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2.3.1.37: 5-aminolevulinate synthase

This is an abbreviated version!
For detailed information about 5-aminolevulinate synthase, go to the full flat file.

Word Map on EC 2.3.1.37

Reaction

succinyl-CoA
+
glycine
=
5-aminolevulinate
 +
CoA
 +
CO2

Synonyms

5-ALA synthase, 5-ALAS, 5-aminolevulinate synthase, 5-aminolevulinate synthetase, 5-aminolevulinic acid synthase, 5-aminolevulinic acid synthetase, ALA, ALA synthase, ALA synthetase, ALA-S, ALAS, ALAS2, alpha-aminolevulinic acid synthase, aminolevulinate synthase, aminolevulinate synthase 2, aminolevulinate synthetase, aminolevulinic acid synthase, aminolevulinic acid synthase 2, aminolevulinic acid synthetase, aminolevulinic synthetase, delta-ALAS, delta-aminolevulinate synthase, delta-aminolevulinate synthetase, delta-aminolevulinic acid synthase, delta-aminolevulinic acid synthase 2, delta-aminolevulinic acid synthetase, delta-aminolevulinic synthetase, erythroid 5-aminolevulinate synthase, erythroid-specific 5-aminolevulinate synthase, Hem1, hemA, HemT, mALAS-2, sigma-aminolevulinate synthase, synthase, aminolevulinate, synthetase, aminolevulinate

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.37 5-aminolevulinate synthase

Expression

Expression on EC 2.3.1.37 - 5-aminolevulinate synthase

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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
analysis of the 5' regulatory region of 5-aminolevulinate synthase gene in variegate porphyria patients heterozygous for the causative R59W mutation in the protoporphyrinogen oxidase gene. In the presence of estrogen and ERalpha, the wild-type -853C/-1253T allele induces a 47% increase in transcription, while the -853T/-1253A double mutant allele showed a 35% increase in transcription. The highest induction is observed for the mutant -853T/1253T allele generating an increase of 66%
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elevated mRNA and protein levels of isoform ALAS2 are observed among patients with erythropoietic protoporphyria. Iron deprivation increases the amount of isoform ALAS2 mRNA
enzyme expressions is significantly increased in the stomach after Vibrio parahaemolyticus infection
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fasting (starvation) induces enzyme activity. Griseofulvin induces enzyme mRNA expression after 2 days of treatment
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hemT expression is strongly upregulated under anaerobic-dark growth conditions when cells are respiring dimethyl sulfoxide, versus aerobic-dark or phototrophic (anaerobic-light) conditions
HIF1R knockdown by RNA interference decreased the level of ALAS2 expression. In silico analysis reveal three potential hypoxia-response elements (HREs) that are located 611, 621, and 741 bp downstream of the ALAS2 gene
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in mouse model of erythropoietic protoporphyria, isoflurane induces 5-aminolevulinate synthase activity and increases excretion of porphyrin precursors
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increased expression of erythroid specific 5-aminolevulinate synthase ALAS2 and gamma-globin mRNAs after 48 h of hypoxia. Exogenous TGF-beta1 induces hemoglobinization and the expression of ALAS2 mRNA in YN-1-0-A cells, but not of c-globin and mitoferrin mRNAs. A specific inhibitor of intracellular TGF-b signaling markedly reduces the degree of the hypoxia-mediated increase in the expression of ALAS2 mRNA in YN-1-0-A cells
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the enzyme activity is negatively regulated by heme in various ways, such as the repression of enzyme gene expression, degradation of enzyme mRNA, and inhibition of mitochondrial translocation of the mammalian precursor protein
the enzyme expression decreases significantly with age in the hepatopancreas and intestine
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the enzyme is negatively regulated by heme at the level of mitochondrial import
the presence of low-activity mitochondrial AAA+ unfoldase CLPX increases the posttranslational stability of the enzyme, causing increased protein level
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the relative expression of ALAS1 mRNA, the first and rate-limiting enzyme for heme biosynthesis under normal physiological conditions, is significantly reduced by nearly 90% in patients with Alzheimer's disease compared to control. The relative expression of porphobilinogen deaminase mRNA, the third enzyme in the heme synthesis pathway and a secondary rate-limiting enzyme in heme biosynthesis, is also significantly reduced by nearly 60% in brain of patients with Alzheimer's disease and significantly related to apolipoprotein E genotype. The relative expression of aminolevulinate dehydratase mRNA, the second and a non-rate-limiting enzyme for heme biosynthesis, is unchanged between the two groups
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under hypoxic conditions, significantly increased ALAS2 mRNA and protein levels are detected in K562 cells and erythroid induction cultures of CD34+ hematopoietic stem/progenitor cells
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