2017
DOI: 10.1002/slct.201702128
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High Resolution Crystal Structures of the Acetohydroxyacid Synthase‐Pyruvate Complex Provide New Insights into Its Catalytic Mechanism

Abstract: Acetohydroxyacid synthase (AHAS) is the first enzyme in the biosynthesis pathway of the branched‐chain amino acids, catalyzing the condensation of pyruvate with another molecule of pyruvate or with 2‐ketobutyrate, to produce 2‐acetolactate or 2‐acetohydroxybutyrate, respectively. The catalytic subunit of the dimeric enzyme has thiamin diphosphate (ThDP), a divalent metal ion, flavin adenine dinucleotide (FAD), and two molecules of oxygen (O2(I) and O2(II)) as cofactors. Here, crystal structures of Saccharomyce… Show more

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Cited by 10 publications
(10 citation statements)
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“…6(C)) and, by extension, resistance to this herbicide in E. crus‐galli . These results were consistent with those previous reports stating that Phe‐206 plays a key role in herbicide binding and the maintenance of ALS catalytic activity 10, 47–49 …”
Section: Discussionsupporting
confidence: 93%
See 1 more Smart Citation
“…6(C)) and, by extension, resistance to this herbicide in E. crus‐galli . These results were consistent with those previous reports stating that Phe‐206 plays a key role in herbicide binding and the maintenance of ALS catalytic activity 10, 47–49 …”
Section: Discussionsupporting
confidence: 93%
“…These results were consistent with those previous reports stating that Phe-206 plays a key role in herbicide binding and the maintenance of ALS catalytic activity. 10,[47][48][49] Actually, the RIs were all comparable between the whole-plant (10.8 and 4.1) and enzyme test (6.0 and 8.1). If the mutation frequency (the Phe-206-Leu mutation frequency in E. crus-galli was <100%) and the dilution effect 8 of multiple ALS gene copies (three ALS genes copies were observed in the allohexaploid E. crus-galli 13,14 and only one copy mutant) were taken into account, the Phe-206-Leu might contribute limited to penoxsulam resistance.…”
Section: Confirmation Of the Phe-206-leu Mutation Conferring Als Herb...mentioning
confidence: 72%
“…The overall structures of ThAHAS and ThAHAS-HA complex are almost identical, with a root-mean-square (rms) deviation of 0.166 Å for 511 Cα atoms between them (Figure S10). The two active sites are located at the dimer interface and are on opposite sides of the complex, as observed in SceAHAS . Unambiguous electron densities for Mg 2+ , FAD, and thiamine thiazolone diphosphate (ThThDP) are found in both monomers in both ThAHAS and ThAHAS-HA structures (Figure S12).…”
Section: Results and Discussionmentioning
confidence: 75%
“…The two active sites are located at the dimer interface and are on opposite sides of the complex, as observed in SceAHAS. 54 Unambiguous electron densities for Mg 2+ , FAD, and thiamine thiazolone diphosphate (ThThDP) are found in both monomers in both ThAHAS and ThAHAS-HA structures (Figure S12). The isoalloxazine rings of FAD molecules are essentially planar.…”
Section: Journal Of the American Chemical Societymentioning
confidence: 99%
“… a Stereoview of At AHAS (PDB code: 5K6Q 30 ) with pyruvate (Pyr_1 and Pyr_2) and an intact ThDP cofactor modeled. This model is based on the structure of the highly homologous Saccharomyces cerevisiae AHAS ( Sc AHAS), whose structure has been solved in complex with pyruvate (PDB code: 6BD9 37 ). The first pyruvate interacts with W574 through an anion–π interaction.…”
Section: Introductionmentioning
confidence: 99%