1eb3
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structures of 5-aminolaevulinic acid dehydratase complexed with two, irreversible inhibitors (4-oxosebacic acid and 4,7-dioxosebacic acid) have, been solved at high resolution. Both inhibitors bind by forming a Schiff, base link with Lys 263 at the active site. Previous inhibitor binding, studies have defined the interactions made by only one of the two, substrate moieties (P-side substrate) which bind to the enzyme during, catalysis. The structures reported here provide an improved definition of, the interactions made by both of the substrate molecules (A- and P-side, substrates). The most intriguing result is the novel finding that, 4,7-dioxosebacic acid forms a second Schiff base with the enzyme involving, Lys 210. It has been known for many years that P-side substrate forms a, .. | + | The structures of 5-aminolaevulinic acid dehydratase complexed with two, irreversible inhibitors (4-oxosebacic acid and 4,7-dioxosebacic acid) have, been solved at high resolution. Both inhibitors bind by forming a Schiff, base link with Lys 263 at the active site. Previous inhibitor binding, studies have defined the interactions made by only one of the two, substrate moieties (P-side substrate) which bind to the enzyme during, catalysis. The structures reported here provide an improved definition of, the interactions made by both of the substrate molecules (A- and P-side, substrates). The most intriguing result is the novel finding that, 4,7-dioxosebacic acid forms a second Schiff base with the enzyme involving, Lys 210. It has been known for many years that P-side substrate forms a, Schiff base (with Lys 263) but until now there has been no evidence that, binding of A-side substrate involves formation of a Schiff base with the, enzyme. A catalytic mechanism involving substrate linked to the enzyme, through Schiff bases at both the A- and P-sites is proposed. |
==About this Structure== | ==About this Structure== | ||
| - | 1EB3 is a | + | 1EB3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZN and DSB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EB3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:09:26 2007'' |
Revision as of 11:04, 5 November 2007
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YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE 4,7-DIOXOSEBACIC ACID COMPLEX
Overview
The structures of 5-aminolaevulinic acid dehydratase complexed with two, irreversible inhibitors (4-oxosebacic acid and 4,7-dioxosebacic acid) have, been solved at high resolution. Both inhibitors bind by forming a Schiff, base link with Lys 263 at the active site. Previous inhibitor binding, studies have defined the interactions made by only one of the two, substrate moieties (P-side substrate) which bind to the enzyme during, catalysis. The structures reported here provide an improved definition of, the interactions made by both of the substrate molecules (A- and P-side, substrates). The most intriguing result is the novel finding that, 4,7-dioxosebacic acid forms a second Schiff base with the enzyme involving, Lys 210. It has been known for many years that P-side substrate forms a, Schiff base (with Lys 263) but until now there has been no evidence that, binding of A-side substrate involves formation of a Schiff base with the, enzyme. A catalytic mechanism involving substrate linked to the enzyme, through Schiff bases at both the A- and P-sites is proposed.
About this Structure
1EB3 is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN and DSB as ligands. Active as Porphobilinogen synthase, with EC number 4.2.1.24 Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from OCA.
Reference
The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitors., Erskine PT, Coates L, Newbold R, Brindley AA, Stauffer F, Wood SP, Warren MJ, Cooper JB, Shoolingin-Jordan PM, Neier R, FEBS Lett. 2001 Aug 17;503(2-3):196-200. PMID:11513881
Page seeded by OCA on Mon Nov 5 13:09:26 2007
Categories: Porphobilinogen synthase | Saccharomyces cerevisiae | Single protein | Brindley, A.A. | Coates, L. | Cooper, J.B. | Erskine, P.T. | Neier, R. | Newbold, R. | Shoolingin-Jordan, P.M. | Stauffer, F. | Warren, M.J. | Wood, S.P. | DSB | ZN | Aldolase | Dehydratase | Tetrapyrrole synthesis | Tim barrel
