Evidence map›Paper›PMID 27609111›Full record

ArticleBMC plant biology2016

Calcium/calmodulin alleviates substrate inhibition in a strawberry UDP-glucosyltransferase involved in fruit anthocyanin biosynthesis.

Hui Peng, Tianbao Yang, Bruce D Whitaker, Lingfei Shangguan, Jinggui Fang

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Cell Wall Integrity Signaling in Fruit Ripening.International journal of molecular sciences · 2023
    Review
  5. Review
  6. Effect of CaClFrontiers in plant science · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Hui PengAgricultural Research Service of U.S. Department of Agriculture, From the Food Quality Laboratory, Beltsville Agricultural Research Center, Beltsville, MD, 20705, USA.
Tianbao YangAgricultural Research Service of U.S. Department of Agriculture, From the Food Quality Laboratory, Beltsville Agricultural Research Center, Beltsville, MD, 20705, USA. tianbao.yang@ars.usda.gov.
Bruce D WhitakerAgricultural Research Service of U.S. Department of Agriculture, From the Food Quality Laboratory, Beltsville Agricultural Research Center, Beltsville, MD, 20705, USA.
Lingfei ShangguanAgricultural Research Service of U.S. Department of Agriculture, From the Food Quality Laboratory, Beltsville Agricultural Research Center, Beltsville, MD, 20705, USA.
Jinggui FangCollege of Horticulture, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China.
Beltsville Agricultural Research Center · USAgricultural Research Service · USNanjing Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundUDP-glucosyltransferase (UGT) is a key enzyme for anthocyanin biosynthesis, which by catalyzing glycosylation of anthocyanidins increases their solubility and accumulation in plants. Previously we showed that pre-harvest spray of CaCl2 enhanced anthocyanin accumulation in strawberry fruit by stimulating the expression of anthocyanin structural genes including a fruit specific FvUGT1.

resultsTo further understand the regulation of anthocyanin biosynthesis, we conducted kinetic analysis of recombinant FvUGT1 on glycosylation of pelargonidin, the major anthocyanidin in strawberry fruit. At the fixed pelargonidin concentration, FvUGT1 catalyzed the sugar transfer from UDP-glucose basically following Michaelis-Menten kinetics. By contrast, at the fixed UDP-glucose concentration, pelargonidin over 150 μM exhibited marked partial substrate inhibition in an uncompetitive mode. These results suggest that the sugar acceptor at high concentration inhibits FvUGT1 activity by binding to another site in addition to the catalytic site. Furthermore, calcium/calmodulin specifically bound FvUGT1 at a site partially overlapping with the interdomain linker, and significantly relieved the substrate inhibition. In the presence of 0.1 and 0.5 μM calmodulin, V max was increased by 71.4 and 327 %, respectively.

conclusionsFvUGT1 activity is inhibited by anthocyanidin, the sugar acceptor substrate, and calcium/calmodulin binding to FvUGT1 enhances anthocyanin accumulation via alleviation of this substrate inhibition.

Indexed as

Amino Acid SequenceAnthocyaninsCalciumCalmodulinFragariaFruitGlucosyltransferasesGlycosylationKineticsPlant ProteinsSequence AlignmentAnthocyaninsCalciumCalmodulinGlucosyltransferasesPlant ProteinsCalcium signalingEnzyme kineticsFragaria vescaPelargonidinUGT

Identifiers

PMID27609111
PMCPMC5017016
OpenAlexW2513270718

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.