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Literature summary for 2.3.1.37 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

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

Cloned(Commentary)

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

General Stability

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

Inhibitors

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

Localization

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

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

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Gallus gallus
-
erythrocyte
-
Homo sapiens
-
liver
-
Gallus gallus
-
liver
-
Homo sapiens
-
liver
-
Rattus norvegicus
-
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
-
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
-
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
-
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
-
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)

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

Cofactor

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