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Literature summary for 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 (Comment) Organism
Streptomyces avermitilis

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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


Organism UniProt Comment Textmining
Streptomyces avermitilis Q82IZ1

Substrates and Products (Substrate)

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