Lead poisoning, haem synthesis and 5-aminolaevulinic acid dehydratase

Martin J. Warren; Jon B. Cooper; Stephen P. Wood; Peter M. Shoolingin-jordan

doi:10.1016/S0968-0004(98)01219-5

Lead poisoning, haem synthesis and 5-aminolaevulinic acid dehydratase

Martin J. Warren, Jon B. Cooper, Stephen P. Wood, Peter M. Shoolingin-jordan

Institute of Life Sciences and Healthcare

Research output: Contribution to journal › Article › peer-review

Abstract

In mammals and yeast, 5-aminolaevulinic acid dehydratase is a zinc-dependent enzyme that catalyses the synthesis of porphobilinogen—the pyrrole building block that is incorporated into all modified tetrapyrroles, including haem, chlorophyll and vitamin B12. The X-ray structure of this enzyme reveals how substitution of the catalytically important zinc ion by lead inactivates the enzyme and causes a form of pseudo-porphyria.

Original language	English
Pages (from-to)	217-221
Journal	Trends in Biochemical Sciences
Volume	23
Issue number	6
DOIs	https://doi.org/10.1016/S0968-0004(98)01219-5
Publication status	Published - 1 Jun 1998

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title = "Lead poisoning, haem synthesis and 5-aminolaevulinic acid dehydratase",

abstract = "In mammals and yeast, 5-aminolaevulinic acid dehydratase is a zinc-dependent enzyme that catalyses the synthesis of porphobilinogen—the pyrrole building block that is incorporated into all modified tetrapyrroles, including haem, chlorophyll and vitamin B12. The X-ray structure of this enzyme reveals how substitution of the catalytically important zinc ion by lead inactivates the enzyme and causes a form of pseudo-porphyria.",

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AU - Warren, Martin J.

AU - Cooper, Jon B.

AU - Wood, Stephen P.

AU - Shoolingin-jordan, Peter M.

PY - 1998/6/1

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N2 - In mammals and yeast, 5-aminolaevulinic acid dehydratase is a zinc-dependent enzyme that catalyses the synthesis of porphobilinogen—the pyrrole building block that is incorporated into all modified tetrapyrroles, including haem, chlorophyll and vitamin B12. The X-ray structure of this enzyme reveals how substitution of the catalytically important zinc ion by lead inactivates the enzyme and causes a form of pseudo-porphyria.

AB - In mammals and yeast, 5-aminolaevulinic acid dehydratase is a zinc-dependent enzyme that catalyses the synthesis of porphobilinogen—the pyrrole building block that is incorporated into all modified tetrapyrroles, including haem, chlorophyll and vitamin B12. The X-ray structure of this enzyme reveals how substitution of the catalytically important zinc ion by lead inactivates the enzyme and causes a form of pseudo-porphyria.

U2 - 10.1016/S0968-0004(98)01219-5

DO - 10.1016/S0968-0004(98)01219-5

M3 - Article

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SP - 217

EP - 221

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

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Lead poisoning, haem synthesis and 5-aminolaevulinic acid dehydratase

Abstract

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