4.2.1.24: porphobilinogen synthase

This is an abbreviated version!
For detailed information about porphobilinogen synthase, go to the full flat file.

Reaction

2 5-aminolevulinate =

Synonyms

5-aminolaevulinic acid dehydratase, 5-aminolevulinate dehydrase, 5-aminolevulinate dehydratase, 5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing), 5-aminolevulinic acid dehydrase, 5-aminolevulinic acid dehydratase, 5-levulinic acid dehydratase, Al-D, ALA dehydratase, ALA synthetase, ALA-D, ALAD, ALADH, aminolevulinate dehydrase, aminolevulinate dehydratase, aminolevulinic dehydratase, CF-2, d-ALAD, delta aminolevulinic acid dehydratase, delta-ALA-D, delta-ALAD, delta-aminolevulinate dehydrase, delta-aminolevulinate dehydratase, delta-aminolevulinate dehydrataseALAD, delta-aminolevulinic acid dehydrase, delta-aminolevulinic acid dehydratase, delta-aminolevulinic dehydratase, gamma-aminolevulinic acid dehydratase, HemB, PaPBGS, PBG synthase, PBG-S, PBG-synthase, PBGS, Pcal_1709, PfALAD, PGBS, Porphobilinogen synthase, porphobilinogen synthetase, synthase, porphobilinogen, TgPBGS

ECTree

     4 Lyases

         4.2 Carbon-oxygen lyases

             4.2.1 Hydro-lyases

                4.2.1.24 porphobilinogen synthase

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Results	in table
8	Activating Compound
38384	AA Sequence
13	Application
1	CAS Registry Number
20	Cloned(Commentary)
15	Crystallization (Commentary)
736	Disease/ Diagnostics
3	Expression
11	General Information
3	General Stability
34	IC50 Value
220	Inhibitors
1	kcat/KM [mM/s]
27	Ki Value [mM]
36	KM Value [mM]
11	Localization
89	Metals/Ions
70	Molecular Weight [Da]
30	Natural Substrates/ Products (Substrates)
522	Organism
2	Oxidation Stability
8	Pathway
81	PDB ID
42	pH Optimum
7	pH Range
1	pH Stability
1	pI Value
25	Protein Variants
35	Purification (Commentary)
8	Reaction
3	Reaction Type
194	Reference
116	Source Tissue
27	Specific Activity [micromol/min/mg]
3	Storage Stability
117	Substrates and Products (Substrate)
36	Subunits
109	Synonyms
1	Systematic Name
14	Temperature Optimum [°C]
2	Temperature Range [°C]
7	Temperature Stability [°C]
2	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 4.2.1.24 - porphobilinogen synthase

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SYSTEMATIC NAME

IUBMB Comments

5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing; porphobilinogen-forming)

The enzyme catalyses the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430. The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis. The enzymes from most organisms utilize metal ions (Zn2+, Mg2+, K+, and Na+) as cofactors that reside at multiple sites, including the active site and allosteric sites. Enzymes from archaea, yeast, and metazoa (including human) contain Zn2+ at the active site. In humans, the enzyme is a primary target for the environmental toxin Pb. The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation.