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

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Access to Document

10.1016/S0968-0004(98)01219-5

Cite this

@article{f71c2ea6c46e47acb7cc0ccafb27b85d,

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.",

author = "Warren, \{Martin J.\} and Cooper, \{Jon B.\} and Wood, \{Stephen P.\} and Shoolingin-jordan, \{Peter M.\}",

year = "1998",

month = jun,

day = "1",

doi = "10.1016/S0968-0004(98)01219-5",

language = "English",

volume = "23",

pages = "217--221",

journal = "Trends in Biochemical Sciences",

issn = "0968-0004",

publisher = "Elsevier Limited",

number = "6",

}

TY - JOUR

T1 - Lead poisoning, haem synthesis and 5-aminolaevulinic acid dehydratase

AU - Warren, Martin J.

AU - Cooper, Jon B.

AU - Wood, Stephen P.

AU - Shoolingin-jordan, Peter M.

PY - 1998/6/1

Y1 - 1998/6/1

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

SN - 0968-0004

VL - 23

SP - 217

EP - 221

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

IS - 6

ER -

Lead poisoning, haem synthesis and 5-aminolaevulinic acid dehydratase

Abstract

UN SDGs

Access to Document

Fingerprint

Cite this