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Literature summary for 1.14.20.14 extracted from

  • Mitchell, A.J.; Zhu, Q.; Maggiolo, A.O.; Ananth, N.R.; Hillwig, M.L.; Liu, X.; Boal, A.K.
    Structural basis for halogenation by iron- and 2-oxo-glutarate-dependent enzyme WelO5 (2016), Nat. Chem. Biol., 12, 636-640 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.20.14

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, 2.4 A resolution X-ray crystal structure of WelO5, in complex with its welwitindolinone precursor substrate, 12-epi-fischerindole U and 2.5 A resolution structure of mutant G166D in complex with 12-epi-fischerindole U Hapalosiphon welwitschii

Protein Variants

Protein Variants Comment Organism
G166D 2.5 A resolution structure of G166D WelO5 in complex with 12-epi-fischerindole U shows that Asp166 coordinates FeII and the substrate location observed in wilde-type enzyme WelO5 is retained in the variant enzyme Hapalosiphon welwitschii

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ Asp166 coordinates Fe(II) Hapalosiphon welwitschii

Organism

Organism UniProt Comment Textmining
Hapalosiphon welwitschii A0A067YX61
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Hapalosiphon welwitschii UTEX B 1830 A0A067YX61
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Hapalosiphon welwitschii

Synonyms

Synonyms Comment Organism
welO5
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 Hapalosiphon welwitschii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Hapalosiphon welwitschii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Hapalosiphon welwitschii