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1spu
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1SPU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with CU and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1SPU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with CU and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6]]. Structure known Active Sites: CUA, CUB, M1A, M1B, M2A and M2B. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SPU OCA]]. |
==Reference== | ==Reference== | ||
Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction., Wilmot CM, Murray JM, Alton G, Parsons MR, Convery MA, Blakeley V, Corner AS, Palcic MM, Knowles PF, McPherson MJ, Phillips SE, Biochemistry. 1997 Feb 18;36(7):1608-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9048544 9048544] | Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction., Wilmot CM, Murray JM, Alton G, Parsons MR, Convery MA, Blakeley V, Corner AS, Palcic MM, Knowles PF, McPherson MJ, Phillips SE, Biochemistry. 1997 Feb 18;36(7):1608-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9048544 9048544] | ||
| + | [[Category: Amine oxidase (copper-containing)]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tpq]] | [[Category: tpq]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:26:18 2007'' |
Revision as of 08:21, 30 October 2007
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STRUCTURE OF OXIDOREDUCTASE
Overview
The crystal structure of the complex between the copper amine oxidase from, Escherichia coli (ECAO) and a covalently bound inhibitor, 2-hydrazinopyridine, has been determined to a resolution of 2.0 A. The, inhibitor covalently binds at the 5 position of the quinone ring of the, cofactor, 2,4,5-trihydroxyphenylalaninequinone (TPQ). The inhibitor, complex is analogous to the substrate Schiff base formed during the, reaction with natural monoamine substrate. A proton is abstracted from a, methylene group adjacent to the amine group by a catalytic base during the, reaction. The inhibitor, however, has a nitrogen at this position, preventing proton abstraction and trapping the enzyme in a covalent, complex. The electron density shows this nitrogen is hydrogen bonded to, the side chain of ... [(full description)]
About this Structure
1SPU is a [Single protein] structure of sequence from [Escherichia coli] with CU and CA as [ligands]. Active as [Amine oxidase (copper-containing)], with EC number [1.4.3.6]. Structure known Active Sites: CUA, CUB, M1A, M1B, M2A and M2B. Full crystallographic information is available from [OCA].
Reference
Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction., Wilmot CM, Murray JM, Alton G, Parsons MR, Convery MA, Blakeley V, Corner AS, Palcic MM, Knowles PF, McPherson MJ, Phillips SE, Biochemistry. 1997 Feb 18;36(7):1608-20. PMID:9048544
Page seeded by OCA on Tue Oct 30 10:26:18 2007
