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Differential Recognition of Chirality at C‐2 of 2‐Fluoro‐ and 2‐Methylmevalonate by Mevalonate Kinase – Absolute Configuration of Enzymatically Active 2‐Fluoromevalonate
Author(s) -
Wilde Jürgen,
Eggerer Hermann
Publication year - 1997
Publication title -
liebigs annalen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 0947-3440
DOI - 10.1002/jlac.199719970320
Subject(s) - chemistry , absolute configuration , substituent , chirality (physics) , stereochemistry , yield (engineering) , conformational isomerism , organic chemistry , molecule , chiral symmetry breaking , physics , materials science , quantum mechanics , nambu–jona lasinio model , metallurgy , quark
Abstract Both 2‐methyl‐ and 2‐fluoromevalonate are alternative substrates of mevalonate kinase, but only the fluorinated compound is phorphorylated stereospecifically with respect to the chiral C‐2. The absolute configuration of the racemic pairs of 2‐fluoromevalonate is deduced from 1 H‐ and 13 C‐NMR data. The fluorine substituent shifts the equilibrium between the conformers of mevalolactone. Coupling constants found experimentally for 2‐fluoromevalonate are calculated satisfactorily with INDO‐MO data. Enzymatic analysis of components of the racemic pairs of 2‐fluoromevalonate with mevalonate kinase combined with NMR data yield the absolute configuration of the enzymatically active steroisomer, (2 R ,3 R )‐2‐fluoromevalonate.