Characterization of plastidial starch phosphorylase in Triticum aestivum L. endosperm

Starch phosphorylase (Pho) catalyses the reversible transfer of glucosyl units from glucose1-phosphate to the non-reducing end of an alpha-1,4-linked glucan chain. Two major isoforms of Pho exist in the plastid (Pho1) and cytosol (Pho2). In this paper it is proposed that Pho1 may play an important r...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Journal of plant physiology. - 1979. - 166(2009), 14 vom: 15. Sept., Seite 1465-78
1. Verfasser: Tickle, Paul (VerfasserIn)
Weitere Verfasser: Burrell, Michael M, Coates, Stephen A, Emes, Michael J, Tetlow, Ian J, Bowsher, Caroline G
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2009
Zugriff auf das übergeordnete Werk:Journal of plant physiology
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Starch Phosphorylase EC 2.4.1.-
LEADER 01000naa a22002652 4500
001 NLM189267534
003 DE-627
005 20231223183342.0
007 cr uuu---uuuuu
008 231223s2009 xx |||||o 00| ||eng c
024 7 |a 10.1016/j.jplph.2009.05.004  |2 doi 
028 5 2 |a pubmed24n0631.xml 
035 |a (DE-627)NLM189267534 
035 |a (NLM)19524321 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Tickle, Paul  |e verfasserin  |4 aut 
245 1 0 |a Characterization of plastidial starch phosphorylase in Triticum aestivum L. endosperm 
264 1 |c 2009 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 02.11.2009 
500 |a Date Revised 30.09.2020 
500 |a published: Print-Electronic 
500 |a GENBANK: EU595762 
500 |a Citation Status MEDLINE 
520 |a Starch phosphorylase (Pho) catalyses the reversible transfer of glucosyl units from glucose1-phosphate to the non-reducing end of an alpha-1,4-linked glucan chain. Two major isoforms of Pho exist in the plastid (Pho1) and cytosol (Pho2). In this paper it is proposed that Pho1 may play an important role in recycling glucosyl units from malto-oligosaccharides back into starch synthesis in the developing wheat endosperm. Pho activity was observed in highly purified amyloplast extracts prepared from developing wheat endosperms, representing the first direct evidence of plastidial Pho activity in this tissue. A full-length cDNA clone encoding a plastidial Pho isoform, designated TaPho1, was also isolated from a wheat endosperm cDNA library. The TaPho1 protein and Pho1 enzyme activity levels were shown to increase throughout the period of starch synthesis. These observations add to the growing body of evidence which indicates that this enzyme class has a role in starch synthesis in wheat endosperm and indeed all starch storing tissues 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Starch Phosphorylase  |2 NLM 
650 7 |a EC 2.4.1.-  |2 NLM 
700 1 |a Burrell, Michael M  |e verfasserin  |4 aut 
700 1 |a Coates, Stephen A  |e verfasserin  |4 aut 
700 1 |a Emes, Michael J  |e verfasserin  |4 aut 
700 1 |a Tetlow, Ian J  |e verfasserin  |4 aut 
700 1 |a Bowsher, Caroline G  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Journal of plant physiology  |d 1979  |g 166(2009), 14 vom: 15. Sept., Seite 1465-78  |w (DE-627)NLM098174622  |x 1618-1328  |7 nnns 
773 1 8 |g volume:166  |g year:2009  |g number:14  |g day:15  |g month:09  |g pages:1465-78 
856 4 0 |u http://dx.doi.org/10.1016/j.jplph.2009.05.004  |3 Volltext 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_350 
951 |a AR 
952 |d 166  |j 2009  |e 14  |b 15  |c 09  |h 1465-78