Differentiation dependent changes in the expression of a novel member of the ubiquitin enzyme variant family in the Caco-2 cell

2001 ◽  
Vol 120 (5) ◽  
pp. A500-A501
Author(s):  
G WILD ◽  
J FARIA ◽  
C COSSETTE ◽  
L DUFRESNE ◽  
A VILLANI ◽  
...  
Keyword(s):  
Enzyme Variant

Cell-Specific Chemical Delivery Using a Selective Nitroreductase–Nitroaryl Pair

2018 ◽  
Author(s):  
Todd D. Gruber ◽  
Chithra Krishnamurthy ◽  
Jonathan B. Grimm ◽  
Michael R. Tadross ◽  
Laura M. Wysocki ◽  
...  
Keyword(s):  
Small Molecules ◽  
Mammalian Cells ◽  
Target Cells ◽  
Specific Chemical ◽  
E Coli ◽  
Enzyme Substrate ◽  
Cell Specificity ◽  
General Chemical ◽  
Increased Activity ◽  
Enzyme Variant

<p>The utility of<b> </b>small molecules to probe or perturb biological systems is limited by the lack of cell-specificity. ‘Masking’ the activity of small molecules using a general chemical modification and ‘unmasking’ it only within target cells could overcome this limitation. To this end, we have developed a selective enzyme–substrate pair consisting of engineered variants of <i>E. coli</i> nitroreductase (NTR) and a 2‑nitro-<i>N</i>-methylimidazolyl (NM) masking group. To discover and optimize this NTR–NM system, we synthesized a series of fluorogenic substrates containing different nitroaromatic masking groups, confirmed their stability in cells, and identified the best substrate for NTR. We then engineered the enzyme for improved activity in mammalian cells, ultimately yielding an enzyme variant (enhanced NTR, or eNTR) that possesses up to 100-fold increased activity over wild-type NTR. These improved NTR enzymes combined with the optimal NM masking group enable rapid, selective unmasking of dyes, indicators, and drugs to genetically defined populations of cells.</p>

Structural Basis for Non-Covalent Interaction Between Ubiquitin and the Ubiquitin Conjugating Enzyme Variant Human MMS2

2006 ◽  
Vol 34 (2) ◽  
pp. 89-100 ◽  
Author(s):  
Michael J. Lewis ◽  
Linda F. Saltibus ◽  
D. Duong Hau ◽  
Wei Xiao ◽  
Leo Spyracopoulos
Keyword(s):  
Structural Basis ◽  
Covalent Interaction ◽  
Ubiquitin Conjugating Enzyme ◽  
Enzyme Variant ◽  
Conjugating Enzyme

scholarly journals Characterization of the Ubiquitin E2 Enzyme Variant Gene Family in Arabidopsis

2007 ◽  
Vol 49 (1) ◽  
pp. 120-126 ◽  
Author(s):  
Yu Zhang ◽  
Pei Wen ◽  
On-Sun Lau ◽  
Xing-Wang Deng
Keyword(s):  
Gene Family ◽  
Variant Gene ◽  
Enzyme Variant

scholarly journals Glucosephosphate Isomerase Deficiency: Evidence for In Vivo Instability of an Enzyme Variant With Hemolysis

Blood ◽  
1973 ◽  
Vol 41 (5) ◽  
pp. 691-699 ◽  
Author(s):  
Heidwolf Arnold ◽  
Karl-Georg Blume ◽  
Rupert Engelhardt ◽  
Georg Wilhelm Löhr
Keyword(s):  
Blood Cells ◽  
Cell Populations ◽  
Red Cell ◽  
Glucosephosphate Isomerase ◽  
Metabolic Capacity ◽  
Comparable Amount ◽  
Glucose Phosphate ◽  
Enzyme Variant

Abstract Pathogenesis of hemolysis in glucose-phosphate isomerase (GPI) deficiency was studied. Red cell populations of different ages were obtained by density centrifugation. In comparison to cell populations with comparable amount of reticulocytes, GPI activity decreased faster in the deficient red cells. A method to simulate aging blood cells in vitro was devised. On the first day the rate of glycolysis was normal in the deficient cells, but by the eighth day of the incubation period, the metabolic capacity decreased markedly, and hemolysis was observed. Using mannose as a source of energy, the rate of glycolysis was still normal by the eighth day, which reflects the cause and effect relationship between impairment of energy metabolism and GPI deficiency. It may be concluded that hemolytic anemia in this case of GPI deficiency is caused by the synthesis of a qualitatively changed subunit of the GPI molecule, which is associated with faster inactivation of the enzyme in vivo.

Cell-Specific Chemical Delivery Using a Selective Nitroreductase–Nitroaryl Pair

2018 ◽  
Author(s):  
Todd D. Gruber ◽  
Chithra Krishnamurthy ◽  
Jonathan B. Grimm ◽  
Michael R. Tadross ◽  
Laura M. Wysocki ◽  
...  
Keyword(s):  
Small Molecules ◽  
Mammalian Cells ◽  
Target Cells ◽  
Specific Chemical ◽  
E Coli ◽  
Enzyme Substrate ◽  
Cell Specificity ◽  
General Chemical ◽  
Increased Activity ◽  
Enzyme Variant

<p>The utility of<b> </b>small molecules to probe or perturb biological systems is limited by the lack of cell-specificity. ‘Masking’ the activity of small molecules using a general chemical modification and ‘unmasking’ it only within target cells could overcome this limitation. To this end, we have developed a selective enzyme–substrate pair consisting of engineered variants of <i>E. coli</i> nitroreductase (NTR) and a 2‑nitro-<i>N</i>-methylimidazolyl (NM) masking group. To discover and optimize this NTR–NM system, we synthesized a series of fluorogenic substrates containing different nitroaromatic masking groups, confirmed their stability in cells, and identified the best substrate for NTR. We then engineered the enzyme for improved activity in mammalian cells, ultimately yielding an enzyme variant (enhanced NTR, or eNTR) that possesses up to 100-fold increased activity over wild-type NTR. These improved NTR enzymes combined with the optimal NM masking group enable rapid, selective unmasking of dyes, indicators, and drugs to genetically defined populations of cells.</p>

Uev1A, a ubiquitin conjugating enzyme variant, inhibits stress-induced apoptosis through NF-κB activation

APOPTOSIS ◽  
2006 ◽  
Vol 11 (12) ◽  
pp. 2147-2157 ◽  
Author(s):  
Noor A. Syed ◽  
Parker L. Andersen ◽  
Robert C. Warrington ◽  
Wei Xiao
Keyword(s):  
Ubiquitin Conjugating Enzyme ◽  
Induced Apoptosis ◽  
Enzyme Variant ◽  
Conjugating Enzyme
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