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PDBsum entry 6l9c
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Oxidoreductase
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PDB id
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6l9c
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PDB id:
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| Name: |
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Oxidoreductase
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Title:
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Neutron structure of copper amine oxidase from arthrobacter glibiformis at pd 7.4
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Structure:
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Phenylethylamine oxidase. Chain: x. Synonym: primary amine oxidase. Engineered: yes
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Source:
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Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.14Å
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R-factor:
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0.168
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R-free:
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0.182
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Authors:
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T.Murakawa,K.Kurihara,M.Shoji,C.Shibazaki,T.Sunami,T.Tamada,N.Yano, T.Yamada,K.Kusaka,M.Suzuki,Y.Shigeta,R.Kuroki,H.Hayashi,Y.Yano, K.Tanizawa,M.Adachi,T.Okajima
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Key ref:
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T.Murakawa
et al.
(2020).
Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing.
Proc Natl Acad Sci U S A,
117,
10818-10824.
PubMed id:
DOI:
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Date:
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08-Nov-19
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Release date:
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29-Apr-20
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PROCHECK
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Headers
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References
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P46881
(PAOX_ARTGO) -
Phenylethylamine oxidase from Arthrobacter globiformis
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Seq:
Struc:
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638 a.a.
622 a.a.*
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Key: |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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Enzyme class:
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E.C.1.4.3.21
- primary-amine oxidase.
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Reaction:
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a primary methyl amine + O2 + H2O = an aldehyde + H2O2 + NH4+
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primary methyl amine
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+
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O2
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+
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H2O
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=
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aldehyde
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+
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H2O2
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+
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NH4(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proc Natl Acad Sci U S A
117:10818-10824
(2020)
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PubMed id:
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Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing.
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T.Murakawa,
K.Kurihara,
M.Shoji,
C.Shibazaki,
T.Sunami,
T.Tamada,
N.Yano,
T.Yamada,
K.Kusaka,
M.Suzuki,
Y.Shigeta,
R.Kuroki,
H.Hayashi,
T.Yano,
K.Tanizawa,
M.Adachi,
T.Okajima.
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ABSTRACT
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Recent advances in neutron crystallographic studies have provided structural
bases for quantum behaviors of protons observed in enzymatic reactions. Thus, we
resolved the neutron crystal structure of a bacterial copper (Cu) amine oxidase
(CAO), which contains a prosthetic Cu ion and a protein-derived redox cofactor,
topa quinone (TPQ). We solved hitherto unknown structures of the active site,
including a keto/enolate equilibrium of the cofactor with a nonplanar quinone
ring, unusual proton sharing between the cofactor and the catalytic base, and
metal-induced deprotonation of a histidine residue that coordinates to the Cu.
Our findings show a refined active-site structure that gives detailed
information on the protonation state of dissociable groups, such as the quinone
cofactor, which are critical for catalytic reactions.
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Links
