Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes

@article{Hausinger2004FeIIKetoglutarateDependentHA,
  title={Fe(II)/$\alpha$-Ketoglutarate-Dependent Hydroxylases and Related Enzymes},
  author={Robert P. Hausinger},
  journal={Critical Reviews in Biochemistry and Molecular Biology},
  year={2004},
  volume={39},
  pages={21 - 68}
}
  • R. Hausinger
  • Published 1 January 2004
  • Chemistry
  • Critical Reviews in Biochemistry and Molecular Biology
Fe(II)/α-ketoglutarate (αKG)-dependent hydroxylases catalyze an amazing diversity of reactions that result in protein side-chain modifications, repair of alkylated DNA/RNA, biosynthesis of antibiotics and plant products, metabolism related to lipids, and biodegradation of a variety of compounds. These enzymes possess a β-strand “jellyroll” structural fold that contains three metal-binding ligands found in a His1-X-Asp/Glu-Xn-His2 motif. The cosubstrate, αKG, chelates Fe(II) using its C-2 keto… 
Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH.
TLDR
Data suggest that substrate-induced reorientation of bound O2 is the mechanism utilized by the αKG oxygenases to tightly couple O2 activation to substrate hydroxylation.
Recent examples of α-ketoglutarate-dependent mononuclear non-haem iron enzymes in natural product biosyntheses.
TLDR
Several novel αKG-NHFe enzymes involved in natural product biosyntheses discovered in recent years are summarized, including halogenation reactions, amino acid modifications and tailoring reactions in the biosynthesis of terpenes, lipids, fatty acids and phosphonates.
Advances in Fe(II)/2-ketoglutarate-dependent dioxygenase-mediated C–H bond oxidation for regioselective and stereoselective hydroxyl amino acid synthesis: from structural insights into practical applications
The asymmetric hydroxylation of inactive carbon atoms in organic compounds remains an important reaction in the industrial synthesis of valuable chiral compounds. Fe(II) and 2-ketoglutarate-dependent
The Fe(II)/α‐ketoglutarate‐dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers
TLDR
Comparisons with taurine dioxygenase from Escherichia’coli (TauDEc) demonstrate that both enzymes are quite similar regarding their spectra, structure and kinetics, and only minor differences for the accumulation of intermediates during the reaction have been observed.
Fe(II)/alpha-ketoglutarate hydroxylases involved in nucleobase, nucleoside, nucleotide, and chromatin metabolism.
TLDR
This Perspective focuses on a subgroup of Fe(II)/alpha-ketoglutarate-dependent hydroxylases that are involved in pyrimidine salvage, purine decomposition, nucleoside and nucleotidehydroxylation, DNA/RNA repair, and chromatin modification.
Oxidation by 2-oxoglutarate oxygenases: non-haem iron systems in catalysis and signalling
TLDR
The roles of 2OG oxygenases are discussed in terms of the generic structural and mechanistic features that render the 2OGoxyases suited for their functions.
Characteristics and biotechnology applications of aliphatic amino acid hydroxylases belonging to the Fe(II)/α-ketoglutarate-dependent dioxygenase superfamily
  • M. Hibi, J. Ogawa
  • Chemistry, Medicine
    Applied Microbiology and Biotechnology
  • 2014
TLDR
The characterization and process development of this novel functioning group of Fe/αKG-DOs, found to catalyze the asymmetric hydroxylation of aliphatic amino acids, is reviewed.
Metal ligand substitution and evidence for quinone formation in taurine/alpha-ketoglutarate dioxygenase.
TLDR
These studies present the first systematic mutational analysis of metallocenter ligands in an Fe(II)/alphaKG-dependent hydroxylase and reveal putative Fe(IV)-oxo intermediates as reported in wild-type enzyme, but with distinct kinetics.
α-Amine Desaturation of d-Arginine by the Iron(II)- and 2-(Oxo)glutarate-Dependent l-Arginine 3-Hydroxylase, VioC.
TLDR
It is shown here that the Fe/2OG enzyme, VioC, which is natively an l-arginine 3-hydroxylase, catalyzes an efficient oxidative deamination of its substrate enantiomer, d-Arg, via a hydrolytically labile C2-iminium intermediate.
Self-hydroxylation of taurine/α-ketoglutarate dioxygenase: evidence for more than one oxygen activation mechanism
TLDR
The results demonstrate the two oxygenating mechanisms available to enzymes with a 2-His-1-carboxylate triad, depending on whether the electron source donates one or two electrons.
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    Proceedings of the National Academy of Sciences of the United States of America
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