Molecular cloning and catalytic activity of a membrane-bound prenyl diphosphate phosphatase from Croton stellatopilosus Ohba

2013 ◽  
Vol 91 ◽  
pp. 140-147 ◽  
Author(s):  
Natsajee Nualkaew ◽  
Nils Guennewich ◽  
Karin Springob ◽  
Anuwatchakit Klamrak ◽  
Wanchai De-Eknamkul ◽  
...  
1989 ◽  
Vol 264 (22) ◽  
pp. 13165-13170 ◽  
Author(s):  
F Tan ◽  
S J Chan ◽  
D F Steiner ◽  
J W Schilling ◽  
R A Skidgel

1990 ◽  
Vol 68 (4) ◽  
pp. 651-655 ◽  
Author(s):  
M. A. Alikhan ◽  
V. Storch

Highest tissue Cu concentrations (1728 μg∙g dry weight−1) in whole Oniscus asellus, reared for 7 days on carrot powder containing 50 μg Cu∙g dry weight−1, 10 μg Ni∙g dry weight−1, or a mixture of 50 μg Cu and 10 μg Ni∙g dry weight−1, were observed in isopods on 50 μg Cu∙g dry weight−1, and lowest (917 μg∙g dry weight−1) in those on 10 μg Ni∙g dry weight−1. Highest Ni concentrations (277 and 272 μg∙g dry weight−1) were present in isopods fed on a mixture of 50 μg Cu and 10 μg Ni∙g dry weight−1 and 10 μg Ni∙g dry weight−1, respectively, and lowest (201 μg∙g dry weight−1) in those on 50 μg Cu∙g dry weight−1. Of the total body-tissue Cu, 8–66% was contained in membrane-bound vesicles of hepatopancreatic S-cells, and 73–89% of Ni was present inside the lumen and within S-cells of the hepatopancreas. The presence of Ni in the diet appeared to adversely affect the absorption and hepatopancreatic storage of Cu. Copper slightly enhanced, and nickel drastically reduced, the hepatopancreatic redox (= catalytic activity) and cell-membrane surface potentials. The significance of these findings is discussed.


1999 ◽  
Vol 274 (33) ◽  
pp. 23185-23190 ◽  
Author(s):  
Mitsuhiro Nakano ◽  
Tomotake Morita ◽  
Tomokazu Yamamoto ◽  
Hisashi Sano ◽  
Makoto Ashiuchi ◽  
...  

Cell ◽  
1989 ◽  
Vol 59 (2) ◽  
pp. 335-348 ◽  
Author(s):  
Bruce Mosley ◽  
M.Patricia Beckmann ◽  
Carl J. March ◽  
Rejean L. Idzerda ◽  
Steven D. Gimpel ◽  
...  

FEBS Letters ◽  
1977 ◽  
Vol 73 (2) ◽  
pp. 235-238 ◽  
Author(s):  
A.D. Vinogradov ◽  
V.G. Goloveshkina ◽  
E.V. Gavrikova

2011 ◽  
Vol 441 (1) ◽  
pp. 105-112 ◽  
Author(s):  
Gaëlle Tahay ◽  
Elsa Wiame ◽  
Donatienne Tyteca ◽  
Pierre J. Courtoy ◽  
Emile Van Schaftingen

Aspartate N-acetyltransferase (NAT8L, N-acetyltransferase 8-like), the enzyme that synthesizes N-acetylaspartate, is membrane-bound and is at least partially associated with the ER (endoplasmic reticulum). The aim of the present study was to determine which regions of the protein are important for its catalytic activity and its subcellular localization. Transfection of truncated forms of NAT8L into HEK (human embryonic kidney)-293T cells indicated that the 68 N-terminal residues (regions 1 and 2) have no importance for the catalytic activity and the subcellular localization of this enzyme, which was exclusively associated with the ER. Mutation of conserved residues that precede (Arg81 and Glu101, in region 3) or follow (Asp168 and Arg220, in region 5) the putative membrane region (region 4) markedly affected the kinetic properties, suggesting that regions 3 and 5 form the catalytic domain and that the membrane region has a loop structure. Evidence is provided for the membrane region comprising α-helices and the catalytic site being cytosolic. Transfection of chimaeric proteins in which GFP (green fluorescent protein) was fused to different regions of NAT8L indicated that the membrane region (region 4) is necessary and sufficient to target NAT8L to the ER. Thus NAT8L is targeted to the ER membrane by a hydrophobic loop that connects two regions of the catalytic domain.


FEBS Letters ◽  
1985 ◽  
Vol 179 (1) ◽  
pp. 74-76 ◽  
Author(s):  
A.Yu. Grishanova ◽  
V.M. Mishin ◽  
V.V. Lyakhovich

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