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The plastidic type II ferrochelatase contains a C-terminal chlorophyll a/b (CAB (zeige NPDC1 Proteine)) motif, a conserved hydrophobic stretch homologous to the CAB (zeige NPDC1 Proteine) domain of plant light- harvesting proteins.
The apparent surplus of FeCH activity in the wild type is critical for cell viability under high light due to a regulatory role of FeCH in the distribution of Chl (zeige CHRDL1 Proteine) into apoproteins.
Analysis of the recombinant full-length and truncated ferrochelatase (FeCH) demonstrated that the C-terminal extension is critical for activity of the FeCH and that it is strictly required for oligomerization of this enzyme.
5-aza-2'-deoxycytidine activates iron uptake and heme biosynthesis by increasing c-Myc (zeige MYC Proteine) nuclear localization and binding to the E-boxes of transferrin receptor 1 (zeige TFR Proteine) (TfR1 (zeige TFRC Proteine)) and ferrochelatase (Fech) genes.
analysis of the inhibitory metal ion-binding site in ferrochelatase
Fech forms an oligomeric complex with Mfrn1 (zeige SLC25A37 Proteine) and Abcb10 (zeige ABCB10 Proteine) to synergistically integrate mitochondrial iron importation and use for heme biosynthesis.
Ferrochelatase activity and protein levels were dramatically decreased in Irp2 (zeige IREB2 Proteine)(-/-) spleens, whereas ferrochelatase mRNA levels were increased, demonstrating posttranscriptional regulation of ferrochelatase in vivo
analysis of skin ferrochelatase and photosensitivity in mice and man
exon 10-deleted ferrochelatase heterozygous mice exhibited skin photosensitivity but no liver disease
analysis of the active site loop motif of murine ferrochelatase
hydrogen bonding between ferrochelatase and mesoporphyrin is a key factor in the thermodynamics of the binding reaction
Protoporphyric (Fech(m1pas)/Fech(m1pas) mice (C57BL/6J) showed a higher degree of liver pathology and more protoporphyrin accumulation than corresponding SJL/J and BALB/cJ mice. In the latter mice, mitochondrial respiratory chain activity was increased.
The kinetic mechanisms of inhibition of two variants of ferrochelatase by N-methylprotoporphyrin are reported.
the iron-removal reverse activity of FECH
FECH mRNA was largely significantly decreased in colon adenocarcinomas relative to normal colon tissues.
Using a forward chemical genetic approach, the authors identified the heme synthesis enzyme ferrochelatase (FECH) as necessary for angiogenesis in vitro and in vivo FECH is overexpressed in wet age-related macular degeneration eyes and murine choroidal neovascularization.
Using surface plasmon resonance, physiologically relevant concentrations of isatin (25-100 muM) were found to increase affinity of interactions between human recombinant ferrochelatase (FECH) and NADPH (zeige NQO1 Proteine)-dependent adrenodoxin reductase (ADR (zeige FDXR Proteine)).
In this study, QM/MM and quantum mechanical thermodynamic cycle perturbation free energy calculations were performed to investigate the porphyrin metalation in human ferrochelatase. It suggests a most reasonable pathway including the steps of the ferrous iron approaching from the site with Met76 coordinated and His263 playing the role of accepting proton.
These findings suggest that homozygous polymorphism of the FECH gene is associated with a slight elevation of the protoporphyrin level in erythrocytes, resulting in a mild EPP phenotype
a novel mutation, c.84G >A, in the FECH gene in four individuals with Erythropoietic Protoporphyria, is reported.
High ferrochelatase expression is associated with growth of malarial parasites in erythropoietic protoporphyria patients.
of ASO-V1 into developing human erythroblasts from an overtly EPP subject markedly increased the production of WT FECH mRNA and reduced the accumulation of PPIX to a level similar to that measured in asymptomatic EPP subjects
Sequence analysis of the FECH gene identified a novel missense mutation in exon 4 (c.418>A, G140R) of the FECH gene, as well as the common FECH IVS3-48 polymorphism in erythropoietic protoporphyria.
Loss-of-function FECH and gain-of-function erythroid-specific ALAS2 (zeige ALAS2 Proteine) mutations causing erythropoietic protoporphyria and x-linked protoporphyria in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria.
The protein encoded by this gene is localized to the mitochondrion, where it catalyzes the insertion of the ferrous form of iron into protoporphyrin IX in the heme synthesis pathway. Mutations in this gene are associated with erythropoietic protoporphyria. Two transcript variants encoding different isoforms have been found for this gene. A pseudogene of this gene is found on chromosome 3.
, ferrochelatase, mitochondrial
, heme synthase
, heme synthetase
, protoheme ferro-lyase