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… (More)
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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Review
2009
Review
2009
5-aminolevulinate synthase: catalysis of the first step of heme biosynthesis.
5-Aminolevulinate synthase is a homodimeric pyridoxal 5'-phosphate-dependent enzyme that catalyzes the first step of the heme… (More)
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2004
2004
Role of the heme regulatory motif in the heme-mediated inhibition of mitochondrial import of 5-aminolevulinate synthase.
5-Aminolevulinate synthase (ALAS) is a mitochondrial enzyme that catalyzes the first step of the heme biosynthetic pathway. The… (More)
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2002
2002
Transient state kinetic investigation of 5-aminolevulinate synthase reaction mechanism.
5-Aminolevulinate synthase (ALAS), a pyridoxal 5'-phosphate-dependent enzyme, catalyzes the first, and regulatory, step of the… (More)
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2000
2000
Transcriptional regulation of the murine erythroid-specific 5-aminolevulinate synthase gene.
5-Aminolevulinate synthase (ALAS) catalyzes the first step of the heme biosynthetic pathway in mammalian cells. Separate genes… (More)
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1999
1999
Pre-steady-state reaction of 5-aminolevulinate synthase. Evidence for a rate-determining product release.
5-Aminolevulinate synthase (ALAS) is the first enzyme of the heme biosynthetic pathway in non-plant eukaryotes and the alpha… (More)
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Review
1995
Review
1995
5-Aminolevulinate synthase and the first step of heme biosynthesis.
5-Aminolevulinate synthase catalyzes the condensation of glycine and succinyl-CoA to yield 5-aminolevulinate. In animals, fungi… (More)
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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… (More)
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Highly Cited
1992
Highly Cited
1992
Enzymatic defect in "X-linked" sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency.
Recently, the human gene encoding erythroid-specific delta-aminolevulinate synthase was localized to the chromosomal region Xp21… (More)
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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… (More)
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1989
1989
Expression of delta-aminolevulinate synthase in avian cells: separate genes encode erythroid-specific and nonspecific isozymes.
A controversy has existed in the literature for the past several years regarding the number of vertebrate genes encoding the… (More)
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