1GJP

SCHIFF-BASE COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE WITH 4-OXOSEBACIC ACID

Summary for 1GJP

• Entry DOI: 10.2210/pdb1gjp/pdb
• Related: 1AW5 1EB3 1H7N 1H7O 1H7P 1H7R 1QML 1QNV 1YLV
• Descriptor: 5-AMINOLAEVULINIC ACID DEHYDRATASE, 4-OXODECANEDIOIC ACID, ZINC ION, ... (4 entities in total)
• Functional Keywords: lyase, dehydratase, aldolase, tim barrel, tetrapyrrole synthesis
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 1
• Total formula weight: 37823.58

Authors

Erskine, P.T.,Coates, L.,Newbold, R.,Brindley, A.A.,Wood, S.P.,Warren, M.J.,Cooper, J.B.,Shoolingin-Jordan, P.M.,Neier, R. (deposition date: 2001-08-01, release date: 2001-08-02, Last modification date: 2024-11-13)

Primary citation

Erskine, P.T.,Coates, L.,Newbold, R.,Brindley, A.A.,Stauffer, F.,Wood, S.P.,Warren, M.J.,Cooper, J.B.,Shoolingin-Jordan, P.M.,Neier, R.
The X-Ray Structure of Yeast 5-Aminolaevulinic Acid Dehydratase Complexed with Two Diacid Inhibitors
FEBS Lett., 503:196-, 2001

PubMed Abstract: 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.

PubMed: 11513881
DOI: 10.1016/S0014-5793(01)02721-1

Experimental method

X-RAY DIFFRACTION (1.8 Å)