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Literature summary extracted from

  • Ferreira, G.C.; Gong, J.
    5-Aminolevulinate synthase and the first step of heme biosynthesis (1995), J. Bioenerg. Biomembr., 27, 151-159.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.37 2-allyl-2-isopropylacetamide strong induction of enzyme in liver Gallus gallus
2.3.1.37 2-allyl-2-isopropylacetamide strong induction of enzyme in liver Rattus norvegicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.37
-
 Sinorhizobium meliloti
2.3.1.37
-
 Mus musculus
2.3.1.37
-
 Cereibacter sphaeroides
2.3.1.37
-
 Bradyrhizobium japonicum
2.3.1.37
-
 Rhodobacter capsulatus
2.3.1.37 cDNA from erythroid genetic library Gallus gallus
2.3.1.37 gene hem, functional complementation of Saccharomyces cerevisiae hem1 mutant Saccharomyces cerevisiae
2.3.1.37 liver and erythroid enzyme Homo sapiens
2.3.1.37 liver enzyme Rattus norvegicus

General Stability

EC Number General Stability Organism
2.3.1.37 enzyme is susceptible to proteolytic degradation during isolation, tendency to form aggregates Gallus gallus
2.3.1.37 enzyme is susceptible to proteolytic degradation during isolation, tendency to form aggregates Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.37 hemin
-
 Cereibacter sphaeroides
2.3.1.37 hemin inhibition of the import of the enzyme into the mitochondrial matrix Gallus gallus
2.3.1.37 hemin inhibition of the import of the enzyme into the mitochondrial matrix Homo sapiens
2.3.1.37 hemin inhibition of the import of the enzyme into the mitochondrial matrix Mus musculus
2.3.1.37 hemin
-
 Paracoccus denitrificans
2.3.1.37 hemin inhibition of the import of the enzyme into the mitochondrial matrix Rattus norvegicus
2.3.1.37 hemin inhibition of the import of the enzyme into the mitochondrial matrix Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.37 mitochondrion
-
 Gallus gallus 5739
-
2.3.1.37 mitochondrion
-
 Homo sapiens 5739
-
2.3.1.37 mitochondrion
-
 Rattus norvegicus 5739
-
2.3.1.37 mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.37 additional information
-
 amino acid sequence alignment Gallus gallus
2.3.1.37 additional information
-
 amino acid sequence alignment Paracoccus denitrificans
2.3.1.37 additional information
-
 amino acid sequence alignment Mus musculus
2.3.1.37 additional information
-
 amino acid sequence alignment Homo sapiens
2.3.1.37 additional information
-
 amino acid sequence alignment Rattus norvegicus
2.3.1.37 additional information
-
 amino acid sequence alignment Saccharomyces cerevisiae
2.3.1.37 additional information
-
 amino acid sequence alignment Aspergillus nidulans
2.3.1.37 additional information
-
 amino acid sequence alignment Cereibacter sphaeroides
2.3.1.37 additional information
-
 amino acid sequence alignment Bradyrhizobium japonicum
2.3.1.37 additional information
-
 amino acid sequence alignment Rhodobacter capsulatus
2.3.1.37 additional information
-
 amino acid sequence alignment Agrobacterium tumefaciens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.37 succinyl-CoA + glycine Gallus gallus regulatory mechanisms in hepatic and erythroid cells 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine Mus musculus regulatory mechanisms in hepatic and erythroid cells 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine Homo sapiens regulatory mechanisms in hepatic and erythroid cells 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine Rattus norvegicus regulatory mechanisms in hepatic and erythroid cells 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine Saccharomyces cerevisiae regulatory mechanisms in hepatic and erythroid cells 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine Cereibacter sphaeroides regulatory mechanisms in hepatic and erythroid cells 5-aminolevulinate + CoA + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.37 Agrobacterium tumefaciens
-
-
-
2.3.1.37 Aspergillus nidulans
-
-
-
2.3.1.37 Bradyrhizobium japonicum
-
-
-
2.3.1.37 Cereibacter sphaeroides
-
-
-
2.3.1.37 Euglena gracilis
-
-
-
2.3.1.37 Gallus gallus
-
-
-
2.3.1.37 Homo sapiens
-
-
-
2.3.1.37 Mus musculus
-
-
-
2.3.1.37 Paracoccus denitrificans
-
 i.e. Paracoccus denitrificans
-
2.3.1.37 Rattus norvegicus
-
-
-
2.3.1.37 Rhodobacter capsulatus
-
-
-
2.3.1.37 Saccharomyces cerevisiae
-
-
-
2.3.1.37 Sinorhizobium meliloti
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 mechanism Gallus gallus
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 mechanism Paracoccus denitrificans
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 mechanism Mus musculus
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 mechanism Homo sapiens
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 mechanism Rattus norvegicus
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 mechanism Saccharomyces cerevisiae
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 mechanism Euglena gracilis
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 mechanism Cereibacter sphaeroides
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 cysteine in heme-regulatory motif Mus musculus
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 pyridoxal 5'-phosphate binding site, sequence and function of glycine-rich motif Mus musculus
a
2.3.1.37 succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 ordered bi-bi mechanism in which glycine binds first and 5-aminolevulinic acid dissociates last Cereibacter sphaeroides
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.37 erythrocyte
-
 Gallus gallus
-
2.3.1.37 erythrocyte
-
 Homo sapiens
-
2.3.1.37 liver
-
 Gallus gallus
-
2.3.1.37 liver
-
 Homo sapiens
-
2.3.1.37 liver
-
 Rattus norvegicus
-
2.3.1.37 additional information enzyme is synthezised in the cytosol as the precursor protein and then imported into the mitochondria matrix and cleaved to the mature enzyme, the targeting information is encoded in nonoverlapping regions of the presequence Gallus gallus
-
2.3.1.37 additional information enzyme is synthezised in the cytosol as the precursor protein and then imported into the mitochondria matrix and cleaved to the mature enzyme, the targeting information is encoded in nonoverlapping regions of the presequence Mus musculus
-
2.3.1.37 additional information enzyme is synthezised in the cytosol as the precursor protein and then imported into the mitochondria matrix and cleaved to the mature enzyme, the targeting information is encoded in nonoverlapping regions of the presequence Homo sapiens
-
2.3.1.37 additional information enzyme is synthezised in the cytosol as the precursor protein and then imported into the mitochondria matrix and cleaved to the mature enzyme, the targeting information is encoded in nonoverlapping regions of the presequence Rattus norvegicus
-
2.3.1.37 additional information enzyme is synthezised in the cytosol as the precursor protein and then imported into the mitochondria matrix and cleaved to the mature enzyme, the targeting information is encoded in nonoverlapping regions of the presequence Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.37 succinyl-CoA + glycine
-
 Mus musculus 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine absolutely specific for glycine Gallus gallus 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine absolutely specific for glycine Paracoccus denitrificans 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine absolutely specific for glycine Homo sapiens 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine absolutely specific for glycine Rattus norvegicus 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine absolutely specific for glycine Saccharomyces cerevisiae 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine absolutely specific for glycine Euglena gracilis 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine absolutely specific for glycine Cereibacter sphaeroides 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine regulatory mechanisms in hepatic and erythroid cells Gallus gallus 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine regulatory mechanisms in hepatic and erythroid cells Mus musculus 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine regulatory mechanisms in hepatic and erythroid cells Homo sapiens 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine regulatory mechanisms in hepatic and erythroid cells Rattus norvegicus 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine regulatory mechanisms in hepatic and erythroid cells Saccharomyces cerevisiae 5-aminolevulinate + CoA + CO2
-
 ?
2.3.1.37 succinyl-CoA + glycine regulatory mechanisms in hepatic and erythroid cells Cereibacter sphaeroides 5-aminolevulinate + CoA + CO2
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.37 pyridoxal 5'-phosphate
-
 Sinorhizobium meliloti
2.3.1.37 pyridoxal 5'-phosphate
-
 Aspergillus nidulans
2.3.1.37 pyridoxal 5'-phosphate
-
 Bradyrhizobium japonicum
2.3.1.37 pyridoxal 5'-phosphate
-
 Rhodobacter capsulatus
2.3.1.37 pyridoxal 5'-phosphate
-
 Agrobacterium tumefaciens
2.3.1.37 pyridoxal 5'-phosphate required Gallus gallus
2.3.1.37 pyridoxal 5'-phosphate required Paracoccus denitrificans
2.3.1.37 pyridoxal 5'-phosphate required Mus musculus
2.3.1.37 pyridoxal 5'-phosphate required Homo sapiens
2.3.1.37 pyridoxal 5'-phosphate required Rattus norvegicus
2.3.1.37 pyridoxal 5'-phosphate required Saccharomyces cerevisiae
2.3.1.37 pyridoxal 5'-phosphate required Euglena gracilis
2.3.1.37 pyridoxal 5'-phosphate required Cereibacter sphaeroides