1OHL

YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE PUTATIVE CYCLIC REACTION INTERMEDIATE COMPLEX

Summary for 1OHL

• Entry DOI: 10.2210/pdb1ohl/pdb
• Related: 1AW5 1EB3 1GJP 1H7N 1H7O 1H7P 1H7R 1QML 1QNV 1YLV
• Descriptor: DELTA-AMINOLEVULINIC ACID DEHYDRATASE, ZINC ION, BETA-MERCAPTOETHANOL, ... (5 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: 38154.93

Authors

Erskine, P.T.,Coates, L.,Butler, D.,Youell, J.H.,Brindley, A.A.,Wood, S.P.,Warren, M.J.,Shoolingin-Jordan, P.M.,Cooper, J.B. (deposition date: 2003-05-27, release date: 2003-06-02, Last modification date: 2023-12-13)

Primary citation

Erskine, P.T.,Coates, L.,Butler, D.,Youell, J.H.,Brindley, A.A.,Wood, S.P.,Warren, M.J.,Shoolingin-Jordan, P.M.,Cooper, J.B.
X-Ray Structure of a Putative Reaction Intermediateof 5-Aminolaevulinic Acid Dehydratase
Biochem.J., 373:733-, 2003

PubMed Abstract: The X-ray structure of yeast 5-aminolaevulinic acid dehydratase, in which the catalytic site of the enzyme is complexed with a putative cyclic intermediate composed of both substrate moieties, has been solved at 0.16 nm (1.6 A) resolution. The cyclic intermediate is bound covalently to Lys(263) with the amino group of the aminomethyl side chain ligated to the active-site zinc ion in a position normally occupied by a catalytic hydroxide ion. The cyclic intermediate is catalytically competent, as shown by its turnover in the presence of added substrate to form porphobilinogen. The findings, combined with those of previous studies, are consistent with a catalytic mechanism in which the C-C bond linking both substrates in the intermediate is formed before the C-N bond.

PubMed: 12777167
DOI: 10.1042/BJ20030513

Experimental method

X-RAY DIFFRACTION (1.6 Å)