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]

Crystallization

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Crystallization on EC 2.3.1.37 - 5-aminolevulinate synthase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

hanging drop vapor diffusion, crystal structure of full-length homodimeric enzyme binding its cofactor pyridoxal 5'-phosphate at 2.1 A, and structures of the enzyme in complex with the substrates glycine or succinyl-coenzyme A at 2.7 A and 2.8 A, respectivel

Rhodobacter capsulatus

P18079

673319

in complex with pyridoxal 5'-phosphate, using 0.1 M tri-sodium citrate (pH 5.5), 20% (w/v) PEG 3000

Saccharomyces cerevisiae

P09950

758491