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Literature summary extracted from

  • Azim, N.; Deery, E.; Warren, M.J.; Erskine, P.; Cooper, J.B.; Wood, S.P.; Akhtar, M.
    Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium (2013), Acta Crystallogr. Sect. F, 69, 906-908.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.61 gene hemC, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3) Priestia megaterium

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.61 purified recombinant detagged enzyme, mixing of 2.5 mg/ml protein with 0.1 M sodium cacodylate, pH 6.5-6.8, 0.2 M magnesium acetate, and 25-30%PEG 8000, room temperature, removal of the His tag is necessary to obtain enzyme crystals, X-ray diffraction structure determination and analysis at 1.46-1.60 A resolution Priestia megaterium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.61 4 porphobilinogen + H2O Priestia megaterium
-
 hydroxymethylbilane + 4 NH3
-
 ?
2.5.1.61 4 porphobilinogen + H2O Priestia megaterium ATCC 12872
-
 hydroxymethylbilane + 4 NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.61 Priestia megaterium D5DT75 gene hemC
-
2.5.1.61 Priestia megaterium ATCC 12872 D5DT75 gene hemC
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.61 recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography, removal of the His-tag by thrombin and tag elimination by another step of nickel affinity chromatography Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.61 4 porphobilinogen + H2O
-
 Priestia megaterium hydroxymethylbilane + 4 NH3
-
 ?
2.5.1.61 4 porphobilinogen + H2O
-
 Priestia megaterium ATCC 12872 hydroxymethylbilane + 4 NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.61 PBGD
-
 Priestia megaterium
2.5.1.61 porphobilinogen deaminase
-
 Priestia megaterium

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.61 dipyrromethane
-
 Priestia megaterium

General Information

EC Number General Information Comment Organism
2.5.1.61 metabolism the enzyme hydroxymethylbilane synthase catalyses a key early step of tetrapyrrole biosynthesis pathways in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole Priestia megaterium