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

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.

scholarly journals Mutation at a Strictly Conserved, Active Site Tyrosine in the Copper Amine Oxidase Leads to Uncontrolled Oxygenase Activity

Biochemistry ◽  
2010 ◽  
Vol 49 (34) ◽  
pp. 7393-7402 ◽  
Author(s):  
Zhi-wei Chen ◽  
Saumen Datta ◽  
Jennifer L. DuBois ◽  
Judith P. Klinman ◽  
F. Scott Mathews
Keyword(s):  
Active Site ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Oxygenase Activity ◽  
Active Site Tyrosine ◽  
Copper Amine

High-resolution crystal structure of copper amine oxidase fromArthrobacter globiformis: assignment of bound diatomic molecules as O2

2013 ◽  
Vol 69 (12) ◽  
pp. 2483-2494 ◽  
Author(s):  
Takeshi Murakawa ◽  
Hideyuki Hayashi ◽  
Tomoko Sunami ◽  
Kazuo Kurihara ◽  
Taro Tamada ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Molecular Weight ◽  
Active Site ◽  
Amine Oxidase ◽  
Diatomic Molecules ◽  
Average Molecular Weight ◽  
Copper Amine Oxidase ◽  
Dimer Interface ◽  
Resolution Structure ◽  
Copper Amine

The crystal structure of a copper amine oxidase fromArthrobacter globiformiswas determined at 1.08 Å resolution with the use of low-molecular-weight polyethylene glycol (LMW PEG; average molecular weight ∼200) as a cryoprotectant. The final crystallographicRfactor andRfreewere 13.0 and 15.0%, respectively. Several molecules of LMW PEG were found to occupy cavities in the protein interior, including the active site, which resulted in a marked reduction in the overallBfactor and consequently led to a subatomic resolution structure for a relatively large protein with a monomer molecular weight of ∼70 000. About 40% of the presumed H atoms were observed as clear electron densities in theFo−Fcdifference map. Multiple minor conformers were also identified for many residues. Anisotropic displacement fluctuations were evaluated in the active site, which contains a post-translationally derived quinone cofactor and a Cu atom. Furthermore, diatomic molecules, most likely to be molecular oxygen, are bound to the protein, one of which is located in a region that had previously been proposed as an entry route for the dioxygen substrate from the central cavity of the dimer interface to the active site.

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

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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