The plastid phosphorylase as a multiple-role player in plant metabolism

Copyright © 2019 Elsevier B.V. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 290(2020) vom: 03. Jan., Seite 110303
1. Verfasser: Hwang, Seon-Kap (VerfasserIn)
Weitere Verfasser: Koper, Kaan, Okita, Thomas W
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2020
Zugriff auf das übergeordnete Werk:Plant science : an international journal of experimental plant biology
Schlagworte:Journal Article Review L80 domain PEST motif Photosynthesis Protein phosphorylation Sink-source limitation Starch initiation Starch phosphorylase Starch synthesis mehr... Plant Proteins Starch 9005-25-8 Phosphorylases EC 2.4.1.-
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520 |a The physiological roles of the plastidial phosphorylase in starch metabolism of higher plants have been debated for decades. While estimated physiological substrate levels favor a degradative role, genetic evidence indicates that the plastidial phosphorylase (Pho1) plays an essential role in starch initiation and maturation of the starch granule in developing rice grains. The plastidial enzyme contains a unique peptide domain, up to 82 residues in length depending on the plant species, not found in its cytosolic counterpart or glycogen phosphorylases. The role of this extra peptide domain is perplexing, as its complete removal does not significantly affect the in vitro catalytic or enzymatic regulatory properties of rice Pho1. This peptide domain may have a regulatory function as it contains potential phosphorylation sites and, in some plant Pho1s, a PEST motif, a substrate for proteasome-mediated degradation. We discuss the potential roles of Pho1 and its L80 domain in starch biosynthesis and photosynthesis 
650 4 |a Journal Article 
650 4 |a Review 
650 4 |a L80 domain 
650 4 |a PEST motif 
650 4 |a Photosynthesis 
650 4 |a Protein phosphorylation 
650 4 |a Sink-source limitation 
650 4 |a Starch initiation 
650 4 |a Starch phosphorylase 
650 4 |a Starch synthesis 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Starch  |2 NLM 
650 7 |a 9005-25-8  |2 NLM 
650 7 |a Phosphorylases  |2 NLM 
650 7 |a EC 2.4.1.-  |2 NLM 
700 1 |a Koper, Kaan  |e verfasserin  |4 aut 
700 1 |a Okita, Thomas W  |e verfasserin  |4 aut 
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773 1 8 |g volume:290  |g year:2020  |g day:03  |g month:01  |g pages:110303 
856 4 0 |u http://dx.doi.org/10.1016/j.plantsci.2019.110303  |3 Volltext 
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