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succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
covalent binding of pyridoxal 5'-phosphate and glycine to active site Lys131 is required for optimal activity
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
Tyr121, Asp279, Arg439, and Lys313 are involved in substrate and cofactor binding, mechanism, subunit localisation
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
cysteine in heme-regulatory motif
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
Lys313 acts as a general base during formation of the quinonoid reaction intermediates
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
the active site is located at the subunit interface and contains catalytically essential residues from the two subunits
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
the active site is located at the subunit interface and contains catalytically essential residues from the two subunits
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
three-step kinetic process, ordered kinetic mechanism, reaction mechanism
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
pyridoxal 5'-phosphate binding site, sequence and function of glycine-rich motif
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
ordered bi-bi mechanism in which glycine binds first and 5-aminolevulinic acid dissociates last
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism, aldimine linkage between pyridoxal 5-phosphate and enzyme
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
proposed chemical mechanism of enzyme ALAS2 via (I) internal aldimine complex, (II) glycine-external aldimine, (III) quinonoid intermediate I, (IV) glycine-succinyl-CoA condensation intermediate, (V) 2-amino-3-ketoadipate intermediate, (VI) enol intermediate, (VII) quinonoid intermediate II, and (VIII) 5-aminolevulinate-external aldimine
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
proposed chemical mechanism of enzyme ALAS2. via (I) internal aldimine complex, (II) glycine-external aldimine, (III) quinonoid intermediate I, (IV) glycinesuccinyl-CoA condensation intermediate, (V) 2-amino-3-ketoadipate intermediate, (VI) enol intermediate, (VII) quinonoid intermediate II, and (VIII) 5-aminolevulinate-external aldimine
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
the rate of 5-aminolevulinate release is controlled by a hysteretic kinetic mechanism initiated by conformational changes of the enzyme. The active site residue Thr148 modulates the enzyme's strict amino acid substrate specificity. Catalytic mechanism, overview
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism, aldimine linkage between pyridoxal 5-phosphate and enzyme
-
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
mechanism
-
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
ordered bi-bi mechanism in which glycine binds first and 5-aminolevulinic acid dissociates last
-
-
succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
-
-
-
-
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2-hydroxybutanoyl-CoA + glycine
? + CoA + CO2
-
-
-
-
?
5-aminolevulinate-CoA
2-amino-3-hydroxycyclopent-2-en-1-one + CoASH
-
weak cyclization activity
-
-
-
alpha-glutamyl-CoA + glycine
6-amino-5-oxohexanoate + CoA + CO2
butanoyl-CoA + glycine
? + CoA + CO2
-
-
-
-
?
butyryl-CoA + glycine
?
-
low activity
-
-
?
glutaryl-CoA + glycine
? + CoA + CO2
-
-
-
-
?
octanoyl-CoA + glycine
? + CoA + CO2
-
-
-
-
?
propionyl-CoA + glycine
?
-
low activity
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
succinyl-CoA + L-serine
?
the reaction with L-serine follows a biphasic kinetic process
-
-
?
succinyl-CoA + O-methylglycine
?
-
-
-
?
succinyl-CoA-monomethyl ester + glycine
5-aminolevulinic acid methyl ester + CoA + CO2
additional information
?
-
acetyl-CoA + glycine
?
-
at 2% the rate of the reaction with succinyl-CoA
-
-
?
acetyl-CoA + glycine
?
-
low activity
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
r
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
r
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
-
r
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
r
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
-
r
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
-
-
-
ir
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
key enzyme in tetrapyrrole 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
-
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
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
absolutely specific for glycine
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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 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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
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
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
additional information
?
-
-
enzyme deficiency causes X-linked sideroblastic anemia
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
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
-
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
-
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
-
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
-
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
r
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
-
-
-
?
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
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
r
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
-
r
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
r
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
-
-
-
r
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
-
key enzyme in tetrapyrrole biosynthesis
-
-
?
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
-
-
-
-
?
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
-
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
-
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
-
-
-
?
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
-
rate-limiting enzyme of heme biosynthesis
-
-
?
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
-
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
-
key enzyme in tetrapyrrole biosynthesis
-
-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
-
rate-limiting enzyme of heme biosynthesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0055 - 0.0742
2-hydroxybutanoyl-CoA
0.00054 - 0.0093
butanoyl-CoA
0.0075 - 0.0301
glutaryl-CoA
0.0018 - 0.0172
octanoyl-CoA
0.00077 - 0.015
pyridoxal 5'-phosphate
0.00064 - 52.4
succinyl-CoA
additional information
additional information
-
0.0055
2-hydroxybutanoyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.0061
2-hydroxybutanoyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.0098
2-hydroxybutanoyl-CoA
-
wild-type, pH 7.5, 30°C
0.0742
2-hydroxybutanoyl-CoA
-
mutant R85L/T430V, pH 7.5, 30°C
0.00054
butanoyl-CoA
-
mutant R85L/T430V, pH 7.5, 30°C
0.0027
butanoyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.0061
butanoyl-CoA
-
wild-type, pH 7.5, 30°C
0.0093
butanoyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.0075
glutaryl-CoA
-
mutant R85K, pH 7.5, 30°C
0.017
glutaryl-CoA
-
wild-type, pH 7.5, 30°C
0.0301
glutaryl-CoA
-
mutant R85L, pH 7.5, 30°C
0.00032
glycine
-
pH 7.5, 30°C, ALAS(K313A mutant)/ALAS
0.00045
glycine
-
pH 7.5, 30°C, ALAS/ALAS
0.001
glycine
-
mutant Y428I/R433Q /G434N/E435T/L437N, pH 7.5, 20°C
0.0015
glycine
-
mutant N427H, pH 7.5, 20°C
0.0017
glycine
-
mutant L437Q, pH 7.5, 20°C
0.0018
glycine
-
pH 7.5, 30°C, ALAS/ALAS (K313A mutant)
0.002
glycine
-
mutant Y428N/P432N/R433I/G434E/E435K/L437K, pH 7.5, 20°C
0.002
glycine
-
pH 7.5, 30°C, ALAS
0.0023
glycine
-
mutant A425T, pH 7.5, 20°C
0.0023
glycine
-
mutant V423I/A425P/Y428C/P432R/R433K/E435N, pH 7.5, 20°C
0.0026
glycine
-
mutant A425G/Y428H/R433H/G434N/E435K/L437K, pH 7.5, 20°C
0.0029
glycine
-
mutant R433K/G434K/E435Q/L437Q, pH 7.5, 20°C
0.003
glycine
-
mutant V423L/Y428R/P432E/R433I/G434N/E435Q/L437K, pH 7.5, 20°C
0.011
glycine
-
wild-type, pH 7.5, 20°C
0.0171
glycine
-
wild-type, cosubstrate octanoyl-CoA, pH 7.5, 30°C
0.0172
glycine
-
mutant R85K, cosubstrate butanoyl-CoA, pH 7.5, 30°C
0.0182
glycine
-
mutant R85K, cosubstrate 2-hydroxybutanoyl-CoA, pH 7.5, 30°C
0.02
glycine
-
mutant R85K, cosubstrate succinyl-CoA, pH 7.5, 30°C
0.0212
glycine
-
mutant R85K, cosubstrate glutaryl-CoA, pH 7.5, 30°C
0.0221
glycine
-
wild-type, cosubstrate 2-hydroxybutanoyl-CoA, pH 7.5, 30°C
0.0242
glycine
-
wild-type, cosubstrate succinyl-CoA, pH 7.5, 30°C
0.0252
glycine
-
mutant R85K, cosubstrate octanoyl-CoA, pH 7.5, 30°C
0.0284
glycine
-
wild-type, cosubstrate glutaryl-CoA, pH 7.5, 30°C
0.0293
glycine
-
wild-type, cosubstrate butanoyl-CoA, pH 7.5, 30°C
0.0552
glycine
-
mutant R85L, cosubstrate octanoyl-CoA, pH 7.5, 30°C
0.0591
glycine
-
mutant R85L, cosubstrate 2-hydroxybutanoyl-CoA, pH 7.5, 30°C
0.0631
glycine
-
mutant R85L, cosubstrate succinyl-CoA, pH 7.5, 30°C
0.0703
glycine
-
mutant R85L, cosubstrate butanoyl-CoA, pH 7.5, 30°C
0.0706
glycine
-
mutant R85L, cosubstrate glutaryl-CoA, pH 7.5, 30°C
0.0742
glycine
-
mutant cosubstrate octanoyl-CoA, R85L/T430V, pH 7.5, 30°C
0.0882
glycine
-
mutant cosubstrate butanoyl-CoA, R85L/T430V, pH 7.5, 30°C
0.0922
glycine
-
mutant cosubstrate 2-hydroxybutanoyl-CoA, R85L/T430V, pH 7.5, 30°C
0.0984
glycine
-
mutant cosubstrate succinyl-CoA, R85L/T430V, pH 7.5, 30°C
2 - 3
glycine
-
pH 7.5, 30°C, wild-type
2 - 3
glycine
-
pH 7.5, 30°C, ALAS
2 - 3
glycine
wild-type enzyme, pH 7.5, 18°C
2.31
glycine
-
wild type enzyme, at pH 7.5 and 37°C
2.5
glycine
-
papain untreated enzyme
2.63
glycine
-
mutant enzyme H29R, at pH 7.5 and 37°C
3.25
glycine
-
mutant enzyme H15K, at pH 7.5 and 37°C
3.31
glycine
wild type enzyme, at pH 7.5 and 25°C
3.4
glycine
mutant enzyme C398A, at pH 7.5 and 25°C
3.52
glycine
mutant enzyme H340A, at pH 7.5 and 25°C
3.57
glycine
mutant enzyme H340A/C398A, at pH 7.5 and 25°C
6.2
glycine
-
recombinant mutant G144T
6.5
glycine
-
erythroid-specific isoform
6.95
glycine
-
recombinant mutant dimer K149A/K313A
7.5
glycine
-
papain treated enzyme
7.5
glycine
pH 7.4, 37°C, recombinant mutant DELTAAGTG
7.7
glycine
pH 7.4, 37°C, recombinant mutant F557X
8
glycine
pH 7.5, 37°C, wild-type enzyme
8
glycine
wild type enzyme, at pH 7.5 and 37°C
9.3
glycine
-
recombinant mutant G144A
9.3
glycine
pH 7.4, 37°C, recombinant wild-type enzyme
11
glycine
mutant N150G, pH 7.5, 18°C
11
glycine
mutant enzyme DELTAmALAS2, at pH 7.5 and 37°C
11.3
glycine
-
mutant enzyme T363S, at pH 7.2 and 37°C
11.7
glycine
-
recombinant erythroid isoform
11.7
glycine
-
pH 7.5, 20°C, mutant 2XALAS
11.8
glycine
-
pH 7.5, 30°C, ALAS/ALAS (K313A mutant)
11.9
glycine
-
recombinant mutant G144S
12
glycine
-
mutant V423L/Y428R/P432E/R433I/G434N/E435Q/L437K, pH 7.5, 20°C
12
glycine
mutant N150F, pH 7.5, 18°C
12
glycine
pH 7.4, 37°C, recombinant mutant Q548X
12.5
glycine
-
recombinant erythroid isoform
13
glycine
-
mutant A425G/Y428H/R433H/G434N/E435K/L437K, pH 7.5, 20°C
13
glycine
-
mutant Y428N/P432N/R433I/G434E/E435K/L437K, pH 7.5, 20°C
13
glycine
pH 7.4, 37°C, recombinant mutant DELTAAT
13.5
glycine
pH 7.4, 37°C, recombinant mutant DELTAG
14
glycine
-
pH 7.5, 20°C, wild-type
14
glycine
-
mutant V423I/A425P/Y428C/P432R/R433K/E435N, pH 7.5, 20°C
14
glycine
-
wild-type, pH 7.5, 20°C
14
glycine
-
mutant enzyme T83S, at pH 7.2 and 37°C
14.4
glycine
-
recombinant erythroid isoform mutant R433K
14.8
glycine
-
pH 7.5, 30°C, ALAS(K313A mutant)/ALAS
15
glycine
-
mutant N427H, pH 7.5, 20°C
16
glycine
-
mutant R433K/G434K/E435Q/L437Q, pH 7.5, 20°C
16
glycine
-
mutant Y428I/R433Q /G434N/E435T/L437N, pH 7.5, 20°C
16
glycine
mutant N150A, pH 7.5, 18°C
16
glycine
mutant N150H, pH 7.5, 18°C
16.7
glycine
-
pH 7.5, 30°C, mutant 2XALAS
16.7
glycine
-
pH 7.5, 30°C, ALAS/ALAS
16.7
glycine
-
mutant enzyme T83S/T363S, at pH 7.2 and 37°C
18
glycine
-
mutant S254A, 30°C, pH 7.5
18.4
glycine
-
recombinant erythroid isoform mutant R433L
23
glycine
-
recombinant erythroid isoform wild-type
24
glycine
-
mutant L437Q, pH 7.5, 20°C
25
glycine
-
wild-type, 30°C, pH 7.5
25
glycine
-
mutant A425T, pH 7.5, 20°C
26.4
glycine
isoform HemA, pH and temperature not specified in the publication
27
glycine
-
mutant S254T, 30°C, pH 7.5
31.7
glycine
-
wild type enzyme, at pH 7.2 and 37°C
31.7
glycine
isoform HemA, pH and temperature not specified in the publication
39
glycine
mutant N150W, pH 7.5, 18°C
43.4
glycine
isoform HemA, pH and temperature not specified in the publication
46.8
glycine
mutant C281P of isoform HemT, pH and temperature not specified in the publication
50
glycine
-
recombinant enzyme
50
glycine
pH 7.5, 37°C, mutant K221V
51
glycine
-
recombinant protein
52.2
glycine
-
recombinant mutant Y121H
52.2
glycine
-
recombinant mutant G142C
52.5
glycine
isoform HemT, pH and temperature not specified in the publication
103
glycine
-
recombinant erythroid isoform mutant R439K
140
glycine
-
recombinant erythroid isoform mutant D279E
400
glycine
-
recombinant mutant Y121F
0.0018
octanoyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.0034
octanoyl-CoA
-
wild-type, pH 7.5, 30°C
0.0103
octanoyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.0172
octanoyl-CoA
-
mutant R85L/T430V, pH 7.5, 30°C
0.00077
pyridoxal 5'-phosphate
-
-
0.001 - 0.01
pyridoxal 5'-phosphate
-
-
0.003
pyridoxal 5'-phosphate
-
-
0.015
pyridoxal 5'-phosphate
-
-
0.00064
succinyl-CoA
-
recombinant mutant G144A
0.001
succinyl-CoA
pH 7.5, 37°C, wild-type enzyme
0.0011
succinyl-CoA
mutant N150W, pH 7.5, 18°C
0.0012
succinyl-CoA
-
recombinant erythroid isoform and mutant G144S
0.0012
succinyl-CoA
-
mutant S254T, 30°C, pH 7.5
0.0012
succinyl-CoA
mutant N150H, pH 7.5, 18°C
0.0013
succinyl-CoA
-
wild-type, 30°C, pH 7.5
0.0016
succinyl-CoA
-
recombinant mutant Y121H
0.0019
succinyl-CoA
-
recombinant mutant G144T
0.002
succinyl-CoA
-
recombinant erythroid isoform wild-type
0.002
succinyl-CoA
-
recombinant mutant G142C
0.002
succinyl-CoA
-
recombinant mutant G142C
0.002
succinyl-CoA
-
erythroid-specific isoform
0.0021
succinyl-CoA
mutant N150G, pH 7.5, 18°C
0.0022
succinyl-CoA
-
recombinant erythroid isoform mutant R433K
0.0022
succinyl-CoA
mutant N150F, pH 7.5, 18°C
0.0023
succinyl-CoA
wild-type enzyme, pH 7.5, 18°C
0.0024
succinyl-CoA
mutant enzyme H340A, at pH 7.5 and 25°C
0.00242
succinyl-CoA
wild type enzyme, at pH 7.5 and 25°C
0.00255
succinyl-CoA
mutant enzyme C398A, at pH 7.5 and 25°C
0.00258
succinyl-CoA
mutant enzyme H340A/C398A, at pH 7.5 and 25°C
0.0029
succinyl-CoA
-
wild-type, pH 7.5, 30°C
0.0032
succinyl-CoA
-
recombinant erythroid isoform mutant R433L
0.0038
succinyl-CoA
mutant N150A, pH 7.5, 18°C
0.0124
succinyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.014
succinyl-CoA
-
recombinant mutant Y121F
0.0146
succinyl-CoA
-
wild type enzyme, at pH 7.2 and 37°C
0.0146
succinyl-CoA
isoform HemA, pH and temperature not specified in the publication
0.015
succinyl-CoA
isoform HemT, pH and temperature not specified in the publication
0.01513
succinyl-CoA
-
mutant enzyme H15K, at pH 7.5 and 37°C
0.0176
succinyl-CoA
isoform HemA, pH and temperature not specified in the publication
0.0184
succinyl-CoA
isoform HemA, pH and temperature not specified in the publication
0.0203
succinyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.0214
succinyl-CoA
-
wild type enzyme, at pH 7.5 and 37°C
0.02227
succinyl-CoA
-
mutant enzyme H29R, at pH 7.5 and 37°C
0.023
succinyl-CoA
pH 7.5, 37°C, mutant K221V
0.0261
succinyl-CoA
mutant C281P of isoform HemT, pH and temperature not specified in the publication
0.027
succinyl-CoA
-
recombinant erythroid isoform mutant R439K
0.032
succinyl-CoA
-
mutant S254A, 30°C, pH 7.5
0.035
succinyl-CoA
-
recombinant erythroid isoform mutant D279E
0.0357
succinyl-CoA
pH 7.4, 37°C, recombinant mutant DELTAAGTG
0.0398
succinyl-CoA
pH 7.4, 37°C, recombinant mutant DELTAAT
0.0401
succinyl-CoA
pH 7.4, 37°C, recombinant mutant DELTAG
0.0407
succinyl-CoA
pH 7.4, 37°C, recombinant wild-type enzyme
0.055
succinyl-CoA
-
recombinant protein
0.0774
succinyl-CoA
-
mutant enzyme T83S, at pH 7.2 and 37°C
0.096
succinyl-CoA
-
mutant R85L/T430V, pH 7.5, 30°C
0.1
succinyl-CoA
-
recombinant enzyme
0.1302
succinyl-CoA
-
mutant enzyme T83S/T363S, at pH 7.2 and 37°C
0.1645
succinyl-CoA
-
mutant enzyme T363S, at pH 7.2 and 37°C
0.45
succinyl-CoA
-
pH 7.5, 30°C, mutant 2XALAS
0.63
succinyl-CoA
-
pH 7.5, 20°C, mutant 2XALAS
1
succinyl-CoA
wild type enzyme, at pH 7.5 and 37°C
1.3
succinyl-CoA
mutant enzyme DELTAmALAS2, at pH 7.5 and 37°C
1.52
succinyl-CoA
-
recombinant mutant dimer K149A/K313A
2.3
succinyl-CoA
-
pH 7.5, 30°C, wild-type
11
succinyl-CoA
-
pH 7.5, 20°C, wild-type
36.3
succinyl-CoA
pH 7.4, 37°C, recombinant mutant F557X
49.55
succinyl-CoA
pH 7.5
52.4
succinyl-CoA
pH 7.4, 37°C, recombinant mutant Q548X
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
overview
-
additional information
additional information
-
overview
-
additional information
additional information
-
overview
-
additional information
additional information
-
overview
-
additional information
additional information
Michaelis-Menten steady-state kinetics, overview
-
additional information
additional information
kinetics analysis of wild-type and mutant enzymes, single and multiple turnover and stopped flow measurements, substrate protection study, overview
-
additional information
additional information
-
kinetics analysis of wild-type and mutant enzymes, single and multiple turnover and stopped flow measurements, substrate protection study, overview
-
additional information
additional information
Michaelis-Menten steady-state kinetics, two-step sequential kinetic mechanism , and thermodynamics. Both the reaction for wild-type hALAS2 and those for the X-linked protoporphyria variants comprised a single kinetic step associated with quinonoid intermediate formation followed by one decay step. Rates for the two steps range from 9.8-14.3/s and from 1.37-1.97 s for the reactions of the XLPP variants, whereas those for the wild-type hALAS2-catalyzed reaction are 6.6/s and 0.70/s
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics, two-step sequential kinetic mechanism , and thermodynamics. Both the reaction for wild-type hALAS2 and those for the X-linked protoporphyria variants comprised a single kinetic step associated with quinonoid intermediate formation followed by one decay step. Rates for the two steps range from 9.8-14.3/s and from 1.37-1.97 s for the reactions of the XLPP variants, whereas those for the wild-type hALAS2-catalyzed reaction are 6.6/s and 0.70/s
-
additional information
additional information
pre-steady state and steady state kinetics, overview
-
additional information
additional information
-
pre-steady state and steady state kinetics, overview
-
additional information
additional information
pre-steady-state and steady-state kinetics of wild-type and mutant enzymes, stopped-flow measurements, single and mutiple turnover rates, equilibrium dissociation constants, binding isotherms, detailed overview
-
additional information
additional information
-
pre-steady-state and steady-state kinetics of wild-type and mutant enzymes, stopped-flow measurements, single and mutiple turnover rates, equilibrium dissociation constants, binding isotherms, detailed overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.01 - 0.067
2-hydroxybutanoyl-CoA
0.001 - 0.17
butanoyl-CoA
0.037 - 0.117
glutaryl-CoA
0.00002 - 0.34
octanoyl-CoA
0.002 - 55.48
succinyl-CoA
0.01
2-hydroxybutanoyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.047
2-hydroxybutanoyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.067
2-hydroxybutanoyl-CoA
-
wild-type, pH 7.5, 30°C
0.001
butanoyl-CoA
-
mutant R85L/T430V, pH 7.5, 30°C
0.0335
butanoyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.105
butanoyl-CoA
-
wild-type, pH 7.5, 30°C
0.17
butanoyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.037
glutaryl-CoA
-
mutant R85L, pH 7.5, 30°C
0.05
glutaryl-CoA
-
mutant R85K, pH 7.5, 30°C
0.117
glutaryl-CoA
-
wild-type, pH 7.5, 30°C
0.016
glycine
-
pH 7.5, 20°C, wild-type
0.02
glycine
-
wild-type, co-substrate: succinyl-CoA, pH 7.5, 20°C
0.03
glycine
-
co-substrate: succinyl-CoA, mutant L437Q, pH 7.5, 20°C
0.05
glycine
-
mutant S254T, 30°C, pH 7.5
0.07
glycine
-
co-substrate: succinyl-CoA, mutant A425T, pH 7.5, 20°C
0.07
glycine
-
co-substrate: succinyl-CoA, mutant N427H, pH 7.5, 20°C
0.07
glycine
-
pH 7.5, 30°C, ALAS/ALAS (K313A mutant)
0.11
glycine
-
pH 7.5, 20°C, mutant 2XALAS
0.14
glycine
-
wild-type, 30°C, pH 7.5
0.16
glycine
-
co-substrate: succinyl-CoA, mutant V423I/A425P/Y428C/P432R/R433K/E435N, pH 7.5, 20°C
0.166
glycine
-
pH 7.5, 30°C, ALAS
0.167
glycine
-
pH 7.5, 30°C, wild-type
0.17
glycine
-
co-substrate: succinyl-CoA, mutant Y428I/R433Q /G434N/E435T/L437N, pH 7.5, 20°C
0.2
glycine
-
co-substrate: succinyl-CoA, mutant A425G/Y428H/R433H/G434N/E435K/L437K, pH 7.5, 20°C
0.2
glycine
-
co-substrate: succinyl-CoA, mutant R433K/G434K/E435Q/L437Q, pH 7.5, 20°C
0.23
glycine
-
co-substrate: succinyl-CoA, mutant Y428N/P432N/R433I/G434E/E435K/L437K, pH 7.5, 20°C
0.25
glycine
wild type enzyme, at pH 7.5 and 37°C
0.27
glycine
-
mutant S254A, 30°C, pH 7.5
0.31
glycine
-
co-substrate: succinyl-CoA, mutant V423L/Y428R/P432E/R433I/G434N/E435Q/L437K, pH 7.5, 20°C
0.32
glycine
mutant enzyme DELTAmALAS2, at pH 7.5 and 37°C
0.36
glycine
-
pH 7.5, 30°C, ALAS(K313A mutant)/ALAS
0.92
glycine
-
pH 7.5, 30°C, mutant 2XALAS
0.92
glycine
-
pH 7.5, 30°C, ALAS/ALAS
1.01
glycine
isoform HemT, pH and temperature not specified in the publication
1.06
glycine
isoform HemA, pH and temperature not specified in the publication
1.1
glycine
isoform HemA, pH and temperature not specified in the publication
1.3
glycine
isoform HemA, pH and temperature not specified in the publication
1.61
glycine
mutant enzyme H340A, at pH 7.5 and 25°C
1.69
glycine
mutant enzyme C398A, at pH 7.5 and 25°C
1.73
glycine
wild type enzyme, at pH 7.5 and 25°C
1.79
glycine
mutant enzyme H340A/C398A, at pH 7.5 and 25°C
12
glycine
-
mutant enzyme T363S, at pH 7.2 and 37°C
12.1
glycine
-
mutant enzyme T83S, at pH 7.2 and 37°C
13.1
glycine
-
mutant enzyme T83S/T363S, at pH 7.2 and 37°C
55.48
glycine
mutant C281P of isoform HemT, pH and temperature not specified in the publication
63.4
glycine
-
wild type enzyme, at pH 7.2 and 37°C
0.00002
octanoyl-CoA
-
mutant R85L/T430V, pH 7.5, 30°C
0.03
octanoyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.172
octanoyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.34
octanoyl-CoA
-
wild-type, pH 7.5, 30°C
0.002
succinyl-CoA
-
mutant R85L/T430V, pH 7.5, 30°C
0.016
succinyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.0183
succinyl-CoA
-
recombinant erythroid isoform mutant G142C
0.0355
succinyl-CoA
-
recombinant erythroid isoform mutant Y121H
0.04
succinyl-CoA
mutant N150H, pH 7.5, 18°C
0.06
succinyl-CoA
mutant N150F, pH 7.5, 18°C
0.0633
succinyl-CoA
-
recombinant erythroid isoform mutant G144T
0.09
succinyl-CoA
mutant N150W, pH 7.5, 18°C
0.0967
succinyl-CoA
-
recombinant erythroid isoform mutant D279E
0.107
succinyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.12
succinyl-CoA
-
recombinant erythroid isoform mutant G144S
0.13
succinyl-CoA
mutant N150A, pH 7.5, 18°C
0.132
succinyl-CoA
-
recombinant erythroid isoform mutant G144A
0.15
succinyl-CoA
mutant N150G, pH 7.5, 18°C
0.16
succinyl-CoA
wild-type enzyme, pH 7.5, 18°C
0.167
succinyl-CoA
-
recombinant erythroid isoform
0.167
succinyl-CoA
-
wild-type, pH 7.5, 30°C
0.17
succinyl-CoA
pH 7.5, 37°C, mutant K221V
0.235
succinyl-CoA
-
recombinant erythroid isoform mutant Y121F
0.25
succinyl-CoA
pH 7.5, 37°C, wild-type enzyme
0.308
succinyl-CoA
-
recombinant erythroid isoform
0.508
succinyl-CoA
-
recombinant erythroid mutant R439K
0.658
succinyl-CoA
-
recombinant erythroid isoform
0.842
succinyl-CoA
-
recombinant erythroid mutant R433L
1.01
succinyl-CoA
isoform HemT, pH and temperature not specified in the publication
1.06
succinyl-CoA
isoform HemA, pH and temperature not specified in the publication
1.1
succinyl-CoA
isoform HemA, pH and temperature not specified in the publication
1.3
succinyl-CoA
isoform HemA, pH and temperature not specified in the publication
1.35
succinyl-CoA
-
recombinant erythroid mutant R433K
1.61
succinyl-CoA
mutant enzyme H340A, at pH 7.5 and 25°C
1.69
succinyl-CoA
mutant enzyme C398A, at pH 7.5 and 25°C
1.73
succinyl-CoA
wild type enzyme, at pH 7.5 and 25°C
1.79
succinyl-CoA
mutant enzyme H340A/C398A, at pH 7.5 and 25°C
2.74
succinyl-CoA
-
wild type enzyme, at pH 7.5 and 37°C
3.1
succinyl-CoA
-
mutant enzyme H15K, at pH 7.5 and 37°C
3.2
succinyl-CoA
-
mutant enzyme H29R, at pH 7.5 and 37°C
55.48
succinyl-CoA
mutant C281P of isoform HemT, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0018 - 0.022
2-hydroxybutanoyl-CoA
0.0005 - 0.062
butanoyl-CoA
0.0007 - 0.0068
glutaryl-CoA
0.055 - 0.117
octanoyl-CoA
0.0002 - 250
succinyl-CoA
0.0018
2-hydroxybutanoyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.007
2-hydroxybutanoyl-CoA
-
wild-type, pH 7.5, 30°C
0.0085
2-hydroxybutanoyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.022
2-hydroxybutanoyl-CoA
-
mutant R85L/T430V, pH 7.5, 30°C
0.0005
butanoyl-CoA
-
mutant R85L/T430V, pH 7.5, 30°C
0.0035
butanoyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.02
butanoyl-CoA
-
wild-type, pH 7.5, 30°C
0.062
butanoyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.0007
glutaryl-CoA
-
mutant R85K, pH 7.5, 30°C
0.0012
glutaryl-CoA
-
mutant R85L, pH 7.5, 30°C
0.0068
glutaryl-CoA
-
wild-type, pH 7.5, 30°C
0.00002
glycine
-
mutant cosubstrate succinyl-CoA, R85L/T430V, pH 7.5, 30°C
0.00017
glycine
-
mutant R85K, cosubstrate glutaryl-CoA, pH 7.5, 30°C
0.00018
glycine
-
mutant R85L, cosubstrate 2-hydroxybutanoyl-CoA, pH 7.5, 30°C
0.0002
glycine
-
mutant R85L, cosubstrate succinyl-CoA, pH 7.5, 30°C
0.0005
glycine
-
mutant R85L, cosubstrate butanoyl-CoA, pH 7.5, 30°C
0.0005
glycine
-
mutant R85L, cosubstrate octanoyl-CoA, pH 7.5, 30°C
0.0019
glycine
-
mutant S254T, 30°C, pH 7.5
0.0023
glycine
-
mutant R85K, cosubstrate 2-hydroxybutanoyl-CoA, pH 7.5, 30°C
0.0023
glycine
mutant N150W, pH 7.5, 18°C
0.0025
glycine
mutant N150H, pH 7.5, 18°C
0.0028
glycine
-
wild-type, cosubstrate 2-hydroxybutanoyl-CoA, pH 7.5, 30°C
0.0043
glycine
-
wild-type, cosubstrate butanoyl-CoA, pH 7.5, 30°C
0.0048
glycine
-
wild-type, cosubstrate glutaryl-CoA, pH 7.5, 30°C
0.005
glycine
-
mutant R85K, cosubstrate succinyl-CoA, pH 7.5, 30°C
0.005
glycine
mutant N150F, pH 7.5, 18°C
0.0056
glycine
-
wild-type, 30°C, pH 7.5
0.0067
glycine
-
wild-type, cosubstrate succinyl-CoA, pH 7.5, 30°C
0.007
glycine
wild-type enzyme, pH 7.5, 18°C
0.0081
glycine
mutant N150A, pH 7.5, 18°C
0.0083
glycine
-
mutant R85K, cosubstrate butanoyl-CoA, pH 7.5, 30°C
0.0087
glycine
-
mutant R85K, cosubstrate octanoyl-CoA, pH 7.5, 30°C
0.0136
glycine
mutant N150G, pH 7.5, 18°C
0.015
glycine
-
mutant S254A, 30°C, pH 7.5
0.019
glycine
isoform HemT, pH and temperature not specified in the publication
0.02
glycine
-
mutant cosubstrate octanoyl-CoA, R85L/T430V, pH 7.5, 30°C
0.02
glycine
-
wild-type, cosubstrate octanoyl-CoA, pH 7.5, 30°C
0.02
glycine
mutant C281P of isoform HemT, pH and temperature not specified in the publication
0.026
glycine
isoform HemA, pH and temperature not specified in the publication
0.0291
glycine
mutant enzyme DELTAmALAS2, at pH 7.5 and 37°C
0.0312
glycine
wild type enzyme, at pH 7.5 and 37°C
0.033
glycine
isoform HemA, pH and temperature not specified in the publication
0.049
glycine
isoform HemA, pH and temperature not specified in the publication
0.13
glycine
-
mutant R85L, cosubstrate glutaryl-CoA, pH 7.5, 30°C
0.79
glycine
-
mutant enzyme T83S/T363S, at pH 7.2 and 37°C
0.87
glycine
-
mutant enzyme T83S, at pH 7.2 and 37°C
0.88
glycine
-
mutant enzyme H15K, at pH 7.5 and 37°C
1.07
glycine
-
mutant enzyme T363S, at pH 7.2 and 37°C
1.18
glycine
-
wild type enzyme, at pH 7.5 and 37°C
1.22
glycine
-
mutant enzyme H29R, at pH 7.5 and 37°C
2
glycine
-
wild type enzyme, at pH 7.2 and 37°C
0.055
octanoyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.113
octanoyl-CoA
-
wild-type, pH 7.5, 30°C
0.117
octanoyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.0002
succinyl-CoA
-
mutant R85L/T430V, pH 7.5, 30°C
0.0008
succinyl-CoA
-
mutant R85L, pH 7.5, 30°C
0.0084
succinyl-CoA
-
mutant S254A, 30°C, pH 7.5
0.0089
succinyl-CoA
-
mutant R85K, pH 7.5, 30°C
0.042
succinyl-CoA
-
mutant S254T, 30°C, pH 7.5
0.073
succinyl-CoA
-
mutant enzyme T363S, at pH 7.2 and 37°C
0.102
succinyl-CoA
-
mutant enzyme T83S/T363S, at pH 7.2 and 37°C
0.11
succinyl-CoA
-
wild-type, 30°C, pH 7.5
0.16
succinyl-CoA
-
mutant enzyme T83S, at pH 7.2 and 37°C
0.55
succinyl-CoA
-
wild-type, pH 7.5, 30°C
4.34
succinyl-CoA
-
wild type enzyme, at pH 7.2 and 37°C
7
succinyl-CoA
pH 7.5, 37°C, mutant K221V
27
succinyl-CoA
mutant N150F, pH 7.5, 18°C
33
succinyl-CoA
mutant N150H, pH 7.5, 18°C
34
succinyl-CoA
mutant N150A, pH 7.5, 18°C
35.4
succinyl-CoA
mutant C281P of isoform HemT, pH and temperature not specified in the publication
62.5
succinyl-CoA
isoform HemA, pH and temperature not specified in the publication
67.2
succinyl-CoA
isoform HemT, pH and temperature not specified in the publication
70
succinyl-CoA
wild-type enzyme, pH 7.5, 18°C
70.3
succinyl-CoA
isoform HemA, pH and temperature not specified in the publication
71
succinyl-CoA
mutant N150G, pH 7.5, 18°C
72.4
succinyl-CoA
isoform HemA, pH and temperature not specified in the publication
82
succinyl-CoA
mutant N150W, pH 7.5, 18°C
130
succinyl-CoA
-
wild type enzyme, at pH 7.5 and 37°C
140
succinyl-CoA
-
mutant enzyme H29R, at pH 7.5 and 37°C
230
succinyl-CoA
-
mutant enzyme H15K, at pH 7.5 and 37°C
246
succinyl-CoA
mutant enzyme DELTAmALAS2, at pH 7.5 and 37°C
250
succinyl-CoA
wild type enzyme, at pH 7.5 and 37°C
250
succinyl-CoA
pH 7.5, 37°C, wild-type enzyme
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C398A
the mutant shows reduced activity compared to the wild type enzyme
H340A
the mutant shows reduced activity compared to the wild type enzyme
H340A/C398A
the mutant shows reduced activity compared to the wild type enzyme
C398A
-
the mutant shows reduced activity compared to the wild type enzyme
-
H340A
-
the mutant shows reduced activity compared to the wild type enzyme
-
H340A/C398A
-
the mutant shows reduced activity compared to the wild type enzyme
-
C281P
the mutant shows about wild type activity. In the presence of 0.001 mM hemin, mutant C281P of isoform HemT retains 100% of its activity
T363S
-
the mutant shows strongly reduced 5-aminolevulinate synthase activity relative to the wild type enzyme
T83S
-
the mutant shows strongly reduced 5-aminolevulinate synthase activity relative to the wild type enzyme
T83S/T363S
-
the mutant shows strongly reduced 5-aminolevulinate synthase activity relative to the wild type enzyme
A425G/Y428H/R433H/G434N/E435K/L437K
-
hexa variant, kcat increased compared to wild-type, Km (Gly) comparable to wild-type, Km (succinyl-CoA) decreased compared to wild-type
A425T
-
single variant, kcat slightly increased compared to wild-type, Km (Gly) comparable to wild-type, Km (succinyl-CoA) decreased compared to wild-type
L437Q
-
single variant, kcat comparable to wild-type, Km (Gly) comparable to wild-type, Km (succinyl-CoA) decreased compared to wild-type
N427H
-
single variant, kcat slightly increased compared to wild-type, Km (Gly) comparable to wild-type, Km (succinyl-CoA) decreased compared to wild-type
R433K/G434K/E435Q/L437Q
-
quadruple variant, kcat increased compared to wild-type, Km (Gly) comparable to wild-type, Km (succinyl-CoA) decreased compared to wild-type
V423I/A425P/Y428C/P432R/R433K/E435N
-
hexa variant, kcat increased compared to wild-type, Km (Gly) comparable to wild-type, Km (succinyl-CoA) decreased compared to wild-type
V423L/Y428R/P432E/R433I/G434N/E435Q/L437K
-
hepta variant, kcat increased compared to wild-type, Km (Gly) comparable to wild-type, Km (succinyl-CoA) decreased compared to wild-type
Y428I/R433Q /G434N/E435T/L437N
-
penta variant, kcat increased compared to wild-type, Km (Gly) comparable to wild-type, Km (succinyl-CoA) decreased compared to wild-type
Y428N/P432N/R433I/G434E/E435K/L437K
-
hexa variant, kcat increased compared to wild-type, Km (Gly) comparable to wild-type, Km (succinyl-CoA) decreased compared to wild-type
F557X
site-directed mutagenesis, a ALAS2 exon 11, c.1670-1671TC>GA mutation
M567I
-
mutant shows 25% of wild-type activity, while its half-life is longer than that of wild-type
S568G
-
mutant shows decreased catalytic activity in vitro (20% compared to wild-type), but a higher half-life compared to those of wild-type ALAS2
V562A
-
mutant shows a higher catalytic activity in vitro, but a shorter half-life in vivo compared to those of wild-type ALAS2
D279A
-
exchange mutant of potential cofactor binding residue Asp279, no activity, dissociation constant for pyridoxal 5'-phosphate is 19fold increased, different mode of cofactor binding, no formation of quinonoid reaction intermediate, which can be restored by addition of analogue N-methyl-pyridoxal 5'-phosphate
D279E
-
exchange mutant of potential cofactor binding residue Asp279, 30fold reduced catalytic efficiency for succinyl-CoA compared to the wild-type
G142C
-
glycine-rich motif mutant, 15fold increased dissociation constant value for binding of cofactor pyridoxal 5'-phosphate, 6% turnover compared to the wild-type, 4fold increase of Km-value for glycine
G144A
-
glycine-rich motif mutant, 8.5fold increased dissociation constant value for binding of cofactor pyridoxal 5'-phosphate, 43% turnover compared to the wild-type, unaltered Km-values for the substrates
G144S
-
glycine-rich motif mutant, 8fold increased dissociation constant value for binding of cofactor pyridoxal 5'-phosphate, 39% turnover compared to the wild-type, unaltered Km-values for the substrates
G144T
-
glycine-rich motif mutant, 24.5fold increased dissociation constant value for binding of cofactor pyridoxal 5'-phosphate, 21% turnover compared to the wild-type, unaltered Km-values for the substrates
K313A/R149A
-
each mutation site located on 1 subunit, 2 plasmids, coexpression of the dimer in Escherichia coli hemA-, functional complementation, 26% activity compared to wild-type
K313G
-
site-directed mutagenesis, mutants of erythroid-specific isoform, exchange of active site lysine residue 313, binding of pyridoxal 5'-phosphate and glycine noncovalently, reduced activity, because covalent binding is required
K313R
-
formation of quinonoid reaction intermediates
N150A
site-directed mutagenesis, the mutation significantly reduces the rate of quinonoid intermediate formation in the forward direction
N150F
site-directed mutagenesis, the mutation significantly reduces the rate of quinonoid intermediate formation in the forward direction, while increasing the reverse reaction rate
N150G
site-directed mutagenesis, the mutation significantly reduces the rate of quinonoid intermediate formation in the forward direction
N150H
site-directed mutagenesis, the mutation significantly reduces the rate of quinonoid intermediate formation in the forward direction, while increasing the reverse reaction rate
N150W
site-directed mutagenesis, the mutation significantly reduces the rate of quinonoid intermediate formation in the forward direction
R149A
-
mutation site located at the active site of 1 subunit, functional complementation of Escherichia coli mutant strain hemA-, no activity
R433L
-
active site mutant, similar to the wild-type
R439K
-
active site mutant, 77% activity compared to the wild-type, 9-13fold increased Km for both substrates, 5fold increased dissociation constant for glycine
R439L
-
active site mutant, no activity, 30fold increased dissociation constant for glycine
R85K
-
catalytic efficiency similar to wild-type
R85L
-
68fold increase in catalytic efficincy with substrate octanoyl-CoA
R85L/T430V
-
strong decrease in catalytic efficiency
S254A
-
increase in Km value for succinyl-Coa and kcat value. Removal of the side chain hydroxyl group alters the microenvironment of the PLP cofactor and hinders succinyl-CoA binding
S254T
-
decrease in kcat value without altering Km value
T148A
site-directed mutagenesis, the active site Thr148 mutation modulates the enzyme's strict amino acid substrate specificity
V423L/Y428R/P432E/R433I/G434N/E435Q/L437K
site-directed mutagenesis,
V501L/Y506R/P510E/R511I/G512N/E513Q/L515K
hyperactive mutant
Y121F
-
exchange mutant of potential cofactor binding residue Tyr121, 5% activity compared to the wild-type, Km for glycine is 5fold increased, lower affinity for pyridoxal 5'phosphate
Y121H
-
exchange mutant of potential cofactor binding residue Tyr121, 36% activity compared to the wild-type, Km for glycine is 34fold increased, lower affinity for pyridoxal 5'phosphate
H15K
-
the mutant exhibits a 6.0°C higher melting temperature and shows a 10.3fold increase in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H15R
-
the mutant shows an increase in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H176D
-
the mutant shows an increase in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H206F
-
the mutant shows an increase in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H206Y
-
the mutant shows an increase in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H236D
-
the mutant shows an increase in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H293Y
-
the mutant shows a decrease in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H29R
-
the mutant exhibits a 2.3°C higher melting temperature and shows a 6.7fold increase in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H304M
-
the mutant shows a strong increase in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H304Q
-
the mutant shows a decrease in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H304V
-
the mutant shows a decrease in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H322L
-
the mutant shows a severe decrease in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H322V
-
the mutant shows a severe decrease in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H385R
-
the mutant shows a decrease in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H39Y
-
the mutant shows an increase in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H61D
-
the mutant shows a severe decrease in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
H61N
-
the mutant shows a decrease in specific activity after 1 h incubation at 37°C compared to the wild type enzyme
C145R
-
mutant strain G205, lacks enzyme activity, but can complement mutant strain Ole3 with mutation G344C
DELTACT
the variant lacking residues 535-548 has reduced activity (about 65% of wild type)
N157Y/N162S
-
mutant strain G101, lacks enzyme activity, but can complement mutant strain G220 with mutation T452R
R151A
the mutant shows 20% of wild type activity
C281P
-
the mutant shows about wild type activity. In the presence of 0.001 mM hemin, mutant C281P of isoform HemT retains 100% of its activity
-
C281P
-
the mutant shows about wild type activity. In the presence of 0.001 mM hemin, mutant C281P of isoform HemT retains 100% of its activity
-
Q548X
naturally occuring mutation involved in X-linked protoporphyria, 1.6fold increased activity compared to the wild-type enzyme. The increased activity Q548X enzyme does not bind to succinyl-CoA synthetase
Q548X
site-directed mutagenesis, an X-linked protoporphyria-related mutant
K221V
random mutagenesis, library screening, the mutation produces a 23fold increased Km for succinyl-CoA and a 97% decrease in kcat/Km for succinyl-CoA. This reduction in the specificity constant does not stem from lower affinity toward succinyl-CoA, since the Kd for succinyl-CoA of K221V is lower than that of the wild-type enzyme. Mutant K221V has a stronger binding affinity for succinyl-CoA compared to the wild-type enzyme. The mutation reduces the rates of quinonoid intermediate II formation and decay
K221V
the mutant shows severely reduced catalytic efficiency towards succinyl-CoA compared to the wild type enzyme
K313A
-
mutation site located at the active site of 1 subunit, functional complementation of Escherichia coli mutant strain hemA-, no activity
K313A
-
site-directed mutagenesis, mutants of erythroid-specific isoform, exchange of active site lysine residue 313, binding of pyridoxal 5'-phosphate and glycine noncovalently, reduced activity, because covalent binding is required
K313A
site-directed mutagenesis, inactive mutant
K313H
-
site-directed mutagenesis, mutants of erythroid-specific isoform, exchange of active site lysine residue 313, binding of pyridoxal 5'-phosphate and glycine noncovalently, reduced activity, because covalent binding is required
K313H
-
formation of quinonoid reaction intermediates
R433K
-
active site mutant, 2fold increased activity
R433K
site-directed mutagenesis, mALAS2 variant with a mutated presequence, the mutation results in an increase in activity to twice that of the wild-type enzyme, i.e. a 2fold increase in the kcat value and a 1.65 to 1.85fold enhancement in the specificity constants for glycine and succinyl-CoA over those of wild-type, mature mALAS2, 2.5fold increase in protoporphyrin IX accumulation in HeLa cells expressing the R433K precursor with a mutated presequence
additional information
-
analysis of the 5' regulatory region of 5-aminolevulinate synthase gene in variegate porphyria patients heterozygous for the causative R59W mutation in the protoporphyrinogen oxidase gene. In the presence of estrogen and ERalpha, the wild-type -853C/-1253T allele induces a 47% increase in transcription, while the -853T/-1253A double mutant allele showed a 35% increase in transcription. The highest induction is observed for the mutant -853T/1253T allele generating an increase of 66%
additional information
-
the deletion of 33 amino acids at C-terminal end results in higher catalytic activity both in vitro and in vivo with the longer half-life compared to wild-type
additional information
generation of two deletion mutants DELTAAT and DELTAAGTG enzymes. Compared to the purified wild-type enzyme, the deletion mutants show 1.8 and 3.1fold increased activity,respectively, compared to the wild-type enzyme
additional information
generation of X-linked protoporphyria-related deletion mutants delAT and delAGTG, the mutant delAGTG has a significantly increased affinity for the glycine substrate
additional information
-
generation of X-linked protoporphyria-related deletion mutants delAT and delAGTG, the mutant delAGTG has a significantly increased affinity for the glycine substrate
additional information
-
site-directed mutagenesis of hypoxia-inducible factor-1, i.e. HIF-1, binding site in promotor sequence -328/-318, reveales HIF-1 like activation of enzyme expression during hypoxia
additional information
-
stable MEL mutant, no induction of enzyme expression by dimethylsulfoxide, hexamethylene diacetamide and butyric acid, decline of enzyme activity after DMSO application
additional information
-
expression of erythroid-specific isoform in MEL mutant under control of metallothionin promotor results in induction of enzyme activity by addition of Zn2+ and Cd2+ in absence of DMSO
additional information
-
circularly permuted enzyme variants with N-terminal amino acids corrosponding to L25, Q69, N404, N408 and a monomeric protein consisting of two wild-type enzyme subunits covalently linked through the N-terminus of one subunit to the C-terminuns of the other. Analysis of guanidine hydrochloride-induced unfolding, conformational stability, and structure
additional information
-
linkage of two subunits into a single polypeptide chain dimer 2XALAS, results in enzyme with about 7fold greater turnover number than wild-type and with greater A410/A330 ratio
additional information
-
a single chain dimeric ALAS variant is created, in which one of the two active sites harbors a K313A mutation eliminating measurable enzyme activity in order to investigate the unusual enhanced enzymatic activity resulting from linking ALAS dimmers. The two active sites in ALAS/ALAS differentially contribute to the enhanced activity of the enzyme, even though the amount of ALA produced during the first turnover is identical in both active sites. The kcat values of the K313A variants differ significantly depending on which of the two active sites harbors the mutation
additional information
generation of enzyme mutant with mutated mitochondrial presequences, at residues C11 C38, and C70, and a mutation in the active site loop Expression of the mutants in human cells causes significant cellular accumulation of protoporphyrin IX, particularly in the membrane. ALAS2 expression results in an increase in cell death in comparison to aminolevulinic acid treatment producing a similar amount of protoporphyrin IX. Supplementation of cell culture medium with glycine leads to increased protoporphyrin IX accumulation in Malas2-expressing HeLa cells
additional information
-
generation of enzyme mutant with mutated mitochondrial presequences, at residues C11 C38, and C70, and a mutation in the active site loop Expression of the mutants in human cells causes significant cellular accumulation of protoporphyrin IX, particularly in the membrane. ALAS2 expression results in an increase in cell death in comparison to aminolevulinic acid treatment producing a similar amount of protoporphyrin IX. Supplementation of cell culture medium with glycine leads to increased protoporphyrin IX accumulation in Malas2-expressing HeLa cells
additional information
selection of functional mALAS2 variants from the Thr148/Asn150 library of constructs is accomplished by reversing the 5-aminolevulinate auxotrophic phenotype of Escherichia coli hemA (HU227) cells
additional information
-
selection of functional mALAS2 variants from the Thr148/Asn150 library of constructs is accomplished by reversing the 5-aminolevulinate auxotrophic phenotype of Escherichia coli hemA (HU227) cells
additional information
the truncation of the N-terminal region in mutant DELTAmALAS2 does not affect the Km values for either substrate while the kcat of the mutant enzyme, relative to that of the wild type enzyme, is increased by 22%
additional information
-
the truncation of the N-terminal region in mutant DELTAmALAS2 does not affect the Km values for either substrate while the kcat of the mutant enzyme, relative to that of the wild type enzyme, is increased by 22%
additional information
-
construction of transgenic plants of Nicotiana tabacum wild-type and mutant deficient in chlorophyll biosynthesis expressing the enzyme targeted to the plastids, functional complementation of the mutant, regulation
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