2018
DOI: 10.1039/c7np00067g
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Recent examples of α-ketoglutarate-dependent mononuclear non-haem iron enzymes in natural product biosyntheses

Abstract: Covering: up to 2018 α-Ketoglutarate (αKG, also known as 2-oxoglutarate)-dependent mononuclear non-haem iron (αKG-NHFe) enzymes catalyze a wide range of biochemical reactions, including hydroxylation, ring fragmentation, C-C bond cleavage, epimerization, desaturation, endoperoxidation and heterocycle formation. These enzymes utilize iron(ii) as the metallo-cofactor and αKG as the co-substrate. Herein, we summarize several novel αKG-NHFe enzymes involved in natural product biosyntheses discovered in recent year… Show more

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Cited by 146 publications
(148 citation statements)
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References 360 publications
(447 reference statements)
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“…Synteny analysis of BGCs for mycins and peptins production revealed a set of 2 or 3 convergent genes of unknown function that are found, in many producers, right upstream of the mycin cluster. The two first genes encode for, respectively, a putative membrane-anchored protein with a periplasmic JmjC-family hydroxylase domain (Gao et al 2018) and an unknown MFS efflux protein (DHA3 family; transporter classification TC 2.A.1.21). The third gene, absent from some clusters (e.g.…”
Section: Conserved Accessory and Unknown Genesmentioning
confidence: 99%
“…Synteny analysis of BGCs for mycins and peptins production revealed a set of 2 or 3 convergent genes of unknown function that are found, in many producers, right upstream of the mycin cluster. The two first genes encode for, respectively, a putative membrane-anchored protein with a periplasmic JmjC-family hydroxylase domain (Gao et al 2018) and an unknown MFS efflux protein (DHA3 family; transporter classification TC 2.A.1.21). The third gene, absent from some clusters (e.g.…”
Section: Conserved Accessory and Unknown Genesmentioning
confidence: 99%
“…α-KG-Hals belong to the superfamily of α-ketoglutarate-dependent oxygenases (α-KGOs), a diverse family of enzymes that catalyzes hydroxylation, epoxidation, epimerization, demethylation, ring formation, C-C bond cleavage and desaturation reactions. [154,155] α-KG-Hals are structurally and mechanistically related to α-KG-oxygenases, which follow a radical mechanism via formation of a high valent and short-lived Fe IV = O ferryl intermediate ( Figure 1). [156,157] This intermediate is a powerful oxidant that abstracts an hydrogen from un-activated carbon-hydrogen bond creating a substrate radical and another Fe III -hydroxyl (or Chloride) intermediate.…”
Section: Nonheme Fe (Ii)-α-ketoglutarate-dependent Halogenases (α-Kg-mentioning
confidence: 99%
“…There are some excellent reviews on the enzymology and halogenation mechanism of α-KG-Hal and α-KGO superfamily of enzymes for further reading. [154,155,177]…”
Section: Nonheme Fe (Ii)-α-ketoglutarate-dependent Halogenases (α-Kg-mentioning
confidence: 99%
“…Aromatic amino acid hydroxylases represent a small but important group of enzymes responsible for a series of metabolically essential transformations, including the hydroxylation of l ‐tyrosine, l ‐tryptophan or l ‐phenylalanine to yield l ‐DOPA, 5‐hydroxy‐ l ‐tryptophan or l ‐tyrosine, respectively . These non‐heme‐iron‐dependent enzymes bind their metal cofactor at the active site with one glutamate and two histidine residues, a binding mode that is also found in other non‐heme‐iron enzymes such as the α‐ketoglutarate‐dependent dioxygenases . A significant difference from other non‐heme‐iron‐dependent enzymes is the requirement for tetrahydropterin as an additional cofactor.…”
Section: Introductionmentioning
confidence: 99%