1dyu
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1DYU 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/ | + | 1DYU 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_(flavin-containing) Amine oxidase (flavin-containing)]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4]]. Structure known Active Sites: TPA and TPB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DYU OCA]]. |
==Reference== | ==Reference== | ||
The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants., Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, Phillips SE, McPherson MJ, Biochemistry. 1999 Jun 29;38(26):8217-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10387067 10387067] | The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants., Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, Phillips SE, McPherson MJ, Biochemistry. 1999 Jun 29;38(26):8217-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10387067 10387067] | ||
| + | [[Category: Amine oxidase (flavin-containing)]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: wildtype]] | [[Category: wildtype]] | ||
| - | ''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 10:33:01 2007'' |
Revision as of 08:28, 30 October 2007
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THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE: X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS.
Overview
Amine oxidases utilize a proton abstraction mechanism following binding of, the amine substrate to the C5 position of the cofactor, the quinone form, of trihydroxyphenylalanine (TPQ). Previous work [Wilmot, C. M., et al., (1997) Biochemistry 36, 1608-1620] has shown that Asp383 in Escherichia, coliamine oxidase (ECAO) is the catalytic base which performs the key step, of proton abstraction. This paper explores in more depth this and other, roles of Asp383. The crystal structures of three mutational variants are, presented together with their catalytic properties, visible spectra, and, binding properties for a substrate-like inhibitor, 2-hydrazinopyridine, (2-HP), in comparison to those of the wild type enzyme. In wild type ECAO, the TPQ is located in a wedge-shaped pocket which allows ... [(full description)]
About this Structure
1DYU is a [Single protein] structure of sequence from [Escherichia coli] with CU and CA as [ligands]. Active as [Amine oxidase (flavin-containing)], with EC number [1.4.3.4]. Structure known Active Sites: TPA and TPB. Full crystallographic information is available from [OCA].
Reference
The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants., Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, Phillips SE, McPherson MJ, Biochemistry. 1999 Jun 29;38(26):8217-27. PMID:10387067
Page seeded by OCA on Tue Oct 30 10:33:01 2007
