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231225s2017 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2017.07.019
|2 doi
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|a pubmed24n0915.xml
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|a (DE-627)NLM274613247
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|a (NLM)28787650
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|a (PII)S0176-1617(17)30201-8
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Jiang, Junpeng
|e verfasserin
|4 aut
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|a Characterization of starch phosphorylase from the marine green microalga (Chlorophyta) Tetraselmis subcordiformis reveals its potential role in starch biosynthesis
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|c 2017
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 14.05.2018
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2017 Elsevier GmbH. All rights reserved.
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|a In a marine green starch-producing microalga Tetraselmis subcordiformis, the role of starch phosphorylase (SP) in the starch biosynthesis was disclosed by characterizing the enzyme properties and activity variations during the starch accumulation process. TsSP4, a SP isoform accounting for the major SP activity in T. subcordiformis, was unique to be active in a monomer form with a molecular weight of approximately 110kDa. It resembled one of the chloroplast-located SPs (PhoA) in Chlamydomonas reinhardtii with a similarity of 63.3% in sequence, though it possessed the typical L78/80 domain found in the plastidial SPs (Pho1) of higher plants that was absent in PhoA. TsSP4 exhibited moderate sensitivity to ADP-Glc inhibition and had a high activity for longer-chain linear maltooligosacchride (MOS) and amylopectin against highly branched glycogen as the substrates. TsSP4 had 2-fold higher affinity for Glc-1-P in the synthetic direction than for Pi in the phosphorolytic direction, and the catalytic constant kcat for Glc-1-P was 2-fold of that for Pi. Collectively, TsSP4 preferred synthetic rather than phosphorolytic direction. TsSP4 could elongate MOSs even initially with Pi alone in the absence of Glc-1-P, which further supported its synthetic role in the starch biosynthesis. TsSP4 displayed increased activities in the developing and mature stage of starch biosynthesis under nitrogen-starvation conditions, indicating its possible contribution to the amylopectin amplification
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|a Journal Article
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|a Amylopectin
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|a Kinetics
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|a Maltooligosacchride
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|a Nitrogen starvation
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|a Reaction direction
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|a TsSP4
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|a Algal Proteins
|2 NLM
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|a Isoenzymes
|2 NLM
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|a Starch
|2 NLM
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|a 9005-25-8
|2 NLM
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|a Starch Phosphorylase
|2 NLM
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|a EC 2.4.1.-
|2 NLM
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|a Nitrogen
|2 NLM
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|a N762921K75
|2 NLM
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| 700 |
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|a Yao, Changhong
|e verfasserin
|4 aut
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|a Cao, Xupeng
|e verfasserin
|4 aut
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| 700 |
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|a Liu, Yinghui
|e verfasserin
|4 aut
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| 700 |
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|a Xue, Song
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 218(2017) vom: 01. Nov., Seite 84-93
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
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|g volume:218
|g year:2017
|g day:01
|g month:11
|g pages:84-93
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|u http://dx.doi.org/10.1016/j.jplph.2017.07.019
|3 Volltext
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|d 218
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|b 01
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