Zobrazeno 1 - 6
of 6
pro vyhledávání: '"John E. Hung"'
Autor:
Amoolya H. Singh, Benjamin B. Kaufmann-Malaga, Joshua A. Lerman, Daniel P. Dougherty, Yang Zhang, Alexander L. Kilbo, Erin H. Wilson, Chiam Yu Ng, Onur Erbilgin, Kate A. Curran, Christopher D. Reeves, John E. Hung, Simone Mantovani, Zachary A. King, Marites J. Ayson, Judith R. Denery, Chia-Wei Lu, Phillip Norton, Carol Tran, Darren M. Platt, Joel R. Cherry, Sunil S. Chandran, Adam L. Meadows
Engineering microbes to synthesize molecules of societal value has historically been a time consuming and artisanal process, with the synthesis of each new non-native molecule typically warranting its own separate publication. Because most microbial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::494b4676c035c6da704381c0cce91660
https://doi.org/10.1101/2023.01.03.521657
https://doi.org/10.1101/2023.01.03.521657
Autor:
John E Hung, Emily J Fogle, Neha Garg, Jonathan R Chekan, Satish K Nair, Wilfred A van der Donk
Publikováno v:
PLoS ONE, Vol 9, Iss 1, p e87134 (2014)
Phosphite dehydrogenase (PTDH) catalyzes the NAD(+)-dependent oxidation of phosphite to phosphate. This reaction requires the deprotonation of a water nucleophile for attack on phosphite. A crystal structure was recently solved that identified Arg301
Externí odkaz:
https://doaj.org/article/8f14d8f1e6b641e0be15c0454b41523a
Autor:
John E. Hung, Tiddo J. Mooibroek, Derek N. Woolfson, Jeremy N. Harvey, Kara E. Ranaghan, Adrian J. Mulholland, Wilfred A. van der Donk, Gail J. Bartlett
Publikováno v:
Chem. Sci.. 5:2191-2199
Combined quantum mechanics/molecular mechanics (QM/MM) simulations of the reaction catalysed by phosphite dehydrogenase (PTDH) identify Met53 as important for catalysis. This catalytic role is verified by experiments (including replacement by norleuc
Autor:
Wilfred A. van der Donk, Tyler W. Johannes, Huimin Zhao, Emily J. Fogle, Harry D. Christman, William W. Metcalf, John E. Hung
Publikováno v:
Biochemistry
Phosphite dehydrogenase (PTDH) from Pseudomonas stutzeri catalyzes the nicotinamide adenine dinucleotide-dependent oxidation of phosphite to phosphate. The enzyme belongs to the family of D-hydroxy acid dehydrogenases (DHDHs). A search of the protein
Autor:
Christopher P. Mill, Julie A. Francois, Aaron E. Ransome, Richard K. Wilson, Jyothi Thimmapuram, Vincent Magrini, Ketaki Bhide, Lucinda Fulton, Sandra W. Clifton, T. Joseph Kappock, John E. Hung
Publikováno v:
Genome Announcements
The genome sequence of Acetobacter aceti 1023, an acetic acid bacterium adapted to traditional vinegar fermentation, comprises 3.0 Mb (chromosome plus plasmids). A. aceti 1023 is closely related to the cocoa fermenter Acetobacter pasteurianus 386B bu
Autor:
Wilfred A. van der Donk, Satish K. Nair, Emily J. Fogle, Neha Garg, Jonathan R. Chekan, John E. Hung
Publikováno v:
PLoS ONE, Vol 9, Iss 1, p e87134 (2014)
PLoS ONE
PLoS ONE
Phosphite dehydrogenase (PTDH) catalyzes the NAD(+)-dependent oxidation of phosphite to phosphate. This reaction requires the deprotonation of a water nucleophile for attack on phosphite. A crystal structure was recently solved that identified Arg301