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Literature summary extracted from

  • Azim, N.; Deery, E.; Warren, M.J.; Wolfenden, B.A.; Erskine, P.; Cooper, J.B.; Coker, A.; Wood, S.P.; Akhtar, M.
    Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic resolution (2014), Acta Crystallogr. Sect. D, 70, 744-751.
    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 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, 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, removal of the His-tag 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
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.61 More enzyme tertiary structure,overview Priestia megaterium

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 the enzyme possesses a dipyrromethane cofactor, which is covalently linked by a thioether bridge to the invariant cysteine residue, Cys241. The cofactor extends during the reaction by the sequential addition of the four substrate molecules, which are released as a linear tetrapyrrole product. Structure determination of the oxidized form of the dipyrromethane cofactor covalently attached to Cys241, overview. Analysis of oxidation states of the dipyrromethane cofactor and a proposed mechanism for oxidation of the dipyrromethane to dipyrromethene and subsequently dipyrromethanone Priestia megaterium

General Information

EC Number General Information Comment Organism
2.5.1.61 evolution all enzymes in the family adopt a three-domain fold in which domains 1 and 2 resemble the fold of type II periplasmic binding proteins and the third domain, to which the cofactor is covalently attached, adopts a distinct alpha/beta topology Priestia megaterium
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