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 hide
2.3.1.37
-
RECOMMENDED NAME
GeneOntology No.
5-aminolevulinate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
condensation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-amino-3-hydroxycyclopent-2-enone biosynthesis
-
-
Glycine, serine and threonine metabolism
-
-
heme metabolism
-
-
Metabolic pathways
-
-
Porphyrin and chlorophyll metabolism
-
-
tetrapyrrole biosynthesis II (from glycine)
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9037-14-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
no activity in Chromatium sp.
-
-
-
Manually annotated by BRENDA team
2 enzyme forms in cytosol and mitochondria
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
strain KUGB306
Swissprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
mutation in Alas gena cause massive water loss. The cuticle of alas mutant larvae detaches from the epidermis and its basal region is frayed. Reduction of Alas function results in weakening of the extracellular dityrosines network in the cuticle. Alas activity, which initiates heme biosynthesis in the mitochondrion, might be needed for the formation of a dityrosine-based barrier that confers resistance to the internal hydrostatic pressure protecting both the cuticle from transcellular infiltration of body fluid and the animal from dehydration
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxybutanoyl-CoA + glycine
? + CoA + CO2
show the reaction diagram
-
-
-
-
?
acetyl-CoA + glycine
?
show the reaction diagram
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
show the reaction diagram
butanoyl-CoA + glycine
? + CoA + CO2
show the reaction diagram
-
-
-
-
?
butyryl-CoA + glycine
?
show the reaction diagram
-
low activity
-
-
?
glutaryl-CoA + glycine
? + CoA + CO2
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + glycine
? + CoA + CO2
show the reaction diagram
-
-
-
-
?
propionyl-CoA + glycine
?
show the reaction diagram
-
low activity
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
show the reaction diagram
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
show the reaction diagram
additional information
?
-
-
enzyme deficiency causes X-linked sideroblastic anemia
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
show the reaction diagram
additional information
?
-
-
enzyme deficiency causes X-linked sideroblastic anemia
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-methyl-pyridoxal 5'-phosphate
-
in vitro, mutant D279A
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
optimal at concentration of 50 mM, inhibition above 200 mM
potassium ferricyanide
-
activates at 0.5 mM
additional information
-
partially purified enzyme requires high cation concentrations, equivalent to 0.3 M NaCl, for maximum activation, monovalent cations, i.e. Na+, K+, Li+, Rb+ or NH4+, in concentrations from 0.15 M to 0.30 M or divalent cations, i.e. Mg2+, Ca2+ or Mn2+, at lower concentrations of 0.03 M to 0.10 M are effective
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxyethyldisulfide
-
-
2-mercaptoethanol
2-oxoglutarate
aminomalonate
Aminomethylphosphonate
beta-Alanine
bilirubin
-
-
Borohydride
Chloramphenicol
-
-
chlorophyllide a
-
-
CoA
-
noncompetitive
cyanide
-
-
delta-aminolevuinate
deuteroporphyrin
-
-
Diethyl aminomalonate
dithiothreitol
-
-
Divalent cations
ethanolamine
FeCl3
-
addition of imidazole at 0.2 mM prior to FeCl3 prevents inhibition
ferroheme
glutathione
-
-
hemoglobin
Iron-deuteroporphyrin
-
-
Iron-mesoporphyrin
-
-
Iron-protoporphyrin
-
-
Isobutylamine
L-alanine
L-cysteine
-
-
L-Penicillamine
-
-
L-threonine
light
-
above 30 lux intensity
-
mesoporphyrin
-
-
Metalloporphyrins
Mg-protoporphyrin
-
-
Monovalent cations
Myoglobin
N-ethylmaleimide
Na+
-
inhibition of complex form, stimulation of stripped form
NaCl
-
fetal rat liver enzyme
p-chloromercuribenzoate
p-mercuribenzoate
Propanolol
-
-
protoheme
protoporphyrin
pyruvate
succinyl-CoA
-
non-specific isoform ALAS-N in absence of ATP
tergitol
-
fetal enzyme
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-allyl-2-isopropylacetamide
3,5-di-carbethoxy-1,4-dihydrocillidine
Activator protein
Butyric acid
-
induction of enzyme expression, erythroleukemia cells
CoA
-
activates
Dimethylsulfoxide
-
induction of enzyme expression, erythroleukemia cells
dithiothreitol
-
activates
hexamethylene diacetamide
-
induction of enzyme expression, erythroleukemia cells
Lubrol
-
activates, fetal enzyme
-
NaCl
-
required for maximal activity
native activator protein
O2
-
1%, 3fold increase in expression level, promotor activation in transiently transfected HeLa cells, hypoxia-inducible erythroid-isoform
phosphate
-
enzyme is maximally active in presence of 0.005 mM phosphate
vitamin B12
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0055 - 0.0742
2-hydroxybutanoyl-CoA
0.00054 - 0.0093
Butanoyl-CoA
0.0075 - 0.0301
glutaryl-CoA
0.00032 - 400
glycine
0.0018 - 0.0172
Octanoyl-CoA
0.00077 - 0.015
pyridoxal 5'-phosphate
0.003
pyridoxal phosphate
-
-
0.00064 - 49.55
succinyl-CoA
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.067
2-hydroxybutanoyl-CoA
0.001 - 0.17
Butanoyl-CoA
0.037 - 0.117
glutaryl-CoA
0.016 - 0.92
glycine
0.00002 - 0.34
Octanoyl-CoA
0.002 - 1.35
succinyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018 - 0.022
2-hydroxybutanoyl-CoA
0.0005 - 0.062
Butanoyl-CoA
0.0007 - 0.0068
glutaryl-CoA
0.00002 - 0.13
glycine
0.055 - 0.117
Octanoyl-CoA
0.0002 - 0.55
succinyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
5-aminolevulinate
-
versus glycine
0.023
aminomalonate
-
-
10
Aminomethylphosphonate
-
-
0.12
CoA
-
versus glycine
0.035
Hemin
-
-
0.2
metalloporphyrin
-
-
-
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0037
-
crude enzyme extract
0.0057
-
maximal enzyme activity after 3 weeks of storage of tubers at 0-15C at 30 lux
0.018
-
purified enzyme
0.035
-
purified enzyme
0.091
-
purified enzyme
0.16
-
purified enzyme
0.167
-
isozyme II
0.35
-
purified enzyme
0.375
-
purified isozyme I
0.558
-
purified enzyme
0.58
-
purified enzyme
0.62
-
purified enzyme
0.65
-
purified enzyme
1.22
-
purified enzyme
1.34
-
purified enzyme
1.87
-
purified erythroid-specific isoform
2.17 - 2.83
-
purified enzyme
2.17
-
purified enzyme
2.22
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
-
7.1 - 7.5
-
isoenzyme A
7.4 - 7.6
8.5
-
erythroid-specific isoform
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 8.6
-
about 50% of activity maximum at pH 5.8 and pH 8.6
6.5 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
sodium butyrate treatment activates ALAS2 gene transcription
Manually annotated by BRENDA team
-
high expression of isoform ALAS1
Manually annotated by BRENDA team
-
cells
Manually annotated by BRENDA team
-
ALA-S activity is induced by acute administration of anaesthetics (89%), veronal (240%), and ethanol (80). ALA-S mRNA expression augmented by chronic administration of eflurane, allylisopropylacetamide and veronal
Manually annotated by BRENDA team
-
high expression of isoform ALAS1
Manually annotated by BRENDA team
-
high expression of isoform ALAS1
Manually annotated by BRENDA team
-
erythroid induction cultures of CD34+ hematopoietic stem/progenitor cells
Manually annotated by BRENDA team
-
erythroid-specific isoform
Manually annotated by BRENDA team
-
including submandibular and parotid glands, high expression of ALAS1
Manually annotated by BRENDA team
-
sodium butyrate treatment activates ALAS2 gene transcription
Manually annotated by BRENDA team
-
high expression of isoform ALAS1
Manually annotated by BRENDA team
-
high expression of isoform ALAS1
Manually annotated by BRENDA team
-
rapid stimulation of ALA-s mRNA by ACTH which acts through cyclic AMP
Manually annotated by BRENDA team
-
high expression of isoform ALAS1
Manually annotated by BRENDA team
-
high expression of isoform ALAS1
Manually annotated by BRENDA team
-
high expression of isoform ALAS1
Manually annotated by BRENDA team
-
dim light and cold-stored, green skin peeling
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information