The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis

Autor: Dacheng Wang, Michael D. L. Suits, Jayne Kelso, Joel T. Weadge, Kissa Batul, Gabriel Moreno-Hagelsieb, Jacqueline Whiteside, Monica Papinski, Marc W. van der Kamp, Kyle Rice, Alena Pratasouskaya, Christopher Bartlett, Rebecca Sullivan, Geoff P. Horsman, Edward Schmidt

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Nature Communications
Rice, K, Batul, K, Whiteside, J, Kelso, J, Papinski, M, Schmidt, E, Pratasouskaya, A, Wang, D, Sullivan, R, Bartlett, C, Weadge, J, Van der Kamp, M, Moreno-Hagelsieb, G, Suits, M & Horsman, G 2019, ' The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis ', Nature Communications, vol. 10, no. 1, 3698 (2019) . https://doi.org/10.1038/s41467-019-11627-6

Phosphonates are rare and unusually bioactive natural products. However, most bacterial phosphonate biosynthetic capacity is dedicated to tailoring cell surfaces with molecules like 2-aminoethylphosphonate (AEP). Although phosphoenolpyruvate mutase (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca93fe827b6a3004afcd8afb92425ab2
http://link.springer.com/article/10.1038/s41467-019-11627-6

Structure of Oxalacetate Acetylhydrolase, a Virulence Factor of the Chestnut Blight Fungus

Autor: Donald L. Nuss, Chen Chen, Osnat Herzberg, Buvaneswari Narayanan, Qihong Sun

Publikováno v: Journal of Biological Chemistry. 285:26685-26696

Oxalacetate acetylhydrolase (OAH), a member of the phosphoenolpyruvate mutase/isocitrate lyase superfamily, catalyzes the hydrolysis of oxalacetate to oxalic acid and acetate. This study shows that knock-out of the oah gene in Cryphonectria parasitic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1960a9290b10db9a9d1f741bc28fe373
https://doi.org/10.1074/jbc.m110.117804

Crystal Structure of the Petal Death Protein from Carnation Flower

Autor: Zhibing Lu, Alexey Teplyakov, Osnat Herzberg, Sijiu Liu, Andrew Howard, Debra Dunaway-Mariano

Publikováno v: Biochemistry. 44:16377-16384

Expression of the PSR132 protein from Dianthus caryophyllus(carnation, clover pink) is induced in response to ethylene production associated with petal senescence, and thus the protein is named petal death protein (PDP). Recent work has established t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92d6f899ee9ec885592ba9cbed46c277
https://doi.org/10.1021/bi051779y

Crystal Structures of 2-Methylisocitrate Lyase in Complex with Product and with Isocitrate Inhibitor Provide Insight into Lyase Substrate Specificity, Catalysis and Evolution

Autor: Sijiu Liu, Eugene Melamud, Zhibing Lu, Debra Dunaway-Mariano, Osnat Herzberg, Yin Han

Publikováno v: Biochemistry. 44:2949-2962

Two crystal structures of the C123S mutant of 2-methylisocitrate lyase have been determined, one with the bound reaction products, Mg(2+)-pyruvate and succinate, and the second with a bound Mg(2+)-(2R,3S)-isocitrate inhibitor. Comparison with the str

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::582498514470d61daabd9ca25566b36c
https://doi.org/10.1021/bi0479712

A flower senescence-related mRNA from carnation encodes a novel protein related to enzymes involved in phosphonate biosynthesis

Autor: William R. Woodson, Amanda S. Brandt, Hong Wang

Publikováno v: Plant Molecular Biology. 22:719-724

We have isolated a cDNA clone (pSR132) representing a mRNA which accumulates in senescing carnation flower petals in response to ethylene. In vitro translation of RNA selected by hybridization with pSR132 indicated the mRNA encoded a polypeptide of a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3565db168757f6e6af8055ecbc8919c9
https://doi.org/10.1007/bf00047414