2.3.1.37: 5-aminolevulinate synthase
This is an abbreviated version!
For detailed information about 5-aminolevulinate synthase, go to the full flat file.
Word Map on EC 2.3.1.37
-
2.3.1.37
-
heme
-
porphyria
-
sideroblastic
-
oxygenase
-
anemia
-
x-linked
-
ferrochelatase
-
hemoglobin
-
marrow
-
porphobilinogen
-
dehydratase
-
pyridoxal
-
uroporphyrinogen
-
protoporphyria
-
iron-responsive
-
hemoprotein
-
erythroblast
-
phenobarbital
-
erythropoietic
-
tetrapyrrole
-
rhodopseudomonas
-
rhodobacter
-
microcytic
-
porphyrinogenic
-
erythroleukemia
-
delta-aminolaevulinate
-
allylisopropylacetamide
-
uroporphyrin
-
medicine
-
synthesis
-
hypochromic
-
pharmacology
-
gata1
-
aip
-
hexachlorobenzene
-
plp-dependent
-
cutanea
-
5'-phosphate-dependent
-
phenobarbital-induced
-
biotechnology
-
neurovisceral
-
nutrition
-
rate-controlling
-
pyrrolase
-
protoporphyrinogen
-
heme-mediated
-
tarda
-
5-aminolaevulinate
-
succinyl-coenzyme
-
bacteriochlorophyll
-
coproporphyrinogen
-
agriculture
-
harderian
-
succinylacetone
- 2.3.1.37
- heme
- porphyria
-
sideroblastic
- oxygenase
- anemia
-
x-linked
-
ferrochelatase
- hemoglobin
- marrow
- porphobilinogen
- dehydratase
- pyridoxal
- uroporphyrinogen
- protoporphyria
-
iron-responsive
- hemoprotein
- erythroblast
- phenobarbital
-
erythropoietic
- tetrapyrrole
- rhodopseudomonas
- rhodobacter
-
microcytic
-
porphyrinogenic
- erythroleukemia
-
delta-aminolaevulinate
-
allylisopropylacetamide
-
uroporphyrin
- medicine
- synthesis
-
hypochromic
- pharmacology
- gata1
- aip
- hexachlorobenzene
-
plp-dependent
-
cutanea
-
5'-phosphate-dependent
-
phenobarbital-induced
- biotechnology
-
neurovisceral
- nutrition
-
rate-controlling
-
pyrrolase
- protoporphyrinogen
-
heme-mediated
- tarda
-
5-aminolaevulinate
-
succinyl-coenzyme
- bacteriochlorophyll
- coproporphyrinogen
- agriculture
-
harderian
- succinylacetone
Reaction
Synonyms
5-ALA synthase, 5-ALAS, 5-aminolevulinate synthase, 5-aminolevulinate synthetase, 5-aminolevulinic acid synthase, 5-aminolevulinic acid synthetase, ALA, ALA synthase, ALA synthetase, ALA-S, ALAS, ALAS2, alpha-aminolevulinic acid synthase, aminolevulinate synthase, aminolevulinate synthase 2, aminolevulinate synthetase, aminolevulinic acid synthase, aminolevulinic acid synthase 2, aminolevulinic acid synthetase, aminolevulinic synthetase, delta-ALAS, delta-aminolevulinate synthase, delta-aminolevulinate synthetase, delta-aminolevulinic acid synthase, delta-aminolevulinic acid synthase 2, delta-aminolevulinic acid synthetase, delta-aminolevulinic synthetase, erythroid 5-aminolevulinate synthase, erythroid-specific 5-aminolevulinate synthase, Hem1, hemA, HemT, mALAS-2, sigma-aminolevulinate synthase, synthase, aminolevulinate, synthetase, aminolevulinate
ECTree
2.3.1.37 5-aminolevulinate synthaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.3.1.37 - 5-aminolevulinate synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-aminolevulinate-CoA
2-amino-3-hydroxycyclopent-2-en-1-one + CoASH
-
weak cyclization activity
-
-
-
succinyl-CoA + L-serine
?
the reaction with L-serine follows a biphasic kinetic process
-
-
?
acetyl-CoA + glycine
?
-
at 2% the rate of the reaction with succinyl-CoA
-
-
?
acetyl-CoA + glycine
?
-
at 2% the rate of the reaction with succinyl-CoA
-
-
?
acetyl-CoA + glycine
?
-
at 2% the rate of the reaction with succinyl-CoA
-
-
?
acetyl-CoA + glycine
?
-
at 2% the rate of the reaction with succinyl-CoA
-
-
?
acetyl-CoA + glycine
?
-
at 2% the rate of the reaction with succinyl-CoA
-
-
?
acetyl-CoA + glycine
?
-
at 2% the rate of the reaction with succinyl-CoA
-
-
?
acetyl-CoA + glycine
?
-
at 2% the rate of the reaction with succinyl-CoA
-
-
?
acetyl-CoA + glycine
?
-
at 2% the rate of the reaction with succinyl-CoA
-
-
?
acetyl-CoA + glycine
?
-
at 2% the rate of the reaction with succinyl-CoA
-
-
?
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
-
at 9% the rate of the reaction with succinyl-CoA
-
-
?
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
-
at 9% the rate of the reaction with succinyl-CoA
-
-
?
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
-
at 9% the rate of the reaction with succinyl-CoA
-
-
?
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
-
at 9% the rate of the reaction with succinyl-CoA
-
-
?
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
-
at 9% the rate of the reaction with succinyl-CoA
-
-
?
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
-
at 9% the rate of the reaction with succinyl-CoA
-
-
?
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
-
at 9% the rate of the reaction with succinyl-CoA
-
-
?
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
-
at 9% the rate of the reaction with succinyl-CoA
-
-
?
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
-
at 9% the rate of the reaction with succinyl-CoA
-
-
?
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
-
at 9% the rate of the reaction with succinyl-CoA
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
ir
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
ir
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for succinyl-CoA
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
enzyme utilizes acetyl-CoA, propionyl-CoA and butyryl-CoA at much lower rates
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
glycine is formed by the reverse reaction under optimum conditions at 4-5% the rate of 5-aminolevulinate formed by the forward reaction under optimum conditions
-
r
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolutely specific for glycine
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
regulatory mechanisms in hepatic and erythroid cells
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolutely specific for glycine
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
ir
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolutely specific for glycine
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
regulatory mechanisms in hepatic and erythroid cells
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
ir
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolutely specific for glycine
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
regulatory mechanisms in hepatic and erythroid cells
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
ALAS2 synthesizes heme specifically for haemoglobin
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
first and rate-limiting step of heme biosynthesis. Repression of 5-aminolevulinate synthase gene by the potent tumor promoter, TPA, involves multiple signal transduction pathways
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
cellular iron status plays a regulatory role
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
regulatory mechanisms in hepatic and erythroid cells
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
first step in heme biosynthesis pathway
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
first step in heme biosynthesis pathway
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
first step in heme biosynthesis pathway
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
5-aminolevulinate synthase operates under the stereoelectronic control predicted by Dunathans hypothesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
it is the CoA, rather than the succinyl moiety, that facilitates binding of succinyl-CoA to wild-type ALAS
-
-
r
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
ir
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolutely specific for glycine
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
ir
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
ir
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for succinyl-CoA
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolutely specific for glycine
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
regulatory mechanisms in hepatic and erythroid cells
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for succinyl-CoA
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
ir
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
ir
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolutely specific for glycine
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
regulatory mechanisms in hepatic and erythroid cells
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
common intermediate in the biosynthesis of chlorophyll and heme
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolute requirement for glycine
-
ir
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
-
?
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
-
at 80% the rate of the reaction with succinyl-CoA
-
-
?
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
-
at 80% the rate of the reaction with succinyl-CoA
-
-
?
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
-
at 80% the rate of the reaction with succinyl-CoA
-
-
?
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
-
at 80% the rate of the reaction with succinyl-CoA
-
-
?
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
-
at 80% the rate of the reaction with succinyl-CoA
-
-
?
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
-
at 80% the rate of the reaction with succinyl-CoA
-
-
?
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
-
at 80% the rate of the reaction with succinyl-CoA
-
-
?
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
-
at 80% the rate of the reaction with succinyl-CoA
-
-
?
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
-
at 80% the rate of the reaction with succinyl-CoA
-
-
?
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
-
at 80% the rate of the reaction with succinyl-CoA
-
-
?
additional information
?
-
-
enzyme deficiency causes X-linked sideroblastic anemia
-
-
?
additional information
?
-
analysis of unstable enzyme-catalyzed reaction intermediates and conformational changes using physiological and non-physiological substrates and promiscuous T148A enzyme variant, overview. Formation of the quinonoid intermediate upon reacting glycine with the enzyme. Significantly, in the absence of the succinyl-CoA substrate, the external aldimine predominates over the glycine quinonoid intermediate. When instead of glycine, L-serine is reacted with the enzyme, a lag phase is observed in the progress curve for the L-serine external aldimine formation, indicating a hysteretic behavior in enzyme ALAS. Hysteresis is not detected in the T148A-catalyzed L-serine external aldimine formation. The rate of 5-aminolevulinate release is also controlled by a hysteretic kinetic mechanism. The active site residue Thr148 modulates the enzyme's strict amino acid substrate specificity, positioning of the glycine external aldimine in the active site, overview
-
-
?
additional information
?
-
-
analysis of unstable enzyme-catalyzed reaction intermediates and conformational changes using physiological and non-physiological substrates and promiscuous T148A enzyme variant, overview. Formation of the quinonoid intermediate upon reacting glycine with the enzyme. Significantly, in the absence of the succinyl-CoA substrate, the external aldimine predominates over the glycine quinonoid intermediate. When instead of glycine, L-serine is reacted with the enzyme, a lag phase is observed in the progress curve for the L-serine external aldimine formation, indicating a hysteretic behavior in enzyme ALAS. Hysteresis is not detected in the T148A-catalyzed L-serine external aldimine formation. The rate of 5-aminolevulinate release is also controlled by a hysteretic kinetic mechanism. The active site residue Thr148 modulates the enzyme's strict amino acid substrate specificity, positioning of the glycine external aldimine in the active site, overview
-
-
?
additional information
?
-
the wild-type enzyme catalyzes the conversion of 5-aminolevulinate into the quinonoid intermediate at a rate 6.3fold slower than the formation of the same quinonoid intermediate from glycine and succinyl-CoA. The mutant N150F enzyme catalyzes the forward reaction at a 1.2fold faster rate than that of the reverse reaction, and the N150H variant reverses the rate values with a 1.7fold faster rate for the reverse reaction than that for the forward reaction. Steric constraints imposed by the active site of wild-type enzyme ALAS contribute toward the amino acid substrate specificity
-
-
?
additional information
?
-
-
the wild-type enzyme catalyzes the conversion of 5-aminolevulinate into the quinonoid intermediate at a rate 6.3fold slower than the formation of the same quinonoid intermediate from glycine and succinyl-CoA. The mutant N150F enzyme catalyzes the forward reaction at a 1.2fold faster rate than that of the reverse reaction, and the N150H variant reverses the rate values with a 1.7fold faster rate for the reverse reaction than that for the forward reaction. Steric constraints imposed by the active site of wild-type enzyme ALAS contribute toward the amino acid substrate specificity
-
-
?
additional information
?
-
no activity with L-alanine, L-serine or L-threonine
-
-
-
additional information
?
-
-
no activity with L-alanine, L-serine or L-threonine
-
-
-
