Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
The quinone cofactor TPQ in copper amine oxidase is generated by posttranslational modification of an active site tyrosine residue. Using X-ray crystallography, we have probed the copper-dependent autooxidation process of TPQ in the enzyme from Arthrobacter globiformis. Apo enzyme crystals were anaerobically soaked with copper; the structure determined from this crystal provides a view of the initial state: the unmodified tyrosine coordinated to the bound copper. Exposure of the copper-bound crystals to oxygen led to the formation of freeze-trapped intermediates; structural analyses indicate that these intermediates contain dihydroxyphenylalanine quinone and trihydroxyphenylalanine. These are the first visualized intermediates during TPQ biogenesis in copper amine oxidase.
X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase.,Kim M, Okajima T, Kishishita S, Yoshimura M, Kawamori A, Tanizawa K, Yamaguchi H Nat Struct Biol. 2002 Aug;9(8):591-6. PMID:12134140[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kim M, Okajima T, Kishishita S, Yoshimura M, Kawamori A, Tanizawa K, Yamaguchi H. X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase. Nat Struct Biol. 2002 Aug;9(8):591-6. PMID:12134140 doi:http://dx.doi.org/10.1038/nsb824
