BRENDA - Enzyme Database show

The porphobilinogen synthase family of metalloenzymes

Jaffe, E.K.; Acta Crystallogr. Sect. D 56, 115-128 (2000)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
4.2.1.24
-
Pseudomonas aeruginosa
4.2.1.24
-
Saccharomyces cerevisiae
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.24
Mg2+
4 Zn at metal binding site A , 4 Zn at metal binding site B and 8 Mg at metal binding site C are required for full activity per homooctamer
Escherichia coli
4.2.1.24
Mg2+
4 Zn at metal binding site A and 8 Mg at metal binding site C are required for full activity per homooctamer
Pisum sativum
4.2.1.24
Mg2+
-
Pseudomonas aeruginosa
4.2.1.24
Zinc
4 Zn at metal binding site A , 4 Zn at metal binding site B and 8 Mg at metal binding site C are required for full activity per homooctamer
Escherichia coli
4.2.1.24
Zinc
4 Zn at metal binding site A and 4 Zn at metal binding site B are required for full activity per homooctamer
Homo sapiens
4.2.1.24
Zinc
4 Zn at metal binding site A and 8 Mg at metal binding site C are required for full activity per homooctamer
Pisum sativum
4.2.1.24
Zinc
8 Zn at metal binding site A and 8 Zn at metal binding site B are required for full activity per homooctamer
Saccharomyces cerevisiae
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
Homo sapiens
-
?
-
-
-
4.2.1.24
5-aminolevulinate
Pseudomonas aeruginosa
enzyme catalyzes the first common step in tetrapyrrole biosynthesis
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.24
Actinobacillus sp.
-
-
-
4.2.1.24
Aquifex sp.
-
-
-
4.2.1.24
Archaeoglobus sp.
-
-
-
4.2.1.24
Bordetella sp.
-
-
-
4.2.1.24
Bradyrhizobium sp.
-
-
-
4.2.1.24
Campylobacter sp.
-
-
-
4.2.1.24
Candida sp. (in: Saccharomycetales)
-
-
-
4.2.1.24
Caulobacter sp.
-
-
-
4.2.1.24
Chlamydia sp.
-
-
-
4.2.1.24
Chlamydomonas sp.
-
-
-
4.2.1.24
Clostridium sp.
-
-
-
4.2.1.24
Deinococcus sp.
-
-
-
4.2.1.24
Escherichia coli
-
-
-
4.2.1.24
Helicobacter sp.
-
-
-
4.2.1.24
Homo sapiens
-
-
-
4.2.1.24
Methanobacterium sp.
-
-
-
4.2.1.24
Methanococcus sp.
-
-
-
4.2.1.24
Methanothermus sp.
-
-
-
4.2.1.24
Mycobacterium sp.
-
-
-
4.2.1.24
Neisseria sp.
-
-
-
4.2.1.24
Physcomitrella sp.
-
-
-
4.2.1.24
Pisum sativum
-
-
-
4.2.1.24
Propionibacterium sp.
-
-
-
4.2.1.24
Pseudomonas aeruginosa
Q59643
-
-
4.2.1.24
Rattus norvegicus
-
-
-
4.2.1.24
Rhodobacter sp.
-
-
-
4.2.1.24
Rickettsia sp.
-
-
-
4.2.1.24
Saccharomyces cerevisiae
P05373
-
-
4.2.1.24
Salmonella sp.
-
-
-
4.2.1.24
Schizosaccharomyces sp.
-
-
-
4.2.1.24
Shewanella sp.
-
-
-
4.2.1.24
Streptomyces sp.
-
-
-
4.2.1.24
Synechocystis sp.
-
-
-
4.2.1.24
Vibrio sp.
-
-
-
4.2.1.24
Yersinia sp.
-
-
-
Reaction
EC Number
Reaction
Commentary
Organism
4.2.1.24
2 5-aminolevulinate = porphobilinogen + 2 H2O
mechanism
Pseudomonas aeruginosa
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
-
210733
Homo sapiens
?
-
-
-
-
4.2.1.24
5-aminolevulinate
enzyme catalyzes the first common step in tetrapyrrole biosynthesis
210733
Pseudomonas aeruginosa
?
-
-
-
-
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.2.1.24
-
Pseudomonas aeruginosa
4.2.1.24
-
Saccharomyces cerevisiae
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.24
Mg2+
4 Zn at metal binding site A , 4 Zn at metal binding site B and 8 Mg at metal binding site C are required for full activity per homooctamer
Escherichia coli
4.2.1.24
Mg2+
4 Zn at metal binding site A and 8 Mg at metal binding site C are required for full activity per homooctamer
Pisum sativum
4.2.1.24
Mg2+
-
Pseudomonas aeruginosa
4.2.1.24
Zinc
4 Zn at metal binding site A , 4 Zn at metal binding site B and 8 Mg at metal binding site C are required for full activity per homooctamer
Escherichia coli
4.2.1.24
Zinc
4 Zn at metal binding site A and 4 Zn at metal binding site B are required for full activity per homooctamer
Homo sapiens
4.2.1.24
Zinc
4 Zn at metal binding site A and 8 Mg at metal binding site C are required for full activity per homooctamer
Pisum sativum
4.2.1.24
Zinc
8 Zn at metal binding site A and 8 Zn at metal binding site B are required for full activity per homooctamer
Saccharomyces cerevisiae
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
Homo sapiens
-
?
-
-
-
4.2.1.24
5-aminolevulinate
Pseudomonas aeruginosa
enzyme catalyzes the first common step in tetrapyrrole biosynthesis
?
-
-
-
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
-
210733
Homo sapiens
?
-
-
-
-
4.2.1.24
5-aminolevulinate
enzyme catalyzes the first common step in tetrapyrrole biosynthesis
210733
Pseudomonas aeruginosa
?
-
-
-
-