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Literature summary extracted from

  • You, Z.; Omura, S.; Ikeda, H.; Cane, D.E.; Jogl, G.
    Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis (2007), J. Biol. Chem., 282, 36552-36560.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.35
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 Streptomyces avermitilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.11.35 complexes with the cofactors iron, alpha-ketoglutarate, and the nonreactive enantiomer of the substrate, ent-1-deoxypentalenic acid, in four different crystal forms to up to 1.31 A resolution. The overall structure of PtlH forms a double-stranded barrel helix fold and the cofactor-binding site for iron and alpha-keto-glutarate is similar to other double-stranded barrel helix fold enzymes. Binding of the substrate enantiomer induces a reorganization of the monoclinic crystal lattice leading to a disorder-order transition of a C-terminal alpha-helix. The newly formed helix blocks the major access to the active site and effectively traps the bound substrate Streptomyces avermitilis

Protein Variants

EC Number Protein Variants Comment Organism
1.14.11.35 R117Q complete loss of activity Streptomyces avermitilis
1.14.11.35 R188Q 280fold decrease in activity Streptomyces avermitilis

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.35 Streptomyces avermitilis Q82IZ1
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.35 additional information no substrate: ent-1-deoxypentalenic acid Streptomyces avermitilis ?
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 ?