Results 191 to 200 of about 256,046 (232)

13C-N.M.R. Studies on the pyrromethane cofactor of hydroxymethylbilane synthase

Tetrahedron Letters, 1988
By growing Escherichiacoli in the presence of 5-amino [5-13C] laevulinic acid, the enzyme hydroxymethylbilane synthase is produced carrying 13C-labels in its pyrromethane cofactor. It is then proved by 13C-n.m.r. spectroscopy that the cofactor is bound to the protein via the sulphur atom of a cysteine residue.
Uwe Beifuss, Graham J Hart, Andrew D Miller, Alan R Battersby   +3 more
openaire   +1 more source

Erythrocyte Hydroxymethylbilane Synthase Activity in a Chinese Family with Acute Intermittent Porphyria

Annals of Clinical Biochemistry: International Journal of Laboratory Medicine, 1988
Etude d'une famille chinoise avec analyse de l'activite enzymatique de l'uroporphyrinogen I synthase erythrocytaire et du porphobilinogen ...
F Y, Lee, K J, Hsiao, Y T, Tsai, S D, Lee, S J, Wu, H S, Jeng   +5 more
openaire   +2 more sources

Biallelic inactivation of protoporphyrinogen oxidase and hydroxymethylbilane synthase is associated with liver cancer in acute porphyrias.

Journal of Hepatology, 2015
Variegate porphyria (VP) and acute intermittent porphyria (AIP), the two most common types of acute porphyrias (AHPs), result from a partial deficiency of protoporphyrinogen oxidase (PPOX) and hydroxymethylbilane synthase (HMBS), respectively. A rare but serious complication in the AHPs is hepatocellular carcinoma (HCC).
X. Schneider-Yin, A. Van Tuyll van Serooskerken, M. Siegesmund, P. Went, Jasmin Barman-Aksözen, R. Bladergroen, P. Komminoth, R. Cloots, V. Winnepenninckx, A. zur Hausen, Markus Weber, A. Driessen, P. Poblete‐Gutiérrez, P. Bauer, C. Schroeder, M. van Geel, E. Minder, J. Frank   +17 more
semanticscholar   +3 more sources

Comparative inhibition of hepatic hydroxymethylbilane synthase by both hard and soft metal cations

Canadian Journal of Biochemistry and Cell Biology, 1984
The in vitro inhibition of hydroxymethylbilane synthase (EC 4.3.1.8, uroporphyrinogen I synthetase) obtained from livers of Sprague–Dawley rats has been studied with a wide range of di- and tri-valent metal ions. After purification by cell lysis, heat treatment, and centrifugation, the stable, soluble enzyme yielded sigmoidal inhibition curves with ...
D J, Farmer, B R, Hollebone
openaire   +2 more sources

Detection of DNA variations in the polymorphic hydroxymethylbilane synthase gene by high-resolution melting analysis

Analytical Biochemistry, 2009
Acute intermittent porphyria (AIP) represents the most frequent type of acute porphyria. The underlying cause is a defect in the hydroxymethylbilane synthase (HMBS) gene. Diagnosis of AIP is crucial for preventing life-threatening, acute attacks among both symptomatic and asymptomatic carriers.
Dana, Ulbrichova-Douderova, Pavel, Martasek   +1 more
openaire   +2 more sources

Molecular basis of acute intermittent porphyria: Mutations and polymorphisms in the human hydroxymethylbilane synthase gene

Human Mutation, 1994
Acute intermittent porphyria (AIP) is an autosomal dominant inborn error of metabolism that results from the half-normal activity of the third enzyme in the heme biosynthetic pathway, hydroxymethylbilane synthase (HMB-synthase). AIP is an ecogenetic condition, with life-threatening acute attacks precipitated by various factors including drugs, alcohol,
K H, Astrin, R J, Desnick
openaire   +2 more sources

A new synthesis of porphobilinogen analogues, inhibitors of hydroxymethylbilane synthase.

Organic & biomolecular chemistry, 2004
Two analogues of porphobilinogen, the 6-methyl and 6,11-ethano derivatives, have been made by a new synthetic route and the 6-methyl analogue has proved to be the most potent inhibitor of hydroxymethylbilane synthase yet reported (Ki = 3 microM).
Raef, Ahmed, Finian J, Leeper
openaire   +1 more source

A splicing mutation in the hydroxymethylbilane synthase gene in a Japanese family with acute intermittent porphyria

Clinical Biochemistry, 1999
Acute intermittent porphyria (AIP) is an autosomal dominant inherited disease caused by a decreased activity of hydroxymethylbilane synthase (HMBS). As far as the gene abnormalities of the HMBS, many different mutations have been reported. In this work, we investigated the presence of mutations in a Japanese family with AIP.A 44-year-old Japanese male ...
N, Maeda, Y, Horie, Y, Sasaki, E, Ueta, K, Adachi, E, Nanba, H, Kawasaki, Y, Kudo, M, Kondo   +8 more
openaire   +2 more sources

Crystal structure of the 2-iodoporphobilinogen-bound holo form of human hydroxymethylbilane synthase

, 2021
H. Sato, M. Sugishima, K. Wada, K. Hirabayashi, M. Tsukaguchi   +4 more
semanticscholar   +1 more source

Crystal structure of the ES2 intermediate form of human hydroxymethylbilane synthase

, 2021
H. Sato, M. Sugishima, K. Wada, K. Hirabayashi, M. Tsukaguchi   +4 more
semanticscholar   +1 more source