ArticleApplied and environmental microbiology2026
Rational selection of ketopantoate hydroxymethyltransferase with low product feedback inhibition based on binding free energy calculation analysis.
Article in Applied and environmental microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The microbial production of pantothenic acid (d-PA) is critically limited by feedback inhibition and low activity of the key enzyme ketopantoate hydroxymethyltransferase (KPHMT). To overcome this, rational enzyme mining based on computational prediction was established. Following sequence conservation analysis, molecular dynamics simulations, and binding free energy (ΔG) calculations, five representative native KPHMT enzymes were selected for experimental validation:
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