Production ofPseudomonas putida cells with high aspartase activity

1990 ◽  
Vol 12 (8) ◽  
pp. 557-562 ◽  
Author(s):  
Sami Maalej ◽  
Nelly Cochet ◽  
Jean-Michel Lebeault
Keyword(s):  
Aspartase Activity

Aspartase Activity of Soils

1996 ◽  
Vol 60 (5) ◽  
pp. 1416-1422 ◽  
Author(s):  
Z. N. Senwo ◽  
M. A. Tabatabai
Keyword(s):  
Aspartase Activity

Reason for higher stability of aspartase activity of immobilized Escherichia coli cells

1977 ◽  
Vol 483 (1) ◽  
pp. 193-202 ◽  
Author(s):  
Tetsuya Tosa ◽  
Tadashi Sato ◽  
Yutaka Nishida ◽  
Ichiro Chibata
Keyword(s):  
Escherichia Coli ◽  
Escherichia Coli Cells ◽  
Aspartase Activity

Studies on the identification and characterization of an aspartase activity in liver of elasmobranch fishes

1972 ◽  
Vol 41 (4) ◽  
pp. 905-919
Author(s):  
Letizia Cutinelli ◽  
Concetta Pietropaolo ◽  
Salvatore Venuta ◽  
Vincenzo Zappia ◽  
Francesco Salvatore
Keyword(s):  
Aspartase Activity ◽  
Elasmobranch Fishes ◽  
Identification And Characterization

scholarly journals Acquisition of Aspartase Activity in Rhizobium leguminosarum WU235

Microbiology ◽  
1984 ◽  
Vol 130 (4) ◽  
pp. 881-886 ◽  
Author(s):  
P. S. Poole ◽  
M. J. Dilworth ◽  
A. R. Glenn
Keyword(s):  
Rhizobium Leguminosarum ◽  
Aspartase Activity

scholarly journals A Novel Mechanism for Resistance to the Antimetabolite N -Phosphonoacetyl-l-Aspartate by Helicobacter pylori

1998 ◽  
Vol 180 (21) ◽  
pp. 5574-5579 ◽  
Author(s):  
Brendan P. Burns ◽  
George L. Mendz ◽  
Stuart L. Hazell
Keyword(s):  
Helicobacter Pylori ◽  
Nmr Spectroscopy ◽  
De Novo ◽  
Bond Cleavage ◽  
Substrate Inhibition ◽  
Mechanism Of Resistance ◽  
Cleavage Activity ◽  
Compound C ◽  
Aspartase Activity ◽  
H Pylori

ABSTRACT The mechanism of resistance toN-phosphonoacetyl-l-aspartate (PALA), a potent inhibitor of aspartate carbamoyltransferase (which catalyzes the first committed step of de novo pyrimidine biosynthesis), inHelicobacter pylori was investigated. At a 1 mM concentration, PALA had no effects on the growth and viability ofH. pylori. The inhibitor was taken up by H. pylori cells and the transport was saturable, with aKm of 14.8 mM and aV max of 19.1 nmol min−1 μl of cell water−1. By 31P nuclear magnetic resonance (NMR) spectroscopy, both PALA and phosphonoacetate were shown to have been metabolized in all isolates of H. pyloristudied. A main metabolic end product was identified as inorganic phosphate, suggesting the presence of an enzyme activity which cleaved the carbon-phosphorus (C-P) bonds. The kinetics of phosphonate group cleavage was saturable, and there was no evidence for substrate inhibition at higher concentrations of either compound. C-P bond cleavage activity was temperature dependent, and the activity was lost in the presence of the metal chelator EDTA. Other cleavages of PALA were observed by 1H NMR spectroscopy, with succinate and malate released as main products. These metabolic products were also formed when N-acetyl-l-aspartate was incubated with H. pylori lysates, suggesting the action of an aspartase. Studies of the cellular location of these enzymes revealed that the C-P bond cleavage activity was localized in the soluble fraction and that the aspartase activity appeared in the membrane-associated fraction. The results suggested that the twoH. pylori enzymes transformed the inhibitor into noncytotoxic products, thus providing the bacterium with a mechanism of resistance to PALA toxicity which appears to be unique.

scholarly journals FACTORS AFFECTING ASPARTASE ACTIVITY

1961 ◽  
Vol 82 (3) ◽  
pp. 383-386 ◽  
Author(s):  
Robert H. Depue ◽  
Albert G. Moat
Keyword(s):  
Factors Affecting ◽  
Aspartase Activity
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