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Publication Abstract from PubMed

The fungicide fragin, which contains a diazeniumdiolate moiety, exhibits a broad spectrum of biological activities. HamA, the key enzyme responsible for forming the nitrogen-nitrogen bond in this moiety, was investigated in this study. We determined the crystal structure of HamA at 2.0 A resolution, revealing a mononuclear iron center in the active site coordinated by both the "2His-1Glu" motif and an acetate group. Notably, HamA adopts a heme oxygenase-like fold, forming a hydrophobic cavity within a helical bundle that likely accommodates the substrate. Structural data confirmed the presence of an acetate and a formate group near the active site and microscale thermophoresis (MST) experiments further demonstrated HamA's ability to bind 2-oxoglutarate (2OG) with a dissociation constant (K (d)) of 208 +/- 1.42 muM. In summary, this study elucidates the 2OG-dependent heme-oxygenase-like enzyme HamA with a monoiron active center, providing critical structural insights into the mechanistic formation of the diazeniumdiolate moiety in fragin.

Structural basis of a 2-oxoglutarate-dependent heme-oxygenase-like enzyme HamA in fragin biosynthesis.,Su B, Zhang T, Yu Y, Liu H RSC Adv. 2025 Oct 15;15(46):38502-38509. doi: 10.1039/d5ra05203c. eCollection , 2025 Oct 14. PMID:41103923^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.