Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Woojoo E. Kim"'
Autor:
Jeffrey T. Mindrebo, Ashay Patel, Woojoo E. Kim, Tony D. Davis, Aochiu Chen, Thomas G. Bartholow, James J. La Clair, J. Andrew McCammon, Joseph P. Noel, Michael D. Burkart
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
The formation of C-C bonds in fatty acid and polyketide biosynthesis depends on β-ketoacyl-acyl carrier protein (ACP) synthases (KSs). Here, the authors present structures of E.coli KSs bound to substrate mimetic bearing ACPs, providing insights int
Externí odkaz:
https://doaj.org/article/8b2f324577e8467b8bb69a969b0ffd83
Autor:
Lorillee Tallorin, JiaLei Wang, Woojoo E. Kim, Swagat Sahu, Nicolas M. Kosa, Pu Yang, Matthew Thompson, Michael K. Gilson, Peter I. Frazier, Michael D. Burkart, Nathan C. Gianneschi
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
The discovery of peptide substrates for enzymes with selective activities is a central goal in chemical biology. Here, the authors develop a hybrid method combining machine learning and experimental testing for fast optimization of peptides for speci
Externí odkaz:
https://doaj.org/article/d9ae7a50ccf5436cb95b497dfe663903
Autor:
Aochiu Chen, Jeffrey T. Mindrebo, Tony D. Davis, Woojoo E. Kim, Yohei Katsuyama, Ziran Jiang, Yasuo Ohnishi, Joseph P. Noel, Michael D. Burkart
Publikováno v:
Acta crystallographica. Section D, Structural biology. 78(Pt 9)
Ketosynthases (KSs) catalyse essential carbon–carbon bond-forming reactions in fatty-acid biosynthesis using a two-step, ping-pong reaction mechanism. In Escherichia coli, there are two homodimeric elongating KSs, FabB and FabF, which possess overl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09ddac663ab6c89e806b5195c14705f5
https://pubmed.ncbi.nlm.nih.gov/36048156
https://pubmed.ncbi.nlm.nih.gov/36048156
Autor:
Aochiu Chen, Jeffrey T. Mindrebo, Tony D. Davis, Woojoo E. Kim, Yohei Katsuyama, Ziran Jiang, Yasuo Ohnishi, Joseph P. Noel, Michael D. Burkart
Ketosynthases (KS) catalyse essential carbon-carbon bond forming reactions in fatty acid biosynthesis using a two-step, ping-pong reaction mechanism. In E. coli, there are two homodimeric elongating KSs, FabB and FabF, both of which possess overlappi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::22b6f1dac41ec51eb2215919587db698
https://doi.org/10.1101/2022.04.04.486996
https://doi.org/10.1101/2022.04.04.486996
Autor:
Woojoo E. Kim, Fumihiro Ishikawa, Rebecca N. Re, Takehiro Suzuki, Naoshi Dohmae, Hideaki Kakeya, Genzoh Tanabe, Michael D. Burkart
Publikováno v:
RSC chemical biology, vol 3, iss 3
Nonribosomal peptide synthetases (NRPSs) are complex multi-modular enzymes containing catalytic domains responsible for the loading and incorporation of amino acids into natural products. These unique molecular factories can produce peptides with non
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8393d800bc0531b5ae6cca362ca67907
https://pubmed.ncbi.nlm.nih.gov/35359491
https://pubmed.ncbi.nlm.nih.gov/35359491
Autor:
Jeffrey T. Mindrebo, Aochiu Chen, Woojoo E. Kim, Rebecca N. Re, Tony D. Davis, Joseph P. Noel, Michael D. Burkart
Publikováno v:
ACS Catal
Ketosynthases (KSs) catalyze carbon-carbon bond forming reactions in fatty acid synthases (FASs) and polyketide synthases (PKSs). KSs utilize a two-step ping pong kinetic mechanism to carry out an overall decarboxylative thio-Claisen condensation tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fe1cb1dc8d76dc847171902e6bdcee6
https://europepmc.org/articles/PMC9524369/
https://europepmc.org/articles/PMC9524369/
Autor:
Katherine Charov, James J. La Clair, Ramunas Stepanauskas, Eric D. Becraft, Frederik Schulz, Woojoo E. Kim, Michael D. Burkart, Mária Džunková, Tanja Woyke, Julia M. Brown
Publikováno v:
ACS Chemical Biology .
ACS Chem Biol
ACS chemical biology, vol 16, iss 5
ACS Chem Biol
ACS chemical biology, vol 16, iss 5
While thousands of environmental metagenomes have been mined for the presence of novel biosynthetic gene clusters, such computational predictions do not provide evidence of their in vivo biosynthetic functionality. Using a fluorescent in situ enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46df94df8e87c2c647f2073ecdb31c2f
http://oceanrep.geomar.de/52609/
http://oceanrep.geomar.de/52609/
Autor:
Aochiu Chen, Michael D. Burkart, Jeffrey T. Mindrebo, Joseph P. Noel, Tony D. Davis, Rebecca N. Re, Woojoo E. Kim
Ketosynthases (KSs) catalyze carbon-carbon bond forming reactions in fatty acid synthases (FASs) and polyketide synthases (PKSs). KSs utilize a two-step ping pong kinetic mechanism to carry out an overall decarboxylative thio-Claisen condensation tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f18dd97b5b465f22011ab467b06e1c22
https://doi.org/10.1101/2021.02.13.431092
https://doi.org/10.1101/2021.02.13.431092
Autor:
Jeffrey T. Mindrebo, Michael D. Burkart, James J. La Clair, Ashay Patel, Qing Zhe Ni, Woojoo E. Kim, Tony D. Davis, Laëtitia Misson
Fatty acid and polyketide synthases catalyze the same core reactions. They utilize an acyl carrier protein (ACP), a small four-helix bundle protein, to covalently tether all substrates and intermediates. ACP plays an active role, interacting with bot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d4214d2b1127c2557952ef63f7eadb4
https://doi.org/10.1016/b978-0-12-409547-2.14662-1
https://doi.org/10.1016/b978-0-12-409547-2.14662-1
Autor:
James J. La Clair, Woojoo E. Kim, Tony D. Davis, Jeffrey T. Mindrebo, Michael D. Burkart, Aochiu Chen, J. Andrew McCammon, Thomas G. Bartholow, Ashay Patel, J.P. Noel
Formation of carbon-carbon bonds via β-ketoacyl-acyl carrier protein (ACP) synthases (KS), are key reactions duringde novofatty acid and polyketide biosynthesis. KSs recognize multiple ACPs and choreograph ping-pong mechanisms often in an iterative
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e2efb4c4fe905ca16f303eee6b6c8f4
https://doi.org/10.1101/644518
https://doi.org/10.1101/644518