Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Jonathan D. Monroe"'
Autor:
Jonathan D. Monroe
Publikováno v:
Plant Direct, Vol 4, Iss 2, Pp n/a-n/a (2020)
Abstract Starch degradation in chloroplasts requires β‐amylase (BAM) activity, but in Arabidopsis, there are nine BAM proteins, five of which are thought to be catalytic. Although single‐gene knockouts revealed the necessity of BAM3 for starch d
Externí odkaz:
https://doaj.org/article/256074d54c5b495992c117ebc0f05ac8
Autor:
Jonathan D. Monroe, Lauren E. Pope, Jillian S. Breault, Christopher E. Berndsen, Amanda R. Storm
Publikováno v:
Frontiers in Plant Science, Vol 9 (2018)
The β-amylase family in Arabidopsis thaliana has nine members, four of which are both plastid-localized and, based on active-site sequence conservation, potentially capable of hydrolyzing starch to maltose. We recently reported that one of these enz
Externí odkaz:
https://doaj.org/article/f2fd0472d5c24effa786eaedf9b26e9d
Autor:
Kenan E Ozcan, Jonathan D Monroe
Publikováno v:
Plant Physiology.
An unusual β-amylase7 (BAM7) gene in some angiosperms, including grasses such as maize (Zea mays), appears to encode 2 functionally distinct proteins: a nuclear-localized transcription factor (BAM7) and a plastid-localized starch hydrolase (BAM2). I
Publikováno v:
Acta Crystallogr D Struct Biol
Starch accumulates in the plastids of green plant tissues during the day to provide carbon for metabolism at night. Starch hydrolysis is catalyzed by members of the β-amylase (BAM) family, which in Arabidopsis thaliana (At) includes nine structurall
Starch accumulates in the plastids of green plant tissue during the day to provide carbon for metabolism at night. Starch hydrolysis is catalyzed by members of the β-amylase (BAM) family, which in Arabidopsis thaliana (At), includes nine structurall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::24c18981c85e2898efa9c18d19a84bd0
https://doi.org/10.1101/2021.10.14.464379
https://doi.org/10.1101/2021.10.14.464379
Publikováno v:
The FASEB Journal. 35
Autor:
Claire M. Ravenburg, Nithesh Chandrasekharan, Ian R. Roy, Christopher E. Berndsen, Jonathan D. Monroe
Publikováno v:
Acta Crystallogr D Struct Biol
Starch is a key energy-storage molecule in plants that requires controlled synthesis and breakdown for effective plant growth. β-Amylases (BAMs) hydrolyze starch into maltose to help to meet the metabolic needs of the plant. In the model plantArabid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d81604c0ff4a3a0a30f3647bd9e629e5
https://europepmc.org/articles/PMC7137110/
https://europepmc.org/articles/PMC7137110/
Autor:
Tewaldemedhine B. Gebrejesus, Catherine E. Torres, Jonathan D. Monroe, Amanda R. Storm, Christopher E. Berndsen, Jillian S. Breault, Lauren E. Pope
Publikováno v:
Plant Physiology. 175:1525-1535
The Arabidopsis (Arabidopsis thaliana) genome contains nine β-amylase (BAM) genes, some of which play important roles in starch hydrolysis. However, little is known about BAM2, a plastid-localized enzyme reported to have extremely low catalytic acti
Autor:
Melanie R Abt, David Seung, Kuan-Jen Lu, Jonathan D. Monroe, Tina B. Schreier, Laure C David, Martina Zanella, Julien Boudet, Samuel C. Zeeman
Publikováno v:
The Plant Cell. 29:1657-1677
The molecular mechanism that initiates the synthesis of starch granules is poorly understood. Here, we discovered two plastidial proteins involved in granule initiation in Arabidopsis thaliana leaves. Both contain coiled coils and a family-48 carbohy
Autor:
Claire M. Ravenburg, Ian R. Roy, Nithesh Chandrasekharan, Jonathan D. Monroe, Christopher E. Berndsen
Starch is a key energy storage molecule in plants that requires controlled synthesis and breakdown for effective plant growth. β-amylases (BAMs) hydrolyze starch into maltose to help meet the metabolic needs of the plant. In the model plant,Arabidop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33fae3d3259db25521283c180c5e5a2d
https://doi.org/10.1101/751602
https://doi.org/10.1101/751602