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Literature summary extracted from

  • Breinig, S.; Kervinen, J.; Stith, L.; Wasson, A.S.; Fairman, R.; Wlodawer, A.; Zdanov, A.; Jaffe, E.K.
    Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase (2003), Nat. Struct. Biol., 10, 757-763.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.24 sitting-drop vapour-diffusion method Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.24 F12L the catalytic activity is very low under conditions at which the wild-type human enzyme is most active Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.24 additional information
-
 additional information the kinetic data do not follow a simple Michaelis-Menten relationship, but can be attributed to catalysis by two different forms of the enzyme that have different Km-values Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.24 197000
-
 variant F12L, equilibrium sedimentation Homo sapiens
4.2.1.24 244000
-
 wild-type enzyme, equilibrium sedimentation Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.24 5-aminolevulinate + 5-aminolevulinate Homo sapiens the enzyme catalyzes the first common step in the biosynthesis of tetrapyrroles porphobilinogen + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.24 Homo sapiens P13716
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.24
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.24 5-aminolevulinate + 5-aminolevulinate the enzyme catalyzes the first common step in the biosynthesis of tetrapyrroles Homo sapiens porphobilinogen + 2 H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.24 More wild-type enzyme and variant F12L exist in different oligomeric states. The wild-type enzyme exists as an octamer and the F12L variant exists as a hexamer. It appears that any equilibrium between octamer and hexamer most probably proceeds through the interconversion of hugging dimer and the detached dimer Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.24 5.9 8 pH 5.9: about 50% of maximal activity, pH 8.0: about 70% of maximal activity, wild-type enzyme Homo sapiens
4.2.1.24 6.8
-
 wild-type enzyme Homo sapiens