Mutation of a Strictly Conserved, Active-Site Residue Alters Substrate Specificity and Cofactor Biogenesis in a Copper Amine Oxidase†

Biochemistry ◽  
1999 ◽  
Vol 38 (12) ◽  
pp. 3683-3693 ◽  
Author(s):  
Joan M. Hevel ◽  
Stephen A. Mills ◽  
Judith P. Klinman
Keyword(s):  
Substrate Specificity ◽  
Active Site ◽  
Amine Oxidase ◽  
Active Site Residue ◽  
Copper Amine Oxidase ◽  
Cofactor Biogenesis ◽  
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

scholarly journals X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase

2002 ◽  
Vol 58 (s1) ◽  
pp. c298-c298
Author(s):  
M. Kim ◽  
T. Okajima ◽  
S. Kishishita ◽  
M. Yoshimura ◽  
A. Kawamori ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
X Ray ◽  
Cofactor Biogenesis ◽  
Copper Amine

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

X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase

2002 ◽  
Author(s):  
Misa Kim ◽  
Toshihide Okajima ◽  
Seiichiro Kishishita ◽  
Megumi Yoshimura ◽  
Asako Kawamori ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
X Ray ◽  
Cofactor Biogenesis ◽  
Copper Amine

Tyrosine 381 in E. coli copper amine oxidase influences substrate specificity

2011 ◽  
Vol 118 (7) ◽  
pp. 1043-1053 ◽  
Author(s):  
Christian R. P. Kurtis ◽  
Peter F. Knowles ◽  
Mark R. Parsons ◽  
Thembaninkosi G. Gaule ◽  
Simon E. V. Phillips ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
E Coli ◽  
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.

Reinvestigation of Metal Ion Specificity for Quinone Cofactor Biogenesis in Bacterial Copper Amine Oxidase†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (36) ◽  
pp. 12041-12048 ◽  
Author(s):  
Toshihide Okajima ◽  
Sei'ichiro Kishishita ◽  
Yen-Chen Chiu ◽  
Takeshi Murakawa ◽  
Misa Kim ◽  
...  
Keyword(s):  
Metal Ion ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Ion Specificity ◽  
Cofactor Biogenesis ◽  
Copper Amine
Sign in / Sign up

Export Citation Format

Share Document