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Literature summary extracted from

  • Storbeck, S.; Saha, S.; Krausze, J.; Klink, B.U.; Heinz, D.W.; Layer, G.
    Crystal structure of the heme d1 biosynthesis enzyme NirE in complex with its substrate reveals new insights into the catalytic mechanism of S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferases (2011), J. Biol. Chem., 286, 26754-26767.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.107 sitting drop vapor diffusion method, using Tris, pH 8.0, 24% (w/v) PEG 6000 for enzyme without substrate, and 0.2 M lithium sulfate, 0.1 M Tris, pH 8.5, 1.26 M ammonium sulfate for enzyme in complex with uroporphyrinogen III Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.107 E114Q the mutant shows strongly reduced activity compared to the wild type enzyme Pseudomonas aeruginosa
2.1.1.107 G189K the mutant shows increased activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme Pseudomonas aeruginosa
2.1.1.107 G189N the mutant shows increased activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme Pseudomonas aeruginosa
2.1.1.107 H161F the mutant shows reduced activity compared to the wild type enzyme Pseudomonas aeruginosa
2.1.1.107 K102A the mutant shows no activity and strongly reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme Pseudomonas aeruginosa
2.1.1.107 M186L the mutant shows strongly reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme Pseudomonas aeruginosa
2.1.1.107 R111K the mutant shows strongly reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme Pseudomonas aeruginosa
2.1.1.107 R149K the mutant shows no activity compared to the wild type enzyme Pseudomonas aeruginosa
2.1.1.107 R51K the mutant shows reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme Pseudomonas aeruginosa

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.107 S-adenosyl-L-homocysteine
-
 Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.107 Pseudomonas aeruginosa P95417
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.107 Ni2+-Sepharose column chromatography Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.107 2 S-adenosyl-L-methionine + uroporphyrinogen III
-
 Pseudomonas aeruginosa 2 S-adenosyl-L-homocysteine + precorrin-2
-
 ir

Subunits

EC Number Subunits Comment Organism
2.1.1.107 homodimer
-
 Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
2.1.1.107 NirE
-
 Pseudomonas aeruginosa
2.1.1.107 S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase
-
 Pseudomonas aeruginosa