BRENDA - Enzyme Database show

Species-specific inhibition of porphobilinogen synthase by 4-oxosebacic acid

Jaffe, E.K.; Kervinen, J.; Martins, J.; Stauffer, F.; Neier, R.; Wlodawer, A.; Zdanov, A.; J. Biol. Chem. 277, 19792-19799 (2002)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
4.2.1.24
crystal structure of enzyme complexed with 4-oxosebaic acid and of enzyme complexed with 4,7-dioxosebaic acid
Escherichia coli
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.2.1.24
4,7-dioxosebaic acid
-
Escherichia coli
4.2.1.24
4-oxosebaic acid
active site-directed irreversible inhibitor, less potent than 4,7-dioxosebaic acid
Escherichia coli
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.24
Zn2+
enzyme uses a catalytic Zn2+
Escherichia coli
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
Escherichia coli
essential step in tetrapyrrole biosynthesis
porphobilinogen + 2 H2O
-
Escherichia coli
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.24
Escherichia coli
P0ACB2
-
-
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
essential step in tetrapyrrole biosynthesis
652256
Escherichia coli
porphobilinogen + 2 H2O
-
652256
Escherichia coli
?
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.2.1.24
crystal structure of enzyme complexed with 4-oxosebaic acid and of enzyme complexed with 4,7-dioxosebaic acid
Escherichia coli
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.2.1.24
4,7-dioxosebaic acid
-
Escherichia coli
4.2.1.24
4-oxosebaic acid
active site-directed irreversible inhibitor, less potent than 4,7-dioxosebaic acid
Escherichia coli
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.24
Zn2+
enzyme uses a catalytic Zn2+
Escherichia coli
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
Escherichia coli
essential step in tetrapyrrole biosynthesis
porphobilinogen + 2 H2O
-
Escherichia coli
?
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
essential step in tetrapyrrole biosynthesis
652256
Escherichia coli
porphobilinogen + 2 H2O
-
652256
Escherichia coli
?