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HMBS encodes a member of the hydroxymethylbilane synthase superfamily. Additionally we are shipping Hydroxymethylbilane Synthase Antibodies (86) and Hydroxymethylbilane Synthase Proteins (12) and many more products for this protein.
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After a diagnostic odyssey, his urine porphobilinogen was found to be significantly elevated and genetic testing showed a previously unreported consensus splice-site mutation IVS4-1G>A in the HMBS gene confirming the diagnosis of Acute Intermittent Porphyria (AIP (show AIP ELISA Kits))
The authors describe the biochemical characterisation of expressed HMBS mutants in a black South African population. This reveals insight into the mechanism of catalytic activity loss, which may inspire investigation into individualised therapy based on the molecular lesion identified.
ALAS1 (show ALAS1 ELISA Kits) mRNA and activity were elevated approximately ~3- and 5-fold, and HMB synthase activity was approximately half-normal (~42%)
in the hepatic cancer tissue of two acute porphyria patients, somatic second-hit mutations result in nearly complete inactivation of PPOX (show OX ELISA Kits) and HMBS
study of hydroxymethylbilane synthase mutations and polymorphisms in Brazilian families with acute intermittent porphyria
Letter/Case Report: R173W mutation of HMBS gene can cause rhabdomyolysis in patients with variant acute intermittent porphyria.
we report a novel PBGD missense mutation.
Novel porphobilinogen deaminase gene mutations have been described in Polish patients with non-erythroid acute intermittent porphyria.
Conformational stability and activity of hydroxymethylbilane synthase (HMSB) and the acute intermittent porphyria K132N and V215E HMSB mutations.
Dense geographic aggregation with one identical haplotype strongly suggests a remote founder phenomenon for these Venezuelan acute intermittent porphyria families, carrying an unreported but most frequent HMBS mutation.
PBGD-deficient mice showed a different response to fasting as measured by altered carbohydrate metabolism in the liver and modified glucose consumption in the brain cortex. Glucose homeostasis in fasted PBGD-deficient mice was efficiently normalized after restoration of PBGD gene expression in the liver.
Porphobilinogen deaminase over-expression in hepatocytes, albeit in a low proportion, reduced precursor accumulation, which is the hallmark of acute porphyric attacks.
PBGD-deficient mice were characterized biochemically during phenobarbital induction of heme synthesis and enzyme replacement.
The interactions observed between the two pyrrole rings of the HEMC dipyrromethane cofactor and the active-site residues are highly specific and are most likely to represent the catalytically relevant binding mode.
Porphobilinogen deaminase deficiency alters vegetative and reproductive development and causes lesions in Arabidopsis.
Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Arabidopsis thaliana. [porphobilinogen deaminase]
This gene encodes a member of the hydroxymethylbilane synthase superfamily. The encoded protein is the third enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of four porphobilinogen molecules into the linear hydroxymethylbilane. Mutations in this gene are associated with the autosomal dominant disease acute intermittent porphyria. Alternatively spliced transcript variants encoding different isoforms have been described.
, porphyria, acute; Chester type
, pre-uroporphyrinogen synthase
, uroporphyrinogen I synthase
, uroporphyrinogen I synthetase
, alternative name: porphobilinogen deaminase
, hydroxymethylbilane synthase
, Hydroxymethylbilane synthase
, porphobilinogen deaminase-like
, Porphobilinogen deaminase