Faculty Opinions recommendation of Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases.

Author(s):  
Rowena Matthews
2006 ◽  
Vol 282 (9) ◽  
pp. 6609-6618 ◽  
Author(s):  
Tzanko I. Doukov ◽  
Hisashi Hemmi ◽  
Catherine L. Drennan ◽  
Stephen W. Ragsdale

Biochemistry ◽  
2016 ◽  
Vol 55 (27) ◽  
pp. 3834-3846 ◽  
Author(s):  
Melek N. Ucisik ◽  
Philip C. Bevilacqua ◽  
Sharon Hammes-Schiffer

2021 ◽  
Vol 9 (1) ◽  
Author(s):  
Yiqing Cai ◽  
Rui Feng ◽  
Tiange Lu ◽  
Xiaomin Chen ◽  
Xiangxiang Zhou ◽  
...  

AbstractN6-methyladenosine (m6A) is a prevalent internal RNA modification in higher eukaryotic cells. As the pivotal m6A regulator, RNA methyltransferase-like 3 (METTL3) is responsible for methyl group transfer in the progression of m6A modification. This epigenetic regulation contributes to the structure and functional regulation of RNA and further promotes tumorigenesis and tumor progression. Accumulating evidence has illustrated the pivotal roles of METTL3 in a variety of human cancers. Here, we systemically summarize the interaction between METTL3 and RNAs, and illustrate the multiple functions of METTL3 in human cancer. METLL3 is aberrantly expressed in a variety of tumors. Elevation of METTL3 is usually associated with rapid progression and poor prognosis of tumors. On the other hand, METTL3 may also function as a tumor suppressor in several cancers. Based on the tumor-promoting effect of METTL3, the possibility of applying METTL3 inhibitors is further discussed, which is expected to provide novel insights into antitumor therapy.


2018 ◽  
Vol 53 (5) ◽  
pp. 379-384 ◽  
Author(s):  
Rafał Frański ◽  
Błażej Gierczyk ◽  
Maciej Zalas ◽  
Wojciech Jankowski ◽  
Marcin Hoffmann

Biomimetics ◽  
2019 ◽  
Vol 4 (4) ◽  
pp. 66
Author(s):  
Park ◽  
Lee

Zinc complexes were synthesized as catalysts that mimic the ability of carbonic anhydrase (CA) for the CO2 hydration reaction (H2O + CO2 → H+ + HCO3-). For these complexes, a tris(2-pyridylmethyl)amine (TPA) ligand mimicking only the active site, and a 6-((bis(pyridin-2-ylmethyl)amino)methyl)pyridin-2-ol (TPA-OH) ligand mimicking the hydrogen-bonding network of the secondary coordination sphere of CA were used. Potentiometric pH titration was used to determine the deprotonation ability of the Zn complexes, and their pKa values were found to be 8.0 and 6.8, respectively. Stopped-flow spectrophotometry was used to confirm the CO2 hydration rate. The rate constants were measured to be 648.4 and 730.6 M-1s-1, respectively. The low pKa value was attributed to the hydrogen-bonding network of the secondary coordination sphere of the catalyst that mimics the behavior of CA, and this was found to increase the CO2 hydration rate of the catalyst.


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