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5-Aminolevulinate synthase

Known as: Aminolevulinic Acid Synthetase, Synthetase, 5-Aminolevulinate, delta Aminolevulinate Synthase 
An enzyme of the transferase class that catalyzes condensation of the succinyl group from succinyl coenzyme A with glycine to form delta… Expand
National Institutes of Health

Related topics

Related topics

12 relations
5-aminolevulinate synthase activityALAS1 geneIn BloodProcess of secretion
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Narrower (2)

ALAS2 protein, humanProtoporphyria, Erythropoietic, X-Linked Dominant

Broader (1)

Acyltransferase

Papers overview

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Highly Cited
2007
Highly Cited
2007
Exercise-induced Mitochondrial Biogenesis Begins before the Increase in Muscle PGC-1α Expression*
Exercise results in rapid increases in expression of the transcription coactivator peroxisome proliferator-activated receptor… Expand
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Highly Cited
1995
Highly Cited
1995
Heme binds to a short sequence that serves a regulatory function in diverse proteins.
Heme is a prosthetic group for numerous enzymes, cytochromes and globins, and it binds tightly, sometimes covalently, to these… Expand
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Highly Cited
1993
Highly Cited
1993
Regulation by heme of mitochondrial protein transport through a conserved amino acid motif.
A conserved motif, termed the heme regulatory motif (HRM), was identified in the presequences of the erythroid delta… Expand
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Highly Cited
1991
Highly Cited
1991
Human erythroid 5‐aminolevulinate synthase: promoter analysis and identification of an iron‐responsive element in the mRNA.
5‐Aminolevulinate synthase (ALAS) catalyzes the first step of the heme biosynthetic pathway. cDNA clones for the human erythroid… Expand
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Highly Cited
1982
Highly Cited
1982
Heme biosynthesis in Rhizobium. Identification of a cloned gene coding for delta-aminolevulinic acid synthetase from Rhizobium meliloti.
A symbiotically important gene system in rhizobial species is the heme biosynthetic pathway. A mutant having reduced levels of… Expand
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Highly Cited
1975
Highly Cited
1975
Heme synthetase deficiency in human protoporphyria. Demonstration of the defect in liver and cultured skin fibroblasts.
The final step in heme biosynthesis is chelation of porphyrin with Fe++ catalyzed by the mitochondrial enzyme heme synthetase. We… Expand
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Highly Cited
1966
Highly Cited
1966
The induction in vitro of the synthesis of delta-aminolevulinic acid synthetase in chemical porphyria: a response to certain drugs, sex hormones, and foreign chemicals.
  • S. Granick
  • The Journal of biological chemistry
  • 1966
    • Corpus ID: 20808677
Abstract 1. A method is described for the primary growth of chick embryo liver cells on cover slips in culture, and the factors… Expand
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Highly Cited
1966
Highly Cited
1966
Delta-aminolevulinic acid synthetase. II. Induction in rat liver.
Abstract Administration of allylisopropylacetamide to rats causes a marked increase in the hepatic ribonucleic acid-dependent… Expand
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Highly Cited
1966
Highly Cited
1966
Delta-aminolevulinic acid synthetase. I. Studies in liver homogenates.
Abstract δ-Aminolevulinic acid synthesis has been demonstrated in both porphyric and normal liver homogenates. A study of the… Expand
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Highly Cited
1963
Highly Cited
1963
Increase in activity of alpha-aminolevulinic acid synthetase in liver mitochondria induced by feeding of 3,5-dicarbethoxy-1,4-dihydrocollidine.
 
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