Osmolytic Effect of Sucrose on Thermal Denaturation of Pea Seedling Copper Amine Oxidase

2017 ◽  
Vol 36 (2) ◽  
pp. 147-153 ◽  
Author(s):  
Mojtaba Amani ◽  
Aboozar Barzegar ◽  
Mohammad Mazani
Keyword(s):  
Thermal Denaturation ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Pea Seedling ◽  
Copper Amine

scholarly journals Molecular Cloning and Heterologous Expression of Pea Seedling Copper Amine Oxidase

2000 ◽  
Vol 64 (4) ◽  
pp. 717-722 ◽  
Author(s):  
Tomoyoshi KOYANAGI ◽  
Kiyoyuki MATSUMURA ◽  
Shun’ichi KURODA ◽  
Katsuyuki TANIZAWA
Keyword(s):  
Heterologous Expression ◽  
Molecular Cloning ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Pea Seedling ◽  
Copper Amine

scholarly journals Time-resolved analysis of catalytic reaction of copper amine oxidase fromArthrobacter globiformis

2011 ◽  
Vol 67 (a1) ◽  
pp. C225-C225
Author(s):  
H. Yamaguchi ◽  
M. Kataoka ◽  
H. Oya ◽  
A. Tominaga ◽  
M. Ohtsu ◽  
...  
Keyword(s):  
Catalytic Reaction ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Time Resolved ◽  
Copper Amine

Molecular cloning and characterization of copper amine oxidase from Huperzia serrata

2012 ◽  
Vol 22 (18) ◽  
pp. 5784-5790 ◽  
Author(s):  
Jieyin Sun ◽  
Hiroyuki Morita ◽  
Guoshen Chen ◽  
Hiroshi Noguchi ◽  
Ikuro Abe
Keyword(s):  
Molecular Cloning ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Huperzia Serrata ◽  
Copper Amine

scholarly journals Unique protonation states of aspartate and topaquinone in the active site of copper amine oxidase

RSC Advances ◽  
2020 ◽  
Vol 10 (63) ◽  
pp. 38631-38639
Author(s):  
Mitsuo Shoji ◽  
Takeshi Murakawa ◽  
Mauro Boero ◽  
Yasuteru Shigeta ◽  
Hideyuki Hayashi ◽  
...  
Keyword(s):  
Biogenic Amines ◽  
Active Site ◽  
Amine Oxidase ◽  
First Principle ◽  
Amine Oxidases ◽  
Oxidative Deamination ◽  
Copper Amine Oxidase ◽  
First Principle Calculations ◽  
Copper Amine Oxidases ◽  
Copper Amine

Copper amine oxidases catalyze the oxidative deamination of biogenic amines. We investigated the unique protonation states in the active site using first-principle calculations.

An Unexpected Role for the Active Site Base in Cofactor Orientation and Flexibility in the Copper Amine Oxidase fromHansenula polymorpha†

Biochemistry ◽  
1999 ◽  
Vol 38 (26) ◽  
pp. 8204-8216 ◽  
Author(s):  
Julie Plastino ◽  
Edward L. Green ◽  
Joann Sanders-Loehr ◽  
Judith P. Klinman
Keyword(s):  
Active Site ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Copper Amine

Lathyrus cicera copper amine oxidase reactions with tryptamine

2012 ◽  
Vol 109 ◽  
pp. 33-39 ◽  
Author(s):  
Paola Pietrangeli ◽  
Andrea Bellelli ◽  
Paola Fattibene ◽  
Bruno Mondovì ◽  
Laura Morpurgo
Keyword(s):  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Lathyrus Cicera ◽  
Copper Amine

Quantum mechanical hydrogen tunneling in bacterial copper amine oxidase reaction

2006 ◽  
Vol 342 (2) ◽  
pp. 414-423 ◽  
Author(s):  
Takeshi Murakawa ◽  
Toshihide Okajima ◽  
Shun’ichi Kuroda ◽  
Takuya Nakamoto ◽  
Masayasu Taki ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Quantum Mechanical ◽  
Hydrogen Tunneling ◽  
Copper Amine Oxidase ◽  
Oxidase Reaction ◽  
Copper Amine
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