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Results 1 - 10 of 22 > >>
EC Number Application Commentary Reference
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9analysis assay of serum and urine for urea with use of urease and leucine dehydrogenase 349698
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9analysis cheap and rapid determination of branched-chain amino and oxo acids 349697
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9analysis flow-injection determination of branched-chain L-amino acids with immobilized leucine dehydrogenase 349678
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9analysis high-performance liquid chromatographic determination of branched-chain alpha-keto acids in serum using immobilized leucine dehydrogenase as post-column reactor 349699
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9analysis postcolumn co-immobilized leucine dehydrogenase-NADH oxidase reactor for the determination of branched-chain amino acids by high-performance liquid chromatography with chemiluminescence detection 349689
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9biotechnology an efficient stereospecific enzymatic synthesis of L-valine, L-leucine, L-norvaline, L-norleucine and L-isoleucine from the corresponding alpha-keto acids by coupling the reactions catalysed by leucine dehydrogenase and glucose dehydrogenase/galactose mutarotase. Giving high yields of L-amino acids, the procedure is economical and easy to perform and to monitor at a synthetically useful scale (1-10 g) 693504
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9drug development construction of bifunctional formate dehydrogenase and leucine dehydrogenase enzymatic complex for efficient cofactor regeneration and L-tert leucine biotransformation. L-tert leucine is a widely used chiral building block in many asymmetric reactions for the synthesis of anti-tumor and anti-HIV drugs -, 742376
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9synthesis coexpression with Bacillus megaterium glucose dehydrogenase in Escherichia coli for the production of L-tert-leucine. A decagram preparation of L-tert-leucine is performed at a substrate concentration of 0.6 M in 1 l scale with 99% conversion after 5.5 h, resulting in 80.1% yield and > 99% enantiomeric excess 743093
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9synthesis coexpression with NAD+-dependent FDH from Candida boidinii in Escherichia coli for synthesis of L-tert-leucine. In a continuous feeding process, at an overall substrate concentration up to 1.5 M, both conversion and enantiomeric excess of >99% and space-time yield of 786 g/l/d are achieved -, 741837
Show all pathways known for 1.4.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.9synthesis conversion of ammonia or urea into essential amino acids, L-Leu, L-Val, and L-Ile, using artificial cells containing an immobilized multienzyme system that consists of EC 1.1.1.1, EC 1.4.1.9, EC 3.5.1.5 and dextran-NAD+ 349696
Results 1 - 10 of 22 > >>