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• W2019982170 abstract "The catalytic cycle of the ATP/Mg 2+ -dependent enzyme β-lactam synthetase (β-LS) from Streptomyces clavuligerus has been observed through a series of x-ray crystallographic snapshots. Chemistry is initiated by the ordered binding of ATP/Mg 2+ and N 2 -(carboxyethyl)- l -arginine (CEA) to the apoenzyme. The apo and ATP/Mg 2+ structures described here, along with the previously described CEA⋅α,β-methyleneadenosine 5′-triphosphate (CEA⋅AMP-CPP)/Mg 2+ structure, illuminate changes in active site geometry that favor adenylation. In addition, an acyladenylate intermediate has been trapped. The substrate analog N 2 -(carboxymethyl)- l -arginine (CMA) was adenylated by ATP in the crystal and represents a close structural analog of the previously proposed CEA-adenylate intermediate. Finally, the structure of the ternary product complex deoxyguanidinoproclavaminic acid (DGPC)⋅AMP/PP i /Mg 2+ has been determined. The CMA-AMP/PP i /Mg 2+ and DGPC⋅AMP/PP i /Mg 2+ structures reveal interactions in the active site that facilitate β-lactam formation. All of the ATP-bound structures differ from the previously described CEA⋅AMP-CPP/Mg 2+ structure in that two Mg 2+ ions are found in the active sites. These Mg 2+ ions play critical roles in both the adenylation and β-lactamization reactions." @default.
• W2019982170 created "2016-06-24" @default.
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• W2019982170 date "2002-10-30" @default.
• W2019982170 modified "2023-09-30" @default.
• W2019982170 title "The catalytic cycle of β-lactam synthetase observed by x-ray crystallographic snapshots" @default.
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• W2019982170 doi "https://doi.org/10.1073/pnas.232361199" @default.
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