cyclicAMP and glucocorticoid responsiveness of the rat carbamoylphosphate synthetase gene requires the interplay of upstream regulatory units

Biochimie ◽  
2007 ◽  
Vol 89 (5) ◽  
pp. 574-580 ◽  
Author(s):  
O SCHONEVELD ◽  
M HOOGENKAMP ◽  
J STALLEN ◽  
I GAEMERS ◽  
W LAMERS
FEBS Letters ◽  
1990 ◽  
Vol 276 (1-2) ◽  
pp. 9-13 ◽  
Author(s):  
Antoon F.M. Moorman ◽  
Piet A.J. de Boer ◽  
Robert Charles ◽  
Wouter H. Lamers

1994 ◽  
Vol 48 (4) ◽  
pp. 213-221 ◽  
Author(s):  
Mikiko Ozaki ◽  
Kazutoyo Terada ◽  
Masaki Kanazawa ◽  
Shigetoshi Fujiyama ◽  
Kimio Tomita ◽  
...  

Gene ◽  
2000 ◽  
Vol 243 (1-2) ◽  
pp. 105-114 ◽  
Author(s):  
Zongmin Zhou ◽  
Anthony E. Metcalf ◽  
Carol J. Lovatt ◽  
Bradley C. Hyman

1984 ◽  
Vol 246 (5) ◽  
pp. R805-R810 ◽  
Author(s):  
J. W. Campbell ◽  
J. E. Vorhaben ◽  
D. D. Smith

Glutamine synthetase, a mitochondrial enzyme in liver of uricotelic reptiles and birds, is present in the cytosolic compartment of Phyllomedusa sauvagei liver. The average level is sufficient to account for the rate of uric acid excretion by adult frogs but is far lower than that present in birds and reptiles. Except for lower carbamoylphosphate synthetase activity, the activities of the urea cycle enzymes in P. sauvagei liver are comparable with those in adult ureotelic amphibians. The subcellular distribution of the urea cycle enzymes is much the same as in ureotelic amphibians and mammals with the possible exception of the occurrence of a small percentage of the carbamoylphosphate synthetase and ornithine transacarbamylase activities in the cytosol. In keeping with the subcellular localization of the enzymes, citrulline, and not glutamine, is formed by isolated liver mitochondria. The rapid degradation of glutamine by these mitochondria suggests a high degree of compartmentation of glutamine in the cytosol of P. sauvagei if it is to function as a precursor of uric acid in this compartment.


Biochimie ◽  
2005 ◽  
Vol 87 (11) ◽  
pp. 1033-1040 ◽  
Author(s):  
Onard J.L.M. Schoneveld ◽  
Ingrid C. Gaemers ◽  
Maarten Hoogenkamp ◽  
Wouter H. Lamers

1982 ◽  
Vol 5 (S1) ◽  
pp. 23-24
Author(s):  
M. Ameen ◽  
T. Palmer ◽  
V. G. Oberholzer

1998 ◽  
Vol 180 (17) ◽  
pp. 4380-4386 ◽  
Author(s):  
Jan Martinussen ◽  
Karin Hammer

ABSTRACT The biosynthesis of carbamoylphosphate is catalyzed by the heterodimeric enzyme carbamoylphosphate synthetase. The genes encoding the two subunits of this enzyme in procaryotes are normally transcribed as an operon, but the gene encoding the large subunit (carB) in Lactococcus lactis is shown to be transcribed as an isolated unit. Carbamoylphosphate is a precursor in the biosynthesis of both pyrimidine nucleotides and arginine. By mutant analysis,L. lactis is shown to possess only onecarB gene; the same gene product is thus required for both biosynthetic pathways. Furthermore, arginine may satisfy the requirement for carbamoylphosphate in pyrimidine biosynthesis through degradation by means of the arginine deiminase pathway. The expression of the carB gene is subject to regulation at the level of transcription by pyrimidines, most probably by an attenuator mechanism. Upstream of the carB gene, an open reading frame showing a high degree of similarity to those of glutathione peroxidases from other organisms was identified.


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