Results 11 to 20 of about 3,705 (210)

Structure and Mechanism of Action of Hydroxymethylbilane Synthase

CHIMIA, 1999
The structure and mode of action of a vital enzyme involved in the biosynthesis of tetrapyrroles have been studied by using modern crystallographic and pre-steady-state kinetic methods.
Alfons Hädener
doaj   +4 more sources

Bi-allelic hydroxymethylbilane synthase inactivation defines a homogenous clinico-molecular subtype of hepatocellular carcinoma. [PDF]

J Hepatol, 2022
Acute intermittent porphyria (AIP), caused by heterozygous germline mutations of the heme synthesis pathway enzyme HMBS (hydroxymethylbilane synthase), confers a high risk of hepatocellular carcinoma (HCC) development. Yet, the role of HMBS in liver tumorigenesis remains unclear.Herein, we explore HMBS alterations in a large series of 758 HCC cases ...
Molina L, Zhu J, Trépo E, Bayard Q, Amaddeo G, GENTHEP Consortium, Blanc JF, Calderaro J, Ma X, Zucman-Rossi J, Letouzé E.   +10 more
europepmc   +8 more sources

Plasmodium falciparum hydroxymethylbilane synthase does not house any cosynthase activity within the haem biosynthetic pathway. [PDF]

Microbiology (Reading), 2021
Abstract The production of uroporphyrinogen III, the universal progenitor of macrocyclic, modified tetrapyrroles, is produced from aminolaevulinic acid (ALA) by a conserved pathway involving three enzymes: porphobilinogen synthase (PBGS), hydroxymethylbilane synthase (HmbS) and uroporphyrinogen III synthase (UroS ...
Scott AF, Deery E, Lawrence AD, Warren MJ.   +3 more
europepmc   +12 more sources

Identification and characterization of 40 novel hydroxymethylbilane synthase mutations that cause acute intermittent porphyria [PDF]

Journal of Inherited Metabolic Disease, 2019
Abstract Acute intermittent porphyria (AIP), an autosomal dominant disorder due to the half‐normal activity of hydroxymethylbilane synthase (HMBS), is characterized by acute neurovisceral attacks that are precipitated by factors that induce heme biosynthesis.
Angelika L Erwin, Manisha Balwani, John D Phillips   +2 more
exaly   +5 more sources

Novel hydroxymethylbilane synthase gene mutation identified and confirmed in a woman with acute intermittent porphyria: A case report. [PDF]

World J Clin Cases, 2022
Acute intermittent porphyria (AIP) is a rare autosomal dominant porphyrin metabolic disease caused by a mutation in the hydroxymethylbilane synthase (HMBS) gene. This study aimed to explore the clinical manifestations of a patient with AIP, to identify a novel HMBS gene mutation in the proband and some of her family members, and to confirm the ...
Zhou YQ, Wang XQ, Jiang J, Huang SL, Dai ZJ, Kong QQ.   +5 more
europepmc   +4 more sources

A novel 3-base deletion (IVS3+2_4delTGG) of the hydroxymethylbilane synthase gene in a Brazilian patient with acute intermittent porphyria [PDF]

Genetics and Molecular Biology, 2007
Acute intermittent porphyria (AIP, OMIM 176000) is an autosomal dominant metabolic disease caused by mutations in the gene encoding hydroxymethylbilane synthase (HMBS; EC 4.3.1.8; formely named porphobilinogen deaminase, PBGD), mapped to chromosome 11q23.
Georgina Severo Ribeiro, Paulo Eurípedes Marchiori, Mário Hiroyuki Hirata, Ivanise Rebecchi, Adriana Natsue Ozaki, Maria Aparecida Nagai, Mariana Lopes dos Santos, Raimundo Antonio Gomes Oliveira, Orlando Cesar de Oliveira Barretto   +8 more
doaj   +2 more sources

Hydroxymethylbilane Synthase Gene Mutation: The Hidden Driver of Abdominal Pain and Neurological Symptoms in Acute Intermittent Porphyria

Journal of Applied Hematology
Mutations in the hydroxymethylbilane synthase (HMBS) gene can lead to a deficiency of the HMBS enzyme, allowing porphyrins to accumulate to toxic levels in the liver and other organs, leading to acute intermittent porphyria (AIP).
Abeer Zakariyah*, Rahaf Alzahrani, Iman Alhazmi, Alia Abotaleb, Mohammed Alasmari, Abdulrahim Basendwah, Rasha Alsubaie, Muhammad Sohaib Khan, Leena Alnajjar, Sultan Altouri   +9 more
doaj   +2 more sources

Crystal structures of hydroxymethylbilane synthase complexed with a substrate analog: a single substrate-binding site for four consecutive condensation steps. [PDF]

Biochem J, 2021
Sato H, Sugishima M, Tsukaguchi M, Masuko T, Iijima M, Takano M, Omata Y, Hirabayashi K, Wada K, Hisaeda Y, Yamamoto K.   +10 more
europepmc   +3 more sources

Human hydroxymethylbilane synthase: Molecular dynamics of the pyrrole chain elongation identifies step-specific residues that cause AIP. [PDF]

Proc Natl Acad Sci U S A, 2018
Bung N, Roy A, Chen B, Das D, Pradhan M, Yasuda M, New MI, Desnick RJ, Bulusu G.   +8 more
europepmc   +3 more sources

A novel 55-basepair deletion of hydroxymethylbilane synthase gene found in a Chinese patient with acute intermittent porphyria and her family: A case report. [PDF]

Medicine (Baltimore), 2018
Ren Y, Xu LX, Liu YF, Xiang CY, Gao F, Wang Y, Bai T, Yin JH, Zhao YL, Yang J.   +9 more
europepmc   +2 more sources