7EEH

Selenomethionine labeled Fe(II)/(alpha)ketoglutarate-dependent dioxygenase TqaL

Summary for 7EEH

• Entry DOI: 10.2210/pdb7eeh/pdb
• Descriptor: TqaL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, FE (III) ION, ... (4 entities in total)
• Functional Keywords: alpha-ketoglutarate dependent dioxygenase, aziridine, biosynthesis, oxidoreductase
• Biological source: Neurospora crassa
• Total number of polymer chains: 4
• Total formula weight: 144644.72

Authors

Bunno, R.,Mori, T.,Awakawa, T.,Abe, I. (deposition date: 2021-03-18, release date: 2021-05-26, Last modification date: 2024-11-13)

Primary citation

Bunno, R.,Awakawa, T.,Mori, T.,Abe, I.
Aziridine Formation by a Fe II / alpha-Ketoglutarate Dependent Oxygenase and 2-Aminoisobutyrate Biosynthesis in Fungi.
Angew.Chem.Int.Ed.Engl., 60:15827-15831, 2021

PubMed Abstract: Aziridine is a characteristically reactive molecule with increased bioactivity due to its strained ring structure. Here, we investigated the biosynthesis of 2-aminoisobutyric acid (AIB) in Penicillium, and successfully reconstituted the three-step biosynthesis from L-Val to AIB in vitro. This previously unknown aziridine formation pathway proceeded with the non-heme iron and α-ketoglutarate-dependent (Fe /αKG) oxygenase TqaL, followed by aziridine ring opening by the haloalkanoic acid dehalogenase (HAD)-type hydrolase TqaF, and subsequent oxidative decarboxylation by the NovR/CloR-like non-heme iron oxygenase TqaM. Furthermore, the X-ray crystal structure of the C-N bond forming Fe /αKG oxygenase TqaL was solved at 2.0 Å resolution. This work presents the first molecular basis for aziridine biogenesis, thereby expanding the catalytic repertoire of the Fe /αKG oxygenases. We also report the unique aziridine ring opening by a HAD-type hydrolase and the remarkable oxidative decarboxylation by a non-heme iron oxygenase to produce AIB.

PubMed: 33973699
DOI: 10.1002/anie.202104644

Experimental method

X-RAY DIFFRACTION (2 Å)