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Literature summary for 2.1.1.107 extracted from

  • Singh, W.; Karabencheva-Christova, T.G.; Black, G.W.; Ainsley, J.; Dover, L.; Christov, C.Z.
    Conformational dynamics, ligand binding and effects of mutations in NirE an S-adenosyl-L-methionine dependent methyltransferase (2016), Sci. Rep., 6, 20107 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
atomistic molecular dynamics study. The binding of the substrate contributes to the stabilization of the structure of the full complex. Conformational changes influence the orientation of the pyrrole rings in the substrate. Conformotional motions lead to more open conformation of enzyme active site to accommodate the substrate Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
E114Q increase in the root mean square deviations of the uroporphyrinogen III substrate in respect to the wild-type Pseudomonas aeruginosa
G189K increase in activity compared to wild-type. The side chain of K189 makes electrostatic interactions with the propionate side chain of ring B with an average distance of 4.0 A. The backbone of K189 makes hydrogen bonds with the propionate side chain of ring B of uroporphyrinogen III Pseudomonas aeruginosa
G189N increase in activity compared to wild-type. Both side chain and the backbone of N189 residue participates in hydrogen bonds with the propionate side chain of ring B of uroporphyrinogen III Pseudomonas aeruginosa
M186L loss of hydrophobic interactions between the side chain of L186 and methyl group of SAM Pseudomonas aeruginosa
R111K the side chain of residue R111 stabilizes the uroporphyrinogen III ring A acetate side chain by electrostatic interactions. Mutant R111K makes very unstable interactions with an average distance of 5 A between the acetate of ring A of uroporphyrinogen III Pseudomonas aeruginosa
R51D residue R51 is mainly involved in stabilization of the propionate side chain of ring A by hydrophobic interactions with an average distance of 4.1 A. In the mutant R51K, the side chain of K51 makes stable electrostatic interactions with the acetate side chain of ring A, however there are no hydrophobic interactions Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa P95417
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Synonyms

Synonyms Comment Organism
NirE
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Pseudomonas aeruginosa