Literature summary for 2.3.1.37 extracted from

Stojanovski, B.M.; Hunter, G.A.; Jahn, M.; Jahn, D.; Ferreira, G.C.
Unstable reaction intermediates and hysteresis during the catalytic cycle of 5-aminolevulinate synthase: implications from using pseudo and alternate substrates and a promiscuous enzyme variant (2014), J. Biol. Chem., 289, 22915-22925.

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Protein Variants

Protein Variants	Comment	Organism
T148A	site-directed mutagenesis, the active site Thr148 mutation modulates the enzyme's strict amino acid substrate specificity	Mus musculus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	pre-steady state and steady state kinetics, overview	Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
succinyl-CoA + glycine	Mus musculus	-	5-aminolevulinate + CoA + CO2	-	r

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	P08680	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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	Mus musculus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	Mus musculus	?	-	?
succinyl-CoA + glycine	-	Mus musculus	5-aminolevulinate + CoA + CO2	-	r
succinyl-CoA + L-serine	the reaction with L-serine follows a biphasic kinetic process	Mus musculus	?	-	?
succinyl-CoA + O-methylglycine	-	Mus musculus	?	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
18	-	assay at	Mus musculus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Mus musculus

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	dependent on	Mus musculus

General Information

General Information	Comment	Organism
metabolism	5-aminolevulinate synthase catalyzs the initial step of mammalian heme biosynthesis	Mus musculus

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Release 2023.1 (January 2023)