scholarly journals Redesign of the colicin E7 nuclease domain into a controlled and specific artificial enzyme

2014 ◽  
Author(s):  
Eszter Németh
Keyword(s):  
Artificial Enzyme ◽  
Nuclease Domain ◽  
Colicin E7

The Crystal Structure of the Nuclease Domain of Colicin E7 Suggests a Mechanism for Binding to Double-stranded DNA by the H–N–H Endonucleases

2002 ◽  
Vol 324 (2) ◽  
pp. 227-236 ◽  
Author(s):  
Yi-Sheng Cheng ◽  
Kuo-Chiang Hsia ◽  
Lyudmila G. Doudeva ◽  
Kin-Fu Chak ◽  
Hanna S. Yuan
Keyword(s):  
Crystal Structure ◽  
Nuclease Domain ◽  
Double Stranded Dna ◽  
Colicin E7

scholarly journals The role of the N-terminal loop in the function of the colicin E7 nuclease domain

2013 ◽  
Vol 18 (3) ◽  
pp. 309-321 ◽  
Author(s):  
Anikó Czene ◽  
Eszter Németh ◽  
István G. Zóka ◽  
Noémi I. Jakab-Simon ◽  
Tamás Körtvélyesi ◽  
...  
Keyword(s):  
Nuclease Domain ◽  
Colicin E7 ◽  
Terminal Loop

scholarly journals Fine tuning of the catalytic activity of colicin E7 nuclease domain by systematic N-terminal mutations

2014 ◽  
Vol 23 (8) ◽  
pp. 1113-1122 ◽  
Author(s):  
Eszter Németh ◽  
Tamás Körtvélyesi ◽  
Peter W. Thulstrup ◽  
Hans E. M. Christensen ◽  
Milan Kožíšek ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Fine Tuning ◽  
Nuclease Domain ◽  
Colicin E7

Fe-N-C Artificial Enzyme: Activation of Oxygen for Dehydrogenation and Monoxygenation of Organic Substrates under Mild Condition and Cancer Therapeutic Application

2018 ◽  
Author(s):  
Fei He ◽  
Li Mi ◽  
Yanfei Shen ◽  
Toshiyuki Mori ◽  
Songqin Liu ◽  
...  
Keyword(s):  
Mild Condition ◽  
Enzyme Activation ◽  
Artificial Enzymes ◽  
Organic Substrates ◽  
Artificial Enzyme ◽  
Therapeutic Application ◽  
Highly Efficient ◽  
Activation Of Oxygen

Developing highly efficient artificial enzymes that directly employ O<sub>2</sub> as terminal oxidant has long been pursued but has rarely achieved yet. We report Fe-N-C has unusual enzyme-like activity in both dehydrogenation and monoxygenation of organic substrates with ~100% selectivity by direct using O<sub>2</sub>.

scholarly journals A 160-bp Palindrome Is a Rad50·Rad32-Dependent Mitotic Recombination Hotspot inSchizosaccharomyces pombe

Genetics ◽  
2002 ◽  
Vol 161 (1) ◽  
pp. 461-468 ◽  
Author(s):  
Joseph A Farah ◽  
Edgar Hartsuiker ◽  
Ken-ichi Mizuno ◽  
Kunihiro Ohta ◽  
Gerald R Smith
Keyword(s):  
Secondary Structure ◽  
Schizosaccharomyces Pombe ◽  
Inverted Repeat ◽  
Mitotic Recombination ◽  
Genome Integrity ◽  
Recombination Hotspot ◽  
Nuclease Domain ◽  
Palindromic Sequences

AbstractPalindromic sequences can form hairpin and cruciform structures that pose a threat to genome integrity. We found that a 160-bp palindrome (an inverted repeat of 80 bp) conferred a mitotic recombination hotspot relative to a control nonpalindromic sequence when inserted into the ade6 gene of Schizosaccharomyces pombe. The hotspot activity of the palindrome, but not the basal level of recombination, was abolished by a rad50 deletion, by a rad50S “separation of function” mutation, or by a rad32-D25A mutation in the nuclease domain of the Rad32 protein, an Mre11 homolog. We propose that upon extrusion of the palindrome the Rad50·Rad32 nuclease complex recognizes and cleaves the secondary structure thus formed and generates a recombinogenic break in the DNA.

scholarly journals Single Nanoparticle to 3D Supercage: Framing for an Artificial Enzyme System

2015 ◽  
Vol 137 (43) ◽  
pp. 13957-13963 ◽  
Author(s):  
Ren Cai ◽  
Dan Yang ◽  
Shengjie Peng ◽  
Xigao Chen ◽  
Yun Huang ◽  
...  
Keyword(s):  
Enzyme System ◽  
Artificial Enzyme ◽  
Single Nanoparticle
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