Results 181 to 190 of about 3,705 (210)

Acute intermittent porphyria: thein vitroexpression of mutant hydroxymethylbilane synthase

Molecular and Cellular Probes, 1997
Acute intermittent porphyria (AIP) is an inborn error of haem biosynthesis caused by a variety of mutations in the gene coding for hydroxymethylbilane synthase (HMB-S). The entire coding sequence of this gene, from each of three South African AIP patients, was therefore screened for mutations using chemical cleavage mismatch (CCM) analysis and any ...
Michael R Moore
exaly   +5 more sources

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Computational modeling of the catalytic mechanism of hydroxymethylbilane synthase

Physical Chemistry Chemical Physics, 2019
Hydroxymethylbilane synthase (HMBS), the third enzyme in the heme biosynthesis pathway, catalyzes the formation of 1-hydroxymethylbilane (HMB) by a stepwise polymerization of four molecules of porphobilinogen (PBG) using the dipyrromethane (DPM) cofactor.
Navneet Bung, Arijit Roy, U. Deva Priyakumar, Gopalakrishnan Bulusu   +3 more
openaire   +2 more sources

Interaction of 5-hydroxymethyl-furfural with hydroxymethylbilane synthase

Phytochemistry, 1997
Abstract The inhibition of chlorophyll biosynthesis in greening cress seedlings (Lepidium sativum L.) by 5-hydroxymethylfurfural (5-HMF), a natural compound isolated from the bulbs of Gladiolus spp. was investigated in vitro and in vivo. A direct reaction between 5-HMF and the chlorophyll precursor porphobilinogen was observed at pH 1.0 but not at pH
Joachim Wübert, Ulrike Oster, Wolfhart Rüdiger   +2 more
exaly   +2 more sources

Time-resolved and static-ensemble structural chemistry of hydroxymethylbilane synthase

Faraday Discuss., 2003
The enzyme hydroxymethylbilane synthase (HMBS, EC 4.3.1.8), 313 amino acid residues and MW 34 kDa, also known as porphobilinogen deaminase (PBGD), catalyses the stepwise polymerization of four molecules of porphobilinogen (PBG) to the linear tetrapyrrole 1-hydroxymethylbilane. Several crystallographic structures of HMBS have been previously determined,
John R, Helliwell, Yeu Perng, Nieh, Jarjis, Habash, Paul F, Faulder, James, Raftery, Michele, Cianci, Michael, Wulff, Alfons, Hädener   +7 more
openaire   +2 more sources

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

Acute Intermittent Porphyria: Heterogeneity of Mutations in the Hydroxymethylbilane Synthase Gene in Italy

Blood Cells, Molecules, and Diseases, 2001
Acute intermittent porphyria (AIP) is an autosomal disorder caused by molecular abnormalities in the gene coding for hydroxymethylbilane synthase (HMBS), the third enzyme in the heme biosynthetic pathway. So far, more than 170 different mutations responsible for AIP have been identified worldwide in the HMBS gene.
F. Martinez di Montemuros, E. Di Pierro, G. Biolcati, E. Rocchi, E. Bissolotti, D. Tavazzi, G. Fiorelli, M.D. Cappellini   +7 more
openaire   +4 more sources

19-Bromo-1-hydroxymethylbilane a novel inhibitor of Uro'gen III synthase

Bioorganic & Medicinal Chemistry, 1994
A novel hydroxymethylbilane analog, 19-Br-HMB (11), has been synthesized. Its activity with the enzyme Uro'gen III synthase shows competitive inhibition.
C, Pichon, B P, Atshaves, R, Danso-Danquah, N J, Stolowich, A I, Scott   +4 more
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Acute intermittent porphyria: alternative splicing of hydroxymethylbilane synthase mRNA excludes exons 3 and 12

Molecular and Cellular Probes, 1998
The hydroxymethylbilane synthase (HMBS) mRNAs from 44 control individuals and 30 patients suffering from acute intermittent porphyria (AIP), were screened for length differences by reverse transcriptase polymerase chain reaction (RT-PCR) and any abnormalities were characterized by direct sequencing.
Michael R Moore
exaly   +5 more sources

New mutations of the hydroxymethylbilane synthase gene in German patients with acute intermittent porphyria

Molecular and Cellular Probes, 1999
Acute intermittent porphyria (AIP) is a low-penetrant, autosomal dominant disorder caused by decreased activity of hydroxymethylbilane synthase (HMBS; MIM 176 000), the third enzyme in the heme biosynthetic pathway. We report the first molecular analysis of HMBS gene mutations in classical AIP patients of German origin.
U, Gross, H, Puy, M, Doss, A M, Robreau, Y, Nordmann, M O, Doss, J C, Deybach   +6 more
exaly   +3 more sources

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