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231224s2016 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2016.10.029
|2 doi
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|a pubmed25n0886.xml
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|a (DE-627)NLM266118488
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|a (NLM)27835851
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|a (PII)S0981-9428(16)30419-3
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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 Yin, Sen
|e verfasserin
|4 aut
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|a Functional analyses of OcRhS1 and OcUER1 involved in UDP-L-rhamnose biosynthesis in Ornithogalum caudatum
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|c 2016
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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
|b cr
|2 rdacarrier
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|a Date Completed 10.04.2017
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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 © 2016 Elsevier Masson SAS. All rights reserved.
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|a UDP-L-rhamnose (UDP-Rha) is an important sugar donor for the synthesis of rhamnose-containing compounds in plants. However, only a few enzymes and their encoding genes involved in UDP-Rha biosynthesis are available in plants. Here, two genes encoding rhamnose synthase (RhS) and bi-functional UDP-4-keto-6-deoxy-D-glucose (UDP-4K6DG) 3, 5-epimerase/UDP-4-keto-L-rhamnose (UDP-4KR) 4-keto-reductase (UER) were isolated from Ornithogalum caudatum based on the RNA-Seq data. The OcRhS1 gene has an ORF (open reading frame) of 2019 bp encoding a tri-functional RhS enzyme. In vitro enzymatic assays revealed OcRhS1 can really convert UDP-D-glucose (UDP-Glc) into UDP-Rha via three consecutive reactions. Biochemical evidences indicated that the recombinant OcRhS1 was active in the pH range of 5-11 and over the temperature range of 0-60 °C. The Km value of OcRhS1 for UDP-Glc was determined to be 1.52 × 10-4 M. OcRhS1 is a multi-domain protein with two sets of cofactor-binding motifs. The cofactors dependent properties of OcRhS1 were thus characterized in this research. Moreover, the N-terminal portion of OcRhS1 (OcRhS1-N) was observed to metabolize UDP-Glc to form intermediate UDP-4K6DG. OcUER1 contains an ORF of 906 bp encoding a polypeptide of 301 aa. OcUER1 shared high similarity with the carboxy-terminal domain of OcRhS1 (OcRhS1-C), suggesting its intrinsic ability of converting UDP-4K6DG into UDP-Rha. It was thus reasonably inferred that UDP-Glc could be bio-transformed into UDP-Rha under the collaborating action of OcRhS1-N and OcUER1. The subsequently biochemical assay verified this notion. Importantly, expression profiles of OcRhS1 and OcUER1 revealed their possible involvement in the biosynthesis of rhamnose-containing polysaccharides in O. caudatum
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|a Journal Article
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|a 5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase
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|a Anti-cancer polysaccharides
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|a O. caudatum
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|a Rhamnose synthase
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|a UDP-4-keto-6-deoxy-D-glucose 3
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|a UDP-L-rhamnose
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Recombinant Proteins
|2 NLM
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|a Uridine Diphosphate Sugars
|2 NLM
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|a Carbohydrate Dehydrogenases
|2 NLM
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| 650 |
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|a EC 1.1.-
|2 NLM
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|a Carbohydrate Epimerases
|2 NLM
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| 650 |
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|a EC 5.1.3.-
|2 NLM
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| 650 |
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|a Rhamnose
|2 NLM
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| 650 |
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|a QN34XC755A
|2 NLM
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| 700 |
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|a Liu, Ming
|e verfasserin
|4 aut
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| 700 |
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|a Kong, Jian-Qiang
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 109(2016) vom: 01. Dez., Seite 536-548
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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| 773 |
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|g volume:109
|g year:2016
|g day:01
|g month:12
|g pages:536-548
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|u http://dx.doi.org/10.1016/j.plaphy.2016.10.029
|3 Volltext
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