159835-34-4Relevant academic research and scientific papers
Microbial whole cell-catalyzed desymmetrization of prochiral malonamides: Practical synthesis of enantioenriched functionalized carbamoylacetates and their application in the preparation of unusual α-amino acids
Zhang, Li-Bin,Wang, De-Xian,Wang, Mei-Xiang
, p. 5604 - 5609 (2011/08/10)
Catalyzed by Rhodococcus erythropolis AJ270, an amidase-containing microbial whole cell catalyst, under very mild conditions, a number of functionalized prochiral malonamides underwent enantioselective desymmetrization reaction to afford high yield of car
2-Benzyl-2-methylsuccinic acid as inhibitor for carboxypeptidase A. synthesis and evaluation
Lee, Mijoon,Jin, Yonghao,Kim, Dong H.
, p. 1755 - 1760 (2007/10/03)
Recently, Asante-Appiah et al. (Asante-Appiah, E.; Seetharaman, J.; Sicheri, F.; Yang, D. S.-C.; Chan, W. W.-C. Biochemistry 1997, 36, 8710-8715) reported that 2-ethyl-2-methylsuccinic acid is a highly potent inhibitor for carboxypeptidase A (CPA), a prototypic zinc protease. The X-ray crystal structure of the complex of the enzyme formed with 2-ethyl-2-methylsuccinic acid revealed that at the active site of CPA there is present a small cavity which accommodates the methyl group of the inhibitor. These investigators postulated that incorporation of a methyl group at the α-position to the carboxylate of existing inhibitors of CPA would improve the inhibitory potency. We have synthesized racemic and optically active 2-benzyl-2-methylsuccinic acids and evaluated their inhibitory activities for CPA to find the K(i) values to be 0.28, 0.15, and 17μM for racemic form, (R)-, and (S)-enantiomer, respectively. Contrary to the expectation, the effect on the binding affinity by the incorporation of the methyl group is minimal. The validity of the proposition that the small cavity may be utilized for the improvement of the inhibitory potency appears questionable. Copyright (C) 1999 Elsevier Science Ltd.
