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Literature summary extracted from

  • Jaffe, E.K.
    The porphobilinogen synthase family of metalloenzymes (2000), Acta Crystallogr. Sect. D, 56, 115-128.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.24
-
 Saccharomyces cerevisiae
4.2.1.24
-
 Pseudomonas aeruginosa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.24 Mg2+
-
 Pseudomonas aeruginosa
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+ 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 8 Mg at metal binding site C are required for full activity per homooctamer Pisum sativum
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 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment 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 Comment Organism Reaction ID
4.2.1.24 2 5-aminolevulinate = porphobilinogen + 2 H2O mechanism Pseudomonas aeruginosa
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.24 5-aminolevulinate
-
 Homo sapiens ?
-
 ?
4.2.1.24 5-aminolevulinate enzyme catalyzes the first common step in tetrapyrrole biosynthesis Pseudomonas aeruginosa ?
-
 ?