Role of a Strictly Conserved Active Site Tyrosine in Cofactor Genesis in the Copper Amine Oxidase fromHansenula polymorpha†

Biochemistry ◽  
2006 ◽  
Vol 45 (10) ◽  
pp. 3178-3188 ◽  
Author(s):  
Jennifer L. DuBois ◽  
Judith P. Klinman
Keyword(s):  
Active Site ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Active Site Tyrosine ◽  
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

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

Kinetic and Structural Studies on the Catalytic Role of the Aspartic Acid Residue Conserved in Copper Amine Oxidase†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (13) ◽  
pp. 4105-4120 ◽  
Author(s):  
Yen-Chen Chiu ◽  
Toshihide Okajima ◽  
Takeshi Murakawa ◽  
Mayumi Uchida ◽  
Masayasu Taki ◽  
...  
Keyword(s):  
Aspartic Acid ◽  
Amine Oxidase ◽  
Structural Studies ◽  
Copper Amine Oxidase ◽  
Aspartic Acid Residue ◽  
Catalytic Role ◽  
Copper Amine

scholarly journals The Copper Amine Oxidase AtCuAOδ Participates in Abscisic Acid-Induced Stomatal Closure in Arabidopsis

Plants ◽  
2019 ◽  
Vol 8 (6) ◽  
pp. 183 ◽  
Author(s):  
Ilaria Fraudentali ◽  
Sandip A. Ghuge ◽  
Andrea Carucci ◽  
Paraskevi Tavladoraki ◽  
Riccardo Angelini ◽  
...  
Keyword(s):  
Abscisic Acid ◽  
Amine Oxidase ◽  
Stomatal Closure ◽  
H2o2 Production ◽  
Amine Oxidases ◽  
Wild Type ◽  
Copper Amine Oxidase ◽  
Copper Amine Oxidases ◽  
Copper Amine

Plant copper amine oxidases (CuAOs) are involved in wound healing, defense against pathogens, methyl-jasmonate-induced protoxylem differentiation, and abscisic acid (ABA)-induced stomatal closure. In the present study, we investigated the role of the Arabidopsis thaliana CuAOδ (AtCuAOδ; At4g12290) in the ABA-mediated stomatal closure by genetic and pharmacological approaches. Obtained data show that AtCuAOδ is up-regulated by ABA and that two Atcuaoδ T-DNA insertional mutants are less responsive to this hormone, showing reduced ABA-mediated stomatal closure and H2O2 accumulation in guard cells as compared to the wild-type (WT) plants. Furthermore, CuAO inhibitors, as well as the hydrogen peroxide (H2O2) scavenger N,N1-dimethylthiourea, reversed most of the ABA-induced stomatal closure in WT plants. Consistently, AtCuAOδ over-expressing transgenic plants display a constitutively increased stomatal closure and increased H2O2 production compared to WT plants. Our data suggest that AtCuAOδ is involved in the H2O2 production related to ABA-induced stomatal closure.

Role of Copper Ion in Bacterial Copper Amine Oxidase:  Spectroscopic and Crystallographic Studies of Metal-Substituted Enzymes

2003 ◽  
Vol 125 (4) ◽  
pp. 1041-1055 ◽  
Author(s):  
Sei'ichiro Kishishita ◽  
Toshihide Okajima ◽  
Misa Kim ◽  
Hiroshi Yamaguchi ◽  
Shun Hirota ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Copper Ion ◽  
Copper Amine Oxidase ◽  
Copper Amine

Unprecedented Copper(II) Complex with a Topoquinone-like Moiety as a Structural and Functional Mimic for Copper Amine Oxidase: Role of Copper(II) in the Genesis and Amine Oxidase Activity

ACS Catalysis ◽  
2019 ◽  
Vol 9 (12) ◽  
pp. 10940-10950 ◽  
Author(s):  
Ritambhara Jangir ◽  
Mursaleem Ansari ◽  
Dhananjayan Kaleeswaran ◽  
Gopalan Rajaraman ◽  
Mallayan Palaniandavar ◽  
...  
Keyword(s):  
Oxidase Activity ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Amine Oxidase Activity ◽  
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.

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