Information on EC 2.3.1.37 - 5-aminolevulinate synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.3.1.37
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RECOMMENDED NAME
GeneOntology No.
5-aminolevulinate synthase
PATHWAY
KEGG Link
MetaCyc Link
Glycine, serine and threonine metabolism
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Metabolic pathways
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Porphyrin and chlorophyll metabolism
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tetrapyrrole biosynthesis II (from glycine)
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SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA:glycine C-succinyltransferase (decarboxylating)
A pyridoxal-phosphate protein. The enzyme in erythrocytes is genetically distinct from that in other tissues.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5-aminolevulinate synthase
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5-aminolevulinate synthase
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5-aminolevulinate synthase
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5-aminolevulinate synthetase
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-
-
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5-aminolevulinic acid synthetase
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-
-
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ALA synthase
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-
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ALA synthase
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ALA synthase
Rattus norvegicus Sprague-Dawley
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-
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ALA synthetase
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-
-
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ALA-S
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ALA-S
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ALAS
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-
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ALAS
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ALAS
Rattus norvegicus Sprague-Dawley
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-
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ALAS2
P22557
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alpha-aminolevulinic acid synthase
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-
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aminolevulinate synthase
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aminolevulinate synthetase
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aminolevulinic acid synthase
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aminolevulinic acid synthetase
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-
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aminolevulinic synthetase
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-
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delta-ALAS
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delta-aminolevulinate synthase
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-
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delta-aminolevulinate synthase
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delta-aminolevulinate synthase
Rattus norvegicus Sprague-Dawley
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-
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delta-aminolevulinate synthetase
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-
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delta-aminolevulinic acid synthase
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-
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delta-aminolevulinic acid synthetase
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-
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delta-aminolevulinic synthetase
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mALAS-2
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mature form of the murine erythroid specific isoform of aminolevulinate synthase
sigma-aminolevulinate synthase
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sigma-aminolevulinate synthase
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sigma-aminolevulinate synthase
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synthase, aminolevulinate
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synthetase, aminolevulinate
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CAS REGISTRY NUMBER
COMMENTARY
9037-14-3
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
2 isoforms ALAS-1 and ALAS-2, a houskeeping form and an erythroid-specific form
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-
Manually annotated by BRENDA team
animals after acetylphenylhydrazine-induced anemia
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-
Manually annotated by BRENDA team
2 isoforms ALAS-1 and ALAS-2, a houskeeping form and an erythroid-specific form
-
-
Manually annotated by BRENDA team
isoform ALAS1
Uniprot
Manually annotated by BRENDA team
major splice variant of enzyme isoform ALAS2, expression in Escherichia coli
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-
Manually annotated by BRENDA team
2 isoforms ALAS-1 and ALAS-2, a houskeeping form and an erythroid-specific form
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-
Manually annotated by BRENDA team
Albino male CF1
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-
Manually annotated by BRENDA team
erythroid specific isoform
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-
Manually annotated by BRENDA team
erythroid-specific isoform
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Manually annotated by BRENDA team
erythroid-specific isoform; gene ALAS-2
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-
Manually annotated by BRENDA team
erythroid-specific isoform; gene ALAS-2; hypoxia-inducible
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Manually annotated by BRENDA team
erythroid-specific isoform; gene ALAS-E
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Manually annotated by BRENDA team
gene hemA
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Manually annotated by BRENDA team
inducible in erythroleukemia cells
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-
Manually annotated by BRENDA team
no activity in Chromatium sp.
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-
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Manually annotated by BRENDA team
2 enzyme forms in cytosol and mitochondria
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-
Manually annotated by BRENDA team
i.e. Paracoccus denitrificans
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Manually annotated by BRENDA team
in cells grown anaerobically and in iron-containing nitrate medium, overview
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Manually annotated by BRENDA team
2 isoenzymes: I, constitutive, and II, inducible related to bacteriochlorophyll formation and light conditions
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-
Manually annotated by BRENDA team
2 isoforms in cytosol and mitochondria
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-
Manually annotated by BRENDA team
drug-induced
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-
Manually annotated by BRENDA team
non-specific, housekeeping isoform ALAS-N and erythroid-specific isoform ALAS-E
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-
Manually annotated by BRENDA team
Sprague-Dawley
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-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
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-
Manually annotated by BRENDA team
2 isozymes; Y
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Manually annotated by BRENDA team
enzyme exists in an inactive or low activity form which can under certain conditions become activated, spontaneous activation in presence of oxygen or an oxidizing agent shows a pH dependence with an optimum at about pH 7.0, assisted by 2-mercaptoethanol
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Manually annotated by BRENDA team
expression in Escherichia coli
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Manually annotated by BRENDA team
Rhodobacter sphaeroides Y
Y
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Manually annotated by BRENDA team
strain KUGB306
Swissprot
Manually annotated by BRENDA team
Rhodopseudomonas palustris KUGB306
strain KUGB306
Swissprot
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion, crystal structure of full-length homodimeric enzyme binding its cofactor pyridoxal 5'-phosphate at 2.1 A, and structures of the enzyme in complex with the substrates glycine or succinyl-coenzyme A at 2.7 A and 2.8 A, respectivel
P18079