavlovsky
Keyword(s):  
Bacillus Subtilis ◽  
Riboflavin Operon ◽  
Phosphate Synthase

Enhanced Riboflavin Production by Expressing Heterologous Riboflavin Operon from B. cereus ATCC14579 in Bacillus subtilis

2010 ◽  
Vol 18 (1) ◽  
pp. 129-136 ◽  
Author(s):  
Yunxia DUAN ◽  
Tao CHEN ◽  
Xun CHEN ◽  
Wang Jingyu ◽  
Xueming ZHAO
Keyword(s):  
Bacillus Subtilis ◽  
Riboflavin Production ◽  
Riboflavin Operon

Glyphosate sensitivity of 5-enol-pyruvylshikimate-3-phosphate synthase from Bacillus subtilis depends upon state of activation induced by monovalent cations

1987 ◽  
Vol 256 (1) ◽  
pp. 325-334 ◽  
Author(s):  
Randy S. Fischer ◽  
Judith L. Rubin ◽  
C. Greg Gaines ◽  
Roy A. Jensen
Keyword(s):  
Bacillus Subtilis ◽  
Monovalent Cations ◽  
Phosphate Synthase

scholarly journals Bacillus subtilis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase revisited: resolution of two long-standing enigmas

2005 ◽  
Vol 390 (2) ◽  
pp. 583-590 ◽  
Author(s):  
Jing Wu ◽  
Galina Ya. Sheflyan ◽  
Ronald W. Woodard
Keyword(s):  
Bacillus Subtilis ◽  
Dipicolinic Acid ◽  
Shikimate Pathway ◽  
Chorismate Mutase ◽  
Highly Active ◽  
Bifunctional Enzymes ◽  
Iron And Zinc ◽  
Bivalent Metal Ions ◽  
Structure In Solution ◽  
Phosphate Synthase

The mono/bifunctional and metallo/non-metallo properties of Bacillus subtilis DAHPS (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase) have been controversial for several decades. The present study investigated the DAHPSs from both the B. subtilis parent Marburg strain and the derivative strain 168 in detail and clarified the above two long-standing questions. The DAHPSs from the parent and the derivative 168 strains have identical sequence and are both bifunctional enzymes with a CM (chorismate mutase) activity and a DAHPS activity. The parent strain expresses a second independent monofunctional CM, encoded by aroH, that is highly active, while the 168 strain expresses an aroH containing a single residue mutation (A112V) that is significantly less active thus leading to previous confusion regarding the mono/bifunctionality of DAHPS. Metal analysis showed that B. subtilis DAHPS as isolated contained iron and zinc and is inactivated by dipicolinic acid; the inactive apoenzyme can be reactivated by bivalent metal ions, indicating that the enzyme is a metalloenzyme. The enzyme-bound metal is insensitive to EDTA treatment, leading to the previous conclusion that this DAHPS does not require a metal. The enzyme displays a homotetrameric structure in solution and appears to follow Michaelis–Menten kinetics with KmPEP=139±11.4 μM for phosphoenolpyruvate, KmE4P=1760±110 μM for D-erythrose 4-phosphate, kcat=4.6±0.1 s−1 for DAHPS activity and Kmchorismate=850±97 μM, kcat=0.41±0.01 s−1 for CM activity. B. subtilis DAHPS is inhibited by the Shikimate pathway intermediates prephenate and chorismate.

The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon

Microbiology ◽  
1999 ◽  
Vol 145 (1) ◽  
pp. 67-73 ◽  
Author(s):  
I. M. Solovieva ◽  
R. A. Kreneva ◽  
D. J. Leak ◽  
D. A. Perumov
Keyword(s):  
Bacillus Subtilis ◽  
Riboflavin Operon

scholarly journals Evidence for the shikimate-3-phosphate interacting site in the N-terminal domain of 5-enolpyruvyl shikimate-3-phosphate synthase of Bacillus subtilis

IUBMB Life ◽  
1996 ◽  
Vol 40 (3) ◽  
pp. 603-610
Author(s):  
Angamuthu Selvapandiyan ◽  
Suhail Ahmad ◽  
Kumud Majumder ◽  
Naresh Arora ◽  
Raj Bhatnagar
Keyword(s):  
Bacillus Subtilis ◽  
Terminal Domain ◽  
Phosphate Synthase

scholarly journals Evidence for an artificially evolved bifunctional 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase-chorismate mutase in Bacillus subtilis.

1980 ◽  
Vol 255 (5) ◽  
pp. 2077-2084
Author(s):  
D.J. Llewellyn ◽  
A. Daday ◽  
G.D. Smith
Keyword(s):  
Bacillus Subtilis ◽  
Chorismate Mutase ◽  
Phosphate Synthase

5-Enolpyruvylshikimate-3-phosphate Synthase of Bacillus subtilis is an Allosteric Enzyme. Analysis of Arg24Asp, Pro105Ser and His385Lys mutations suggests a hidden phosphoenol pyruvate-binding site

1995 ◽  
Vol 229 (1) ◽  
pp. 99-106 ◽  
Author(s):  
Kumud Majumder ◽  
Angamuthu Selvapandiyan ◽  
Farkad A. Fattah ◽  
Naresh Arora ◽  
Suhail Ahmad ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Binding Site ◽  
Enzyme Analysis ◽  
Allosteric Enzyme ◽  
Phosphoenol Pyruvate ◽  
Phosphate Synthase

scholarly journals Characterization of YvcJ, a Conserved P-Loop-Containing Protein, and Its Implication in Competence in Bacillus subtilis

2008 ◽  
Vol 191 (5) ◽  
pp. 1556-1564 ◽  
Author(s):  
Jennifer Luciano ◽  
Elodie Foulquier ◽  
Jean-Raphael Fantino ◽  
Anne Galinier ◽  
Frédérique Pompeo
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Transformation Efficiency ◽  
Cellular Function ◽  
Protein Family ◽  
Wild Type ◽  
Uncharacterized Protein ◽  
E Coli ◽  
Phosphate Synthase

ABSTRACT The uncharacterized protein family UPF0042 of the Swiss-Prot database is predicted to be a member of the conserved group of bacterium-specific P-loop-containing proteins. Here we show that two of its members, YvcJ from Bacillus subtilis and YhbJ, its homologue from Escherichia coli, indeed bind and hydrolyze nucleotides. The cellular function of yvcJ was then addressed. In contrast to results recently obtained for E. coli, which indicated that yhbJ mutants strongly overproduced glucosamine-6-phosphate synthase (GlmS), comparison of the wild type with the yvcJ mutant of B. subtilis showed that GlmS expression was quite similar in the two strains. However, in mutants defective in yvcJ, the transformation efficiency and the fraction of cells that expressed competence were reduced. Furthermore, our data show that YvcJ positively controls the expression of late competence genes. The overexpression of comK or comS compensates for the decrease in competence of the yvcJ mutant. Our results show that even if YvcJ and YhbJ belong to the same family of P-loop-containing proteins, the deletion of corresponding genes has different consequences in B. subtilis and in E. coli.

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