An evaluation of the substrate specificity and asymmetric synthesis potential of the cloned L-lactate dehydrogenase from Bacillusstearothermophilus

التفاصيل البيبلوغرافية
العنوان: An evaluation of the substrate specificity and asymmetric synthesis potential of the cloned L-lactate dehydrogenase from Bacillusstearothermophilus
المؤلفون: Marcel A. Luyten, J. John Holbrook, Anthony R. Clarke, Marvin Gold, J. Bryan Jones, Louis Provencher, James D. Friesen, Daniel Bur, Hla Wynn
المصدر: Canadian Journal of Chemistry. 67:1065-1070
بيانات النشر: Canadian Science Publishing, 1989.
سنة النشر: 1989
مصطلحات موضوعية: Stereospecificity, Biochemistry, Chemistry, Stereochemistry, Organic Chemistry, Enantioselective synthesis, Substrate specificity, Dehydrogenase, L-Lactate dehydrogenase, General Chemistry, Branched-chain alpha-keto acid dehydrogenase complex, Catalysis
الوصف: The potential utility of the L-lactate dehydrogenase of Bacillusstearothermophilus (BSLDH) for stereospecific, preparative-scale reductions of α-keto acids to (S)-α-hydroxy acids of > 99% ee has been demonstrated. BSLDH is a stable, thermophilic, enzyme whose gene has been cloned into a high-expression vector to assure its plentiful supply. Its specificity for keto acid substrates possessing straight- and branched-chain alkyl, cyclopropyl, or phenyl groups has been evaluated in preparative and kinetic terms, and compared with that of the mammalian pig heart enzyme (PHLDH). The specificities of BSLDH and PHLDH are similar, with branched alkyl-chain keto acids being poor substrates for both enzymes. Keywords: enzymes in organic syntheses, lactate dehydrogenase, asymmetric synthesis.
تدمد: 1480-3291
0008-4042
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::c4cd8564150c7c59cd588278b16c31b2Test
https://doi.org/10.1139/v89-161Test
حقوق: CLOSED
رقم الانضمام: edsair.doi...........c4cd8564150c7c59cd588278b16c31b2
قاعدة البيانات: OpenAIRE