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X-WR-CALNAME:ChemE Dept. Seminar Series: Monica E. Neugebauer
X-WR-TIMEZONE:Eastern Time (US & Canada)
BEGIN:VEVENT
DTSTAMP:20261008T104811Z
UID:tag:localist.com\,2008:EventInstance_42412905278289
DTSTART:20230227T201500Z
DTEND:20230227T211500Z
DESCRIPTION:Evolving Enzymes for Biocatalysis and Gene Editing\n\nMonica E.
  Neugebauer\n\nBroad Institute of MIT and Harvard \n\nEnzymes catalyze che
 mical transformations with exquisite selectivity. Through directed evoluti
 on\, we can reprogram enzymes for applications in biocatalysis and medicin
 e. In the first part\, I will discuss my work to discover\, characterize\,
  and engineer FeII/α-ketoglutarate-dependent enzymes that halogenate unac
 tivated Csp3—H bonds. I solved the anaerobic crystal structure of a nove
 l lysine halogenase (BesD)\, discovered homologs that enable the formation
  of nine new chlorinated amino acids\, and developed enzymatic cascades to
  produce chlorinated heterocycles\, diamines\, keto-acids\, and peptides. 
 Through structural studies and high-throughput screening\, I investigated 
 the mechanistic basis for regioselectivity and catalytic selectivity withi
 n this enzyme family and used the resulting insights to engineer hydroxyla
 ses to perform halogenation with activity and selectivity comparable to th
 at of native halogenases. In a second story\, I developed novel cytosine b
 ase editors (CBEs) through directed evolution. Base editors consist of a p
 rogrammable DNA binding protein\, such as catalytically impaired Cas9\, fu
 sed to a deaminase enzyme\, and enable precise nucleotide changes within a
  target site in the genome. CBEs\, which convert C•G base pairs into T
 •A\, are typically larger and have more undesired off-target editing tha
 n their adenine base editor (ABE) counterparts. To develop a new class of 
 CBEs that retain the favorable properties of ABEs\, I used continuous prot
 ein evolution to evolve ABEs to instead perform highly efficient cytosine 
 base editing within therapeutically relevant sites and cell types. These n
 ewly evolved base editors overcome several limitations of existing CBEs an
 d demonstrate the power of protein evolution for addressing challenges in 
 biotechnology.
GEO:42.361054;-71.088332
LOCATION:Building 66\, 66-110
SUMMARY:ChemE Dept. Seminar Series: Monica E. Neugebauer
URL;VALUE=URI:https://calendar.mit.edu/event/cheme_dept_seminar_series_jaso
 n_s_adams_8872
CATEGORIES:Conferences/Seminars/Lectures
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