BRENDA - Enzyme Database show

5-Aminolevulinate synthase and the first step of heme biosynthesis

Ferreira, G.C.; Gong, J.; J. Bioenerg. Biomembr. 27, 151-159 (1995)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
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
Commentary
Organism
2.3.1.37
-
Bradyrhizobium japonicum
2.3.1.37
-
Mus musculus
2.3.1.37
-
Rhodobacter capsulatus
2.3.1.37
-
Rhodobacter sphaeroides
2.3.1.37
-
Sinorhizobium meliloti
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
Commentary
Organism
Structure
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
-
Rhodobacter sphaeroides
2.3.1.37
hemin
inhibition of the import of the enzyme into the mitochondrial matrix
Saccharomyces cerevisiae
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.3.1.37
mitochondrion
-
Gallus gallus
5739
-
2.3.1.37
mitochondrion
-
Rattus norvegicus
5739
-
2.3.1.37
mitochondrion
-
Saccharomyces cerevisiae
5739
-
2.3.1.37
mitochondrion
-
Homo sapiens
5739
-
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.3.1.37
additional information
-
amino acid sequence alignment
Agrobacterium tumefaciens
2.3.1.37
additional information
-
amino acid sequence alignment
Aspergillus nidulans
2.3.1.37
additional information
-
amino acid sequence alignment
Bradyrhizobium japonicum
2.3.1.37
additional information
-
amino acid sequence alignment
Gallus gallus
2.3.1.37
additional information
-
amino acid sequence alignment
Homo sapiens
2.3.1.37
additional information
-
amino acid sequence alignment
Mus musculus
2.3.1.37
additional information
-
amino acid sequence alignment
Paracoccus denitrificans
2.3.1.37
additional information
-
amino acid sequence alignment
Rattus norvegicus
2.3.1.37
additional information
-
amino acid sequence alignment
Rhodobacter capsulatus
2.3.1.37
additional information
-
amino acid sequence alignment
Rhodobacter sphaeroides
2.3.1.37
additional information
-
amino acid sequence alignment
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.3.1.37
succinyl-CoA + glycine
Gallus gallus
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Gallus gallus
?
2.3.1.37
succinyl-CoA + glycine
Mus musculus
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Mus musculus
?
2.3.1.37
succinyl-CoA + glycine
Homo sapiens
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Homo sapiens
?
2.3.1.37
succinyl-CoA + glycine
Rattus norvegicus
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Rattus norvegicus
?
2.3.1.37
succinyl-CoA + glycine
Saccharomyces cerevisiae
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Saccharomyces cerevisiae
?
2.3.1.37
succinyl-CoA + glycine
Rhodobacter sphaeroides
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Rhodobacter sphaeroides
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.3.1.37
Agrobacterium tumefaciens
-
-
-
2.3.1.37
Aspergillus nidulans
-
-
-
2.3.1.37
Bradyrhizobium japonicum
-
-
-
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
Rhodobacter sphaeroides
-
-
-
2.3.1.37
Saccharomyces cerevisiae
-
-
-
2.3.1.37
Sinorhizobium meliloti
-
-
-
Reaction
EC Number
Reaction
Commentary
Organism
2.3.1.37
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
Euglena gracilis
2.3.1.37
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
Gallus gallus
2.3.1.37
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
Homo sapiens
2.3.1.37
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
cysteine in heme-regulatory motif; mechanism; pyridoxal 5'-phosphate binding site, sequence and function of glycine-rich motif
Mus musculus
2.3.1.37
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
Paracoccus denitrificans
2.3.1.37
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
Rattus norvegicus
2.3.1.37
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism; ordered bi-bi mechanism in which glycine binds first and 5-aminolevulinic acid dissociates last
Rhodobacter sphaeroides
2.3.1.37
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
Saccharomyces cerevisiae
Source Tissue
EC Number
Source Tissue
Commentary
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
Saccharomyces cerevisiae
-
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
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
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
Rattus norvegicus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.3.1.37
succinyl-CoA + glycine
-
486850
Mus musculus
5-aminolevulinate + CoA + CO2
-
486850
Mus musculus
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Gallus gallus
5-aminolevulinate + CoA + CO2
-
486850
Gallus gallus
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Paracoccus denitrificans
5-aminolevulinate + CoA + CO2
-
486850
Paracoccus denitrificans
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Homo sapiens
5-aminolevulinate + CoA + CO2
-
486850
Homo sapiens
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Rattus norvegicus
5-aminolevulinate + CoA + CO2
-
486850
Rattus norvegicus
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Saccharomyces cerevisiae
5-aminolevulinate + CoA + CO2
-
486850
Saccharomyces cerevisiae
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Euglena gracilis
5-aminolevulinate + CoA + CO2
-
486850
Euglena gracilis
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Rhodobacter sphaeroides
5-aminolevulinate + CoA + CO2
-
486850
Rhodobacter sphaeroides
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Gallus gallus
5-aminolevulinate + CoA + CO2
-
486850
Gallus gallus
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Mus musculus
5-aminolevulinate + CoA + CO2
-
486850
Mus musculus
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Homo sapiens
5-aminolevulinate + CoA + CO2
-
486850
Homo sapiens
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Rattus norvegicus
5-aminolevulinate + CoA + CO2
-
486850
Rattus norvegicus
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Saccharomyces cerevisiae
5-aminolevulinate + CoA + CO2
-
486850
Saccharomyces cerevisiae
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Rhodobacter sphaeroides
5-aminolevulinate + CoA + CO2
-
486850
Rhodobacter sphaeroides
?
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
2.3.1.37
pyridoxal 5'-phosphate
-
Agrobacterium tumefaciens
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
required
Euglena gracilis
2.3.1.37
pyridoxal 5'-phosphate
required
Paracoccus denitrificans
2.3.1.37
pyridoxal 5'-phosphate
-
Rhodobacter capsulatus
2.3.1.37
pyridoxal 5'-phosphate
required
Rhodobacter sphaeroides
2.3.1.37
pyridoxal 5'-phosphate
-
Sinorhizobium meliloti
2.3.1.37
pyridoxal 5'-phosphate
required
Gallus gallus
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
Mus musculus
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
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) (protein specific)
EC Number
Commentary
Organism
2.3.1.37
-
Bradyrhizobium japonicum
2.3.1.37
-
Mus musculus
2.3.1.37
-
Rhodobacter capsulatus
2.3.1.37
-
Rhodobacter sphaeroides
2.3.1.37
-
Sinorhizobium meliloti
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
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
2.3.1.37
pyridoxal 5'-phosphate
-
Agrobacterium tumefaciens
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
required
Euglena gracilis
2.3.1.37
pyridoxal 5'-phosphate
required
Paracoccus denitrificans
2.3.1.37
pyridoxal 5'-phosphate
-
Rhodobacter capsulatus
2.3.1.37
pyridoxal 5'-phosphate
required
Rhodobacter sphaeroides
2.3.1.37
pyridoxal 5'-phosphate
-
Sinorhizobium meliloti
2.3.1.37
pyridoxal 5'-phosphate
required
Gallus gallus
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
Mus musculus
General Stability (protein specific)
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 (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
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
-
Rhodobacter sphaeroides
2.3.1.37
hemin
inhibition of the import of the enzyme into the mitochondrial matrix
Saccharomyces cerevisiae
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.3.1.37
mitochondrion
-
Gallus gallus
5739
-
2.3.1.37
mitochondrion
-
Rattus norvegicus
5739
-
2.3.1.37
mitochondrion
-
Saccharomyces cerevisiae
5739
-
2.3.1.37
mitochondrion
-
Homo sapiens
5739
-
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.3.1.37
additional information
-
amino acid sequence alignment
Agrobacterium tumefaciens
2.3.1.37
additional information
-
amino acid sequence alignment
Aspergillus nidulans
2.3.1.37
additional information
-
amino acid sequence alignment
Bradyrhizobium japonicum
2.3.1.37
additional information
-
amino acid sequence alignment
Gallus gallus
2.3.1.37
additional information
-
amino acid sequence alignment
Homo sapiens
2.3.1.37
additional information
-
amino acid sequence alignment
Mus musculus
2.3.1.37
additional information
-
amino acid sequence alignment
Paracoccus denitrificans
2.3.1.37
additional information
-
amino acid sequence alignment
Rattus norvegicus
2.3.1.37
additional information
-
amino acid sequence alignment
Rhodobacter capsulatus
2.3.1.37
additional information
-
amino acid sequence alignment
Rhodobacter sphaeroides
2.3.1.37
additional information
-
amino acid sequence alignment
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.3.1.37
succinyl-CoA + glycine
Gallus gallus
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Gallus gallus
?
2.3.1.37
succinyl-CoA + glycine
Mus musculus
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Mus musculus
?
2.3.1.37
succinyl-CoA + glycine
Homo sapiens
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Homo sapiens
?
2.3.1.37
succinyl-CoA + glycine
Rattus norvegicus
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Rattus norvegicus
?
2.3.1.37
succinyl-CoA + glycine
Saccharomyces cerevisiae
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Saccharomyces cerevisiae
?
2.3.1.37
succinyl-CoA + glycine
Rhodobacter sphaeroides
regulatory mechanisms in hepatic and erythroid cells
5-aminolevulinate + CoA + CO2
-
Rhodobacter sphaeroides
?
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
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
Saccharomyces cerevisiae
-
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
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
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
Rattus norvegicus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.3.1.37
succinyl-CoA + glycine
-
486850
Mus musculus
5-aminolevulinate + CoA + CO2
-
486850
Mus musculus
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Gallus gallus
5-aminolevulinate + CoA + CO2
-
486850
Gallus gallus
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Paracoccus denitrificans
5-aminolevulinate + CoA + CO2
-
486850
Paracoccus denitrificans
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Homo sapiens
5-aminolevulinate + CoA + CO2
-
486850
Homo sapiens
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Rattus norvegicus
5-aminolevulinate + CoA + CO2
-
486850
Rattus norvegicus
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Saccharomyces cerevisiae
5-aminolevulinate + CoA + CO2
-
486850
Saccharomyces cerevisiae
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Euglena gracilis
5-aminolevulinate + CoA + CO2
-
486850
Euglena gracilis
?
2.3.1.37
succinyl-CoA + glycine
absolutely specific for glycine
486850
Rhodobacter sphaeroides
5-aminolevulinate + CoA + CO2
-
486850
Rhodobacter sphaeroides
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Gallus gallus
5-aminolevulinate + CoA + CO2
-
486850
Gallus gallus
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Mus musculus
5-aminolevulinate + CoA + CO2
-
486850
Mus musculus
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Homo sapiens
5-aminolevulinate + CoA + CO2
-
486850
Homo sapiens
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Rattus norvegicus
5-aminolevulinate + CoA + CO2
-
486850
Rattus norvegicus
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Saccharomyces cerevisiae
5-aminolevulinate + CoA + CO2
-
486850
Saccharomyces cerevisiae
?
2.3.1.37
succinyl-CoA + glycine
regulatory mechanisms in hepatic and erythroid cells
486850
Rhodobacter sphaeroides
5-aminolevulinate + CoA + CO2
-
486850
Rhodobacter sphaeroides
?