Heidi Therese Hillier

ORCID: 0000-0003-4995-2224
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About
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Research Areas
  • Microbial Metabolic Engineering and Bioproduction
  • Enzyme Catalysis and Immobilization
  • Enzyme Structure and Function
  • Diet and metabolism studies
  • Biofuel production and bioconversion
  • Protein Structure and Dynamics
  • Soil Carbon and Nitrogen Dynamics
  • Metal-Catalyzed Oxygenation Mechanisms
  • Metabolomics and Mass Spectrometry Studies
  • Metabolism and Genetic Disorders
  • Microbial Community Ecology and Physiology

UiT The Arctic University of Norway
2020

Uppsala University
2018

ADH-A from Rhodococcus ruber DSM 44541 catalyzes the oxidation of (S)-1-phenylethanol 3000-fold more efficiently as compared with 2-hydroxylated derivative (R)-phenylethane-1,2-diol. The enzyme is also highly selective for sec-alcohols comparably low activities corresponding primary alcohols. When challenged a substrate containing two secondary alcohols, such 1-phenylpropane-(1R,2S)-diol, favors benzylic carbon this alcohol. catalytic efficiency, however, modest in comparison to activity...

10.1021/acscatal.8b01762 article EN ACS Catalysis 2018-07-05

l ‐2,4‐diaminobutyric acid (DABA) aminotransferases can catalyze the formation of amines at distal ω‐position substrates, and is intial rate‐limiting enzyme in biosynthesis pathway cytoprotecting molecule ( S )‐2‐methyl‐1,4,5,6‐tetrahydro‐4‐pyrimidine carboxylic (ectoine). Although there an industrial interest ectoine, DABA remain poorly characterized. Herein, we present crystal structure EctB (2.45 Å), a aminotransferase from Chromohalobacter salexigens DSM 3043, well‐studied organism with...

10.1111/febs.15265 article EN cc-by FEBS Journal 2020-02-29
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