J
James Hennessy
Researcher at Australian National University
Publications - 20
Citations - 254
James Hennessy is an academic researcher from Australian National University. The author has contributed to research in topics: Catalysis & Cell-free protein synthesis. The author has an hindex of 7, co-authored 20 publications receiving 204 citations.
Papers
More filters
Journal ArticleDOI
Membranes from academia to industry
TL;DR: The perks and pitfalls of membrane research and development are talked about, and how activities at the new Barrer Centre might lead to next-generation separation technologies.
Journal ArticleDOI
Clostridium carboxidivorans strain P7T recombinant formate dehydrogenase catalyzes reduction of CO(2) to formate.
Apostolos Alissandratos,Hye-Kyung Kim,Hayden Matthews,James Hennessy,Amy Philbrook,Christopher J. Easton +5 more
TL;DR: Recombinant formate dehydrogenase from the acetogen Clostridium carboxidivorans strain P7T, expressed in Escherichia coli, shows particular activity towards NADH-dependent carbon dioxide reduction to formate due to the relative binding affinities of the substrates and products.
Journal ArticleDOI
ATP Recycling with Cell Lysate for Enzyme-Catalyzed Chemical Synthesis, Protein Expression and PCR.
TL;DR: In this paper, the utility of this ATP recycling strategy in enzyme-catalyzed chemical synthesis is illustrated through the conversion of uridine to UMP by the lysate from recombinant overexpression of URINE with the E. coli.
Journal ArticleDOI
Cofactor promiscuity among F 420 -dependent reductases enables them to catalyse both oxidation and reduction of the same substrate
Gauri V. Lapalikar,Matthew C. Taylor,Andrew C. Warden,Hideki Onagi,James Hennessy,Roger J. Mulder,Colin Scott,Susan E. Brown,Robyn J. Russell,Christopher J. Easton,John G. Oakeshott +10 more
TL;DR: This work reports that three FDRs from Mycobacterium smegmatis also exhibit a different catalytic function towards some aflatoxins through the use of a different cofactor, the first example of an enzyme showing promiscuity for its cofactor leading to divergence of function against the same substrate.
Journal ArticleDOI
Incorporation of chlorinated analogues of aliphatic amino acids during cell-free protein synthesis
Dannon J. Stigers,Zachary I. Watts,James Hennessy,Hye-Kyung Kim,Romeo Martini,Matthew C. Taylor,Kiyoshi Ozawa,Jeffrey W. Keillor,Nicholas E. Dixon,Christopher J. Easton +9 more
TL;DR: 3-Chloro-Abu and 4-chloro-Nva are biosynthetically incorporated into E. coli peptidyl-Pro cis-trans isomerase B, as substitutes for Val and Leu, respectively, and substituted protein is catalytically active.