127103-94-0Relevant academic research and scientific papers
Studies on the inactivation of bovine liver enoyl-CoA hydratase by (methylenecyclopropyl)formyl-CoA: Elucidation of the inactivation mechanism and identification of cysteine-114 as the entrapped nucleophile
Dakoji,Li,Agnihotri,Zhou,Liu
, p. 9749 - 9759 (2007/10/03)
The inhibitory properties of (methylenecyclopropyl)formyl-CoA (MCPF-CoA), a metabolite derived from a natural amino acid, (methylenecyclopropyl)glycine, against bovine liver enoyl-CoA hydratase (ECH) were characterized. We have previously demonstrated tha
(R)-(-)- and (S)-(+)-Synadenol: synthesis, absolute configuration, and enantioselectivity of antiviral effect.
Qui, Yao-Ling,Hempel, Andrew,Camerman, Norman,Camerman, Arthur,Geiser, Fiona,et al.
, p. 5257 - 5264 (2007/10/03)
Synthesis of (R)-(-)- and (S)-(+)-synadenol (1a and 2a, 95-96% ee) is described. Racemic synadenol (1a + 2a) was deaminated with adenosine deaminase to give (R)-(-)-synadenol (1a) and (S)-(+)-hypoxanthine derivative 5. Acetylation of the latter compound g
Mechanistic study on the inactivation of general Acyl-CoA dehydrogenase by a metabolite of hypoglycin A
Lai, Ming-Tain,Liu, Li-Da,Liu, Hung-Wen
, p. 7388 - 7397 (2007/10/02)
General acyl-CoA dehydrogenase (GAD) is a flavin-dependent (FAD) enzyme that catalyzes the oxidation of a fatty acyl-CoA to the corresponding α,β-enolyl-CoA. When GAD is exposed to (methylenecyclopropyl)acetyl-CoA (MCPA-CoA), a metabolite of hypoglycin A
