1bug
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Catechol oxidases are ubiquitous plant enzymes containing a dinuclear | + | Catechol oxidases are ubiquitous plant enzymes containing a dinuclear copper center. In the wound-response mechanism of the plant they catalyze the oxidation of a broad range of ortho-diphenols to the corresponding o-quinones coupled with the reduction of oxygen to water. The crystal structures of the enzyme from sweet potato in the resting dicupric Cu(II)-Cu(II) state, the reduced dicuprous Cu(I)-Cu(I) form, and in complex with the inhibitor phenylthiourea were analyzed. The catalytic copper center is accommodated in a central four-helix-bundle located in a hydrophobic pocket close to the surface. Both metal binding sites are composed of three histidine ligands. His 109, ligated to the CuA site, is covalently linked to Cys 92 by an unusual thioether bond. Based on biochemical, spectroscopic and the presented structural data, a catalytical mechanism is proposed in which one of the oxygen atoms of the diphenolic substrate binds to CuB of the oxygenated enzyme. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Klabunde, T.]] | [[Category: Klabunde, T.]] | ||
[[Category: Krebs, B.]] | [[Category: Krebs, B.]] | ||
| - | [[Category: Sacchettini, J | + | [[Category: Sacchettini, J C.]] |
[[Category: CU]] | [[Category: CU]] | ||
[[Category: URS]] | [[Category: URS]] | ||
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[[Category: ipomoea batatas]] | [[Category: ipomoea batatas]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:14 2008'' |
Revision as of 09:59, 21 February 2008
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CATECHOL OXIDASE FROM IPOMOEA BATATAS (SWEET POTATOES)-INHIBITOR COMPLEX WITH PHENYLTHIOUREA (PTU)
Overview
Catechol oxidases are ubiquitous plant enzymes containing a dinuclear copper center. In the wound-response mechanism of the plant they catalyze the oxidation of a broad range of ortho-diphenols to the corresponding o-quinones coupled with the reduction of oxygen to water. The crystal structures of the enzyme from sweet potato in the resting dicupric Cu(II)-Cu(II) state, the reduced dicuprous Cu(I)-Cu(I) form, and in complex with the inhibitor phenylthiourea were analyzed. The catalytic copper center is accommodated in a central four-helix-bundle located in a hydrophobic pocket close to the surface. Both metal binding sites are composed of three histidine ligands. His 109, ligated to the CuA site, is covalently linked to Cys 92 by an unusual thioether bond. Based on biochemical, spectroscopic and the presented structural data, a catalytical mechanism is proposed in which one of the oxygen atoms of the diphenolic substrate binds to CuB of the oxygenated enzyme.
About this Structure
1BUG is a Single protein structure of sequence from Ipomoea batatas with and as ligands. Active as Catechol oxidase, with EC number 1.10.3.1 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
Crystal structure of a plant catechol oxidase containing a dicopper center., Klabunde T, Eicken C, Sacchettini JC, Krebs B, Nat Struct Biol. 1998 Dec;5(12):1084-90. PMID:9846879
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