1eb3: Difference between revisions

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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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11513881 (full description)]]
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 [[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]].  
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]]


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