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The mutation in CLPX inactivates its ATPase activity, resulting in coassembly of mutant and WT protomers to form an enzyme with reduced activity. The presence of low-activity CLPX increases the posttranslational stability of ALAS, causing increased ALAS protein and ALA levels, leading to abnormal accumulation of PPIX.
the heme-binding site in the N-terminal region of the mature ALAS1 protein is also necessary for the heme-dependent oxidation of ALAS1.
ALAS1 mRNA and activity were elevated approximately ~3- and 5-fold, and HMB synthase activity was approximately half-normal (~42%)
The -853T variant functions as an enhancer in the presence of estrogen and speculates that the -1253A variant reduces transcription activity.
These results indicate that ALAS1 is a novel NR5A-target gene and participates in steroid hormone production.
Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells.
REVIEW:active site and mechanistic analysis, protein folding, structure and function.
REVIEW: mechanisms involving ALAS deficiency, point mutations, post translational processing, and complex formation with succinyl CoA synthetase subunit B in the pathogenesis of hereditary sideroblastic anemia.
ALAS expression is regulated by AP-1 complex through sequestration of cAMP-response element protein (CRE)-binding protein (CBP) coactivator in human cells
ALAS gene expression is regulated by Hepatic nuclear factor 3 and nuclear factor 1
First described frameshift ALAS2 mutation, CD506-507 (-C).
in the liver of Acute liver failure patients, there may be an increase in free heme concentration which down-regulating ALAS1 gene expression
Alternative splicing of human ALAS1 generates two mRNAs with different 5'-UTRs: a major one, where exon 1B is omitted, and a minor form containing exon 1B.
5-aminolevulinate synthase gene repression by the potent tumor promoter, TPA, involves multiple signal transduction pathways
Expression of candidate genes HPRT1 and ALAS1 in malignant and non-malignant prostate tissue samples after microdissection.
Differential regulation of human ALAS1 mRNA and protein levels by heme and cobalt protoporphyrin.
In this study, we show significant reductions of the rate-limiting enzymes involved in heme biosynthesis, ALAS1 in the postmortem cortex of Alzheimer's disease subjects, providing additional evidence of abnormal heme homeostasis in Alzheimer's disease.
RNAi-mediated silencing of hepatic Alas1 effectively prevents and treats the induced acute attacks in acute intermittent porphyria mice.
Both ALAS1 mRNA and protein content were induced in diabetic animals, accompanied by decreased Akt phosphorylation and increased nuclear FOXO1, PGC-1alpha and FOXO1-PGC-1alpha complex levels.
active site functional asymmetry extends to chimeric ALAS/AONS proteins, which while having a different oligomeric state, exhibit different rates of product release from the two ALAS and two AONS active sites due to the created intermolecular strain
Egr-1 regulates the transcriptional repression of mouse delta-aminolevulinic acid synthase 1 by heme
Mice bearing a homozygous knock-in allele were lethal by embryonic day 8.5, demonstrating that ALAS-N is essential for early embryogenesis.
Ser-254 is critical for formation of a competent catalytic complex by coupling succinyl-CoA binding to enzyme conformational equilibria
identified a drug-responsive enhancer in the ALAS1 gene
Histidine-282 impacts a variety of ALAS functions, including substrate and pyridoxal 5'-phosphate (PLP)-binding and catalysis.
5-aminolevulinate synthase operates under the stereoelectronic control predicted by Dunathan's hypothesis
The findings show that a B2 SINE retrotransposon can contribute to the regulation of ALAS1 and SINEs in 5'-UTR regions contribute to inter-individual differences in gene expression.
This gene encodes the mitochondrial enzyme which is catalyzes the rate-limiting step in heme (iron-protoporphyrin) biosynthesis. The enzyme encoded by this gene is the housekeeping enzyme\; a separate gene encodes a form of the enzyme that is specific for erythroid tissue. The level of the mature encoded protein is regulated by heme: high levels of heme down-regulate the mature enzyme in mitochondria while low heme levels up-regulate. A pseudogene of this gene is located on chromosome 12. Multiple alternatively spliced variants, encoding the same protein, have been identified.
5-aminolevulinate synthase, nonspecific, mitochondrial
, 5-aminolevulinic acid synthase 1
, delta-ALA synthase 1
, delta-aminolevulinate synthase 1
, migration-inducing protein 4
, aminolevulinate synthase H
, succinyl-CoA: glycine C-succinyl transferase
, 5-aminolevulinate synthase 1
, aminolevulinic acid synthase 1
, delta-ALA synthetase
, aminolevulinate, delta, synthase 1
, delta-ALA synthetase 1
, aminolevulinate, delta-, synthase 1
, Delta-ALA synthetase
, 5-aminolevulinate synthase, nonspecific, mitochondrial-like
, 5-aminolevulinic acid synthase
, alanyl-tRNA synthetase protein
, aminolevulinate synthase 1