Enzymatic Hydration Data for Enoyl-PAN Thioesters with ADP Activator

Experimental data from a study on the enantioselective hydration of non-CoA enoyl-thioesters by enoyl-CoA hydratase (ECH). The research demonstrates the activation of the enzyme's active site using 3′,5′-ADP (PAP) to enable catalysis on a wide range of (2E)-enoyl-PAN substrates, yielding products with excellent stereoselectivity (typically >99:1 3S:3R).

Use Cases

• Analyze the relationship between the ADP activator and the structural tightening of the active site oxyanion hole, as described in the structural enzymology findings.
• Model the catalytic efficiency of ECH for different (2E)-enoyl-PAN substrates with varying steric demands and functionalities.
• Validate the reported stereoselectivity outcomes (3S:3R ratios) for synthesized 3-hydroxyacyl-PAN thioester products.
• Investigate the absence of side products, such as cyclization, for acyl chains containing reactive groups like bromide or methyl ester functionalities.

Strengths

• Data supports findings of excellent stereoselectivity, with product ratios typically exceeding 99:1 3S:3R.
• Study demonstrates the synthetic utility of ECH across a wide range of (2E)-enoyl-PAN substrates with different functionalities.
• Structural enzymology insights detail specific atomic distance changes (e.g., NN distance from 5.2 Å to 4.0 Å) in the active site upon activator binding.

Limitations

• The dataset is relatively small at 73.6 MB, limiting the scale of potential computational analysis.
• Specific data structure (e.g., row/column count, file contents) is not described, making initial assessment difficult.
• Data is focused on a specific enzymatic system and may not be generalizable to other CoA-dependent enzymes or reaction types.

Provenance

Source

Figshare, authored by Subhadra Dalwani.

Collection Method

Experimental data from enzymology and synthetic chemistry studies, likely including spectroscopic and chromatographic analyses.

Time Range

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Freshness

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Geography

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