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 ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Molecular Cloning ◽  
Membrane Bound ◽  
Prenyl Diphosphate

scholarly journals Molecular Cloning and Sequencing of the cDNA for Human Membrane-bound Carboxypeptidase M

1989 ◽  
Vol 264 (22) ◽  
pp. 13165-13170 ◽  
Author(s):  
F Tan ◽  
S J Chan ◽  
D F Steiner ◽  
J W Schilling ◽  
R A Skidgel
Keyword(s):  
Molecular Cloning ◽  
Cloning And Sequencing ◽  
Membrane Bound ◽  
Carboxypeptidase M

Copper and nickel uptake and accumulation, and their effects on redox and electrical potentials of hepatopancreatic cells of Oniscus asellus Linnaeus (Porcellionidae, Isopoda)

1990 ◽  
Vol 68 (4) ◽  
pp. 651-655 ◽  
Author(s):  
M. A. Alikhan ◽  
V. Storch
Keyword(s):  
Catalytic Activity ◽  
Cell Membrane ◽  
Membrane Surface ◽  
Dry Weight ◽  
Body Tissue ◽  
Electrical Potentials ◽  
Nickel Uptake ◽  
Membrane Bound ◽  
Total Body ◽  
Cell Membrane Surface

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.

scholarly journals Purification, Molecular Cloning, and Catalytic Activity ofSchizosaccharomyces pombePyridoxal Reductase

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

The murine interleukin-4 receptor: Molecular cloning and characterization of secreted and membrane bound forms

Cell ◽  
1989 ◽  
Vol 59 (2) ◽  
pp. 335-348 ◽  
Author(s):  
Bruce Mosley ◽  
M.Patricia Beckmann ◽  
Carl J. March ◽  
Rejean L. Idzerda ◽  
Steven D. Gimpel ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Interleukin 4 ◽  
Membrane Bound ◽  
Interleukin 4 Receptor

The catalytic activity of soluble and membrane-bound succinate dehydrogenase

FEBS Letters ◽  
1977 ◽  
Vol 73 (2) ◽  
pp. 235-238 ◽  
Author(s):  
A.D. Vinogradov ◽  
V.G. Goloveshkina ◽  
E.V. Gavrikova
Keyword(s):  
Catalytic Activity ◽  
Succinate Dehydrogenase ◽  
Membrane Bound

Determinants of the enzymatic activity and the subcellular localization of aspartate N-acetyltransferase

2011 ◽  
Vol 441 (1) ◽  
pp. 105-112 ◽  
Author(s):  
Gaëlle Tahay ◽  
Elsa Wiame ◽  
Donatienne Tyteca ◽  
Pierre J. Courtoy ◽  
Emile Van Schaftingen
Keyword(s):  
Catalytic Activity ◽  
Subcellular Localization ◽  
Fluorescent Protein ◽  
Catalytic Domain ◽  
Kinetic Properties ◽  
Conserved Residues ◽  
Membrane Bound ◽  
Green Fluorescent ◽  
Necessary And Sufficient ◽  
Membrane Region

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.

Catalytic activity of the membrane-bound methylcholanthrene-inducible cytochrome P-450

FEBS Letters ◽  
1985 ◽  
Vol 179 (1) ◽  
pp. 74-76 ◽  
Author(s):  
A.Yu. Grishanova ◽  
V.M. Mishin ◽  
V.V. Lyakhovich
Keyword(s):  
Catalytic Activity ◽  
Membrane Bound ◽  
Cytochrome P 450
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