X-ray structure of a putative reaction intermediate of 5-aminolaevulinic
acid dehydratase
X-ray structure of a putative reaction intermediate of 5-aminolaevulinic
acid dehydratase
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 Å) 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.
5-aminolaevulinic acid dehydratase, catalytic mechanism, reaction intermediate, trapped intermediate, X-raystructure.
733-738
Erskine, P.T.
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Coates, L.
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Butler, D.
cc1f7fe2-ee46-45cf-bb99-edf377b1460e
Youell, J.H.
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Brindley, A.A.
638ed87e-b0f7-4e74-9433-13bcde83aafc
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Warren, M.J.
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Shoolingin-Jordan, P.M.
ac0bf2cc-ee36-4b30-bcef-525cee2559f7
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
1 August 2003
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Coates, L.
2be36c11-8cb2-4518-a001-953051aa6a23
Butler, D.
cc1f7fe2-ee46-45cf-bb99-edf377b1460e
Youell, J.H.
a7e93bce-07e2-4b33-b9c4-d422eaa51bed
Brindley, A.A.
638ed87e-b0f7-4e74-9433-13bcde83aafc
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Warren, M.J.
6dc30bb6-c290-490e-8aab-44ad27c7c609
Shoolingin-Jordan, P.M.
ac0bf2cc-ee36-4b30-bcef-525cee2559f7
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Erskine, P.T., Coates, L., Butler, D., Youell, J.H., Brindley, A.A., Wood, S.P., Warren, M.J., Shoolingin-Jordan, P.M. and Cooper, J.B.
(2003)
X-ray structure of a putative reaction intermediate of 5-aminolaevulinic
acid dehydratase.
Biochemical Journal, 373 (3), .
(doi:10.1042/BJ20030513).
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 Å) 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.
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Published date: 1 August 2003
Keywords:
5-aminolaevulinic acid dehydratase, catalytic mechanism, reaction intermediate, trapped intermediate, X-raystructure.
Organisations:
Biological Sciences
Identifiers
Local EPrints ID: 24103
URI: http://eprints.soton.ac.uk/id/eprint/24103
ISSN: 1470-8728
PURE UUID: a0ab89aa-0c5a-475f-acc1-b308e126d499
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Date deposited: 22 Mar 2006
Last modified: 15 Mar 2024 06:52
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Contributors
Author:
P.T. Erskine
Author:
L. Coates
Author:
D. Butler
Author:
J.H. Youell
Author:
A.A. Brindley
Author:
S.P. Wood
Author:
M.J. Warren
Author:
J.B. Cooper
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