scholarly journals A Functional Genetic Polymorphism on Human Carbonyl Reductase 1 (CBR1 V88I) Impacts on Catalytic Activity and NADPH Binding Affinity

2007 ◽  
Vol 35 (6) ◽  
pp. 973-980 ◽  
Author(s):  
Vanessa Gonzalez-Covarrubias ◽  
Debashis Ghosh ◽  
Sukhwinder S. Lakhman ◽  
Lakshmi Pendyala ◽  
Javier G. Blanco
2014 ◽  
Vol 82 (12) ◽  
pp. 3397-3409 ◽  
Author(s):  
Sarah Sirin ◽  
David A. Pearlman ◽  
Woody Sherman

2005 ◽  
Vol 102 (5) ◽  
pp. 1785-1790 ◽  
Author(s):  
R. Mikkelsen ◽  
K. E. Mutenda ◽  
A. Mant ◽  
P. Schurmann ◽  
A. Blennow

2000 ◽  
Vol 350 (1) ◽  
pp. 89-92 ◽  
Author(s):  
Michel A. SCIOTTI ◽  
Shizuo NAKAJIN ◽  
Bendicht WERMUTH ◽  
Michael E. BAKER

Carbonyl reductase catalyses the reduction of steroids, prostaglandins and a variety of xenobiotics. An unusual property of human and rat carbonyl reductases is that they undergo modification at lysine-239 by an autocatalytic process involving 2-oxocarboxylic acids, such as pyruvate and 2-oxoglutarate. Comparison of human carbonyl reductase with the pig enzyme, which does not undergo autocatalytic modification, identified three sites, alanine-236, threonine-241 and glutamic acid-246, on human carbonyl reductase that could be important in the reaction of lysine-239 with 2-oxocarboxylic acids. Mutagenesis experiments show that replacement of threonine-241 with proline (T241P) in human carbonyl reductase eliminates the formation of carboxyethyl-lysine-239. In contrast, the T241A mutant has autocatalytic activity similar to wild-type carbonyl reductase. The T241P mutant retains catalytic activity towards menadione, although with one-fifth the catalytic efficiency of wild-type carbonyl reductase. Replacement of threonine-241 with proline is likely to disrupt the local structure near lysine-239. We propose that integrity of this local environment is essential for chemical modification of lysine-239, but not absolutely required for carbonyl reductase activity.


2021 ◽  
Author(s):  
Xin Huang ◽  
Nazym Bashkenova ◽  
Yantao Hong ◽  
Diana Guallar ◽  
Zhe Hu ◽  
...  

SUMMARYTET1 maintains hypomethylation at bivalent promoters through its catalytic activity in embryonic stem cells (ESCs). However, whether and how TET1 exerts catalytic activity-independent functions in regulating bivalent genes is not well understood. Using a proteomics approach, we mapped the TET1 interactome in mouse ESCs and identified PSPC1 as a novel TET1 partner. Genome-wide location analysis reveals that PSPC1 functionally associates with TET1 and Polycomb repressive complex-2 (PRC2) complex. We establish that PSPC1 and TET1 repress, and Neat1, the PSPC1 cognate lncRNA, activates the bivalent gene expression. In ESCs, Neat1 tethers the TET1-PSPC1 pair with PRC2 at bivalent promoters. During the ESC-to-formative epiblast-like stem cell (EpiLC) transition, PSPC1 and TET1 promote PRC2 chromatin occupancy at bivalent gene promoters while restricting Neat1 functions in facilitating PRC2 binding to bivalent gene transcripts. Our study uncovers a novel TET1-PSPC1-Neat1 molecular axis that modulates PRC2 binding affinity to chromatin and bivalent gene transcripts in controlling stem cell bivalency.In BriefTET1 is a transcriptional repressor for bivalent genes in pluripotent stem cells, but its mechanistic action on stem cell bivalency is unclear. Huang et al. use proteomics and genetic approaches to reveal that catalytic activity-independent functions of TET1, coordinated with the paraspeckle components PSPC1 and its cognate lncRNA Neat1, dynamically regulates stem cell bivalency by modulating PRC2 binding affinity to chromatin and bivalent gene transcripts in pluripotent state transition.HighlightsThe TET1 interactome identifies PSPC1 as a novel partner in ESCsTET1 and PSPC1 repress bivalent genes by promoting PRC2 chromatin occupancyNeat1 facilitates bivalent gene activation by promoting PRC2 binding to their mRNAsNeat1 bridges the TET1-PSPC1 and PRC2 complexes in regulating bivalent gene transcription


Author(s):  
J. C. Wheatley ◽  
J. M. Cowley

Rare-earth phosphates are of particular interest because of their catalytic properties associated with the hydrolysis of many aromatic chlorides in the petroleum industry. Lanthanum phosphates (LaPO4) which have been doped with small amounts of copper have shown increased catalytic activity (1). However the physical and chemical characteristics of the samples leading to good catalytic activity are not known.Many catalysts are amorphous and thus do not easily lend themselves to methods of investigation which would include electron microscopy. However, the LaPO4, crystals are quite suitable samples for high resolution techniques.The samples used were obtained from William L. Kehl of Gulf Research and Development Company. The electron microscopy was carried out on a JEOL JEM-100B which had been modified for high resolution microscopy (2). Standard high resolution techniques were employed. Three different sample types were observed: 669A-1-5-7 (poor catalyst), H-L-2 (good catalyst) and 27-011 (good catalyst).


2019 ◽  
Vol 9 (3) ◽  
pp. 811-821 ◽  
Author(s):  
Zhao-Meng Wang ◽  
Li-Juan Liu ◽  
Bo Xiang ◽  
Yue Wang ◽  
Ya-Jing Lyu ◽  
...  

The catalytic activity decreases as –(SiO)3Mo(OH)(O) > –(SiO)2Mo(O)2 > –(O)4–MoO.


2009 ◽  
Author(s):  
Anke Karl ◽  
Loretta Malta ◽  
Alexander Strobel ◽  
Katza Poehnitzsch ◽  
Sirko Rabe

2011 ◽  
Vol 49 (01) ◽  
Author(s):  
MF Sprinzl ◽  
L Bührer ◽  
D Strand ◽  
G Schreiber ◽  
PR Galle ◽  
...  

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