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Literature summary for 2.5.1.61 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
Search for more literature for 2.5.1.61

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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)

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
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)

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

Synonyms

Synonyms Comment Organism
PBGD
-
 Priestia megaterium
porphobilinogen deaminase
-
 Priestia megaterium

Cofactor

Cofactor Comment Organism Structure
dipyrromethane
-
 Priestia megaterium

General Information

General Information Comment Organism
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