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.

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 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.37 5-aminolevulinate synthase

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Results	in table
34	Activating Compound
9466	AA Sequence
14	Application
1	CAS Registry Number
44	Cloned(Commentary)
117	Cofactor
2	Crystallization (Commentary)
765	Disease/ Diagnostics
17	Expression
23	General Information
14	General Stability
244	Inhibitors
83	kcat/KM [mM/s]
10	Ki Value [mM]
226	KM Value [mM]
53	Localization
17	Metals/Ions
74	Molecular Weight [Da]
80	Natural Substrates/ Products (Substrates)
337	Organism
1	Oxidation Stability
8	Pathway
76	PDB ID
31	pH Optimum
4	pH Range
3	pH Stability
4	Posttranslational Modification
100	Protein Variants
47	Purification (Commentary)
49	Reaction
13	Reaction Type
156	Reference
1	Renatured (Commentary)
109	Source Tissue
45	Specific Activity [micromol/min/mg]
17	Storage Stability
220	Substrates and Products (Substrate)
45	Subunits
104	Synonyms
1	Systematic Name
19	Temperature Optimum [°C]
15	Temperature Stability [°C]
90	Turnover Number [1/s]

pH Stability

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pH Stability on EC 2.3.1.37 - 5-aminolevulinate synthase

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

6.8 - 8

Rattus norvegicus

-

unstable below pH 6.8 and above pH 8.0, irreversible loss of activity

486812

9

Rhodopseudomonas palustris

Q6RVB3

retains about 80% of activity

661787

additional information

Mus musculus

P08680

the secondary structure of the enzyme is mostly resilient to pH changes. Partial unfolding is observed at pH 2.0, but further decreasing pH results in acid-induced refolding of the secondary structure to nearly native levels. The tertiary structure rigidity is lost under acidic and specific alkaline conditions, pH 10.5 and pH 9.5 at 37°C, where ALAS populates a molten globule state. As the enzyme becomes less structured with increased alkalinity, the chiral environment of the internal aldimine is also modified. Under acidic conditions, the pyridoxal 5-phosphate cofactor dissociates from the enzyme. Reaction with 8-anilino-1-naphthalenesulfonic acid corroborates increased exposure of hydrophobic clusters in the alkaline and acidic molten globules, far-UV and near-UV circular dichroism study, detailed overview. The alkaline molten globule state of ALAS is catalytically active

735711