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Milton J. Zmijewski

Researcher at Eli Lilly and Company

Publications -  38
Citations -  437

Milton J. Zmijewski is an academic researcher from Eli Lilly and Company. The author has contributed to research in topics: Phthalyl amidase & Amidase. The author has an hindex of 11, co-authored 38 publications receiving 429 citations. Previous affiliations of Milton J. Zmijewski include University of Utah.

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Large-scale stereoselective enzymatic ketone reduction with in situ product removal via polymeric adsorbent resins

TL;DR: The NAD(P)H-dependent enzymatic activity within living Zygosaccharomyces rouxii was utilized to accomplish this reaction and the reaction was scaled-up to a volume of 300 l by utilizing a commercially available agitated filter as a reactor.
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Enantioselective acylation of a beta-lactam intermediate in the synthesis of loracarbef using penicillin G amidase

TL;DR: Penicillin G amidase from E. coli has been shown to selectively acylate, in an efficient manner, the (2R,3S) isomer of a cis, racemic azetidinone intermediate used in a synthesis of loracarbef, a carbacephalosporin antibiotic.
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Enzymatic deacylation of teicoplanin followed by reductive alkylation: synthesis and antibacterial activity of new glycopeptides.

TL;DR: Novel glycopeptides derived from teicoplanin were prepared and evaluated for activity against antibiotic-resistant gram-positive pathogens and some had potent activity against both staphylococci and glycopePTide-resistant enterococci.
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Biosynthesis of vancomycin: identification of TDP-glucose: aglycosyl-vancomycin glucosyltransferase from Amycolatopsis orientalis

TL;DR: Gel filtration studies demonstrated that all the enzyme activity eluted from the column at a molecular weight of 44 kDa, the first report of an enzyme activity that appears to be associated with the biosynthesis of glycopeptide antibiotics.
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Purification, characterization, cDNA cloning and expression of a novel ketoreductase from Zygosaccharomyces rouxii

TL;DR: A novel ketoreductase isolated from Zygosaccharomyces rouxii catalyzes the asymmetric reduction of selected ketone substrates of commercial importance and substrate specificity, lack of a catalytic metal, and extent of protein sequence identity to known reductases suggests that the enzyme falls into the carbonyl reductase enzyme class.