M
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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Journal ArticleDOI
Large-scale stereoselective enzymatic ketone reduction with in situ product removal via polymeric adsorbent resins
Jeffrey Thomas Vicenzi,Milton J. Zmijewski,Reinhard Matthew Robert,Bryan E. Landen,Muth William Lawrence,Paul G. Marler +5 more
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.
Nancy June Snyder,Robin D. G. Cooper,Barbara Shreve Briggs,Milton J. Zmijewski,Deborah L. Mullen,Raymond E. Kaiser,Thalia I. Nicas +6 more
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
Colleen A. Costello,Robert Allen Payson,Michael Andrew Menke,Jeffrey Lynn Larson,Keith A. Brown,Joseph E. Tanner,Raymond E. Kaiser,Charles Lee Hershberger,Milton J. Zmijewski +8 more
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.