BRENDA - Enzyme Database show

Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase

Breinig, S.; Kervinen, J.; Stith, L.; Wasson, A.S.; Fairman, R.; Wlodawer, A.; Zdanov, A.; Jaffe, E.K.; Nat. Struct. Biol. 10, 757-763 (2003)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
4.2.1.24
sitting-drop vapour-diffusion method
Homo sapiens
Engineering
EC Number
Amino acid exchange
Commentary
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
Commentary
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]
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
Homo sapiens
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.24
Homo sapiens
P13716
-
-
Purification (Commentary)
EC Number
Commentary
Organism
4.2.1.24
-
Homo sapiens
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.24
5-aminolevulinate + 5-aminolevulinate
the enzyme catalyzes the first common step in the biosynthesis of tetrapyrroles
653303
Homo sapiens
porphobilinogen + 2 H2O
-
653303
Homo sapiens
?
Subunits
EC Number
Subunits
Commentary
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
Commentary
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
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.2.1.24
sitting-drop vapour-diffusion method
Homo sapiens
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
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] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
Homo sapiens
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.2.1.24
-
Homo sapiens
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.24
5-aminolevulinate + 5-aminolevulinate
the enzyme catalyzes the first common step in the biosynthesis of tetrapyrroles
653303
Homo sapiens
porphobilinogen + 2 H2O
-
653303
Homo sapiens
?
Subunits (protein specific)
EC Number
Subunits
Commentary
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 (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
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