Evidence map›Paper›PMID 36762861›Full record

ArticleActa crystallographica. Section D, Structural biology2023

Structural insight into the hydrolase and synthase activities of an alkaline α-galactosidase from Arabidopsis from complexes with substrate/product.

Phimonphan Chuankhayan, Ruey Hua Lee, Hong Hsiang Guan, Chein Chih Lin, Nai Chi Chen, Yen Chieh Huang, Masato Yoshimura, Atsushi Nakagawa, Chun Jung Chen

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

3 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

9 authors at 4 institutions in 2 countries.

Phimonphan ChuankhayanLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Cente, Hsinchu 30076, Taiwan.
Ruey Hua LeeInstitute of Tropical Plant Sciences and Microbiology, National Cheng Kung University, Tainan City 701, Taiwan.ORCID 0000-0002-8483-1092
Hong Hsiang GuanLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Cente, Hsinchu 30076, Taiwan.ORCID 0000-0001-5061-165X
Chein Chih LinLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Cente, Hsinchu 30076, Taiwan.
Nai Chi ChenLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Cente, Hsinchu 30076, Taiwan.ORCID 0000-0003-1287-1236
Yen Chieh HuangLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Cente, Hsinchu 30076, Taiwan.
Masato YoshimuraLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Cente, Hsinchu 30076, Taiwan.ORCID 0000-0002-7466-2192
Atsushi NakagawaInstitute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-1700-7861
Chun Jung ChenLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Cente, Hsinchu 30076, Taiwan.ORCID 0000-0002-5157-4288
National Synchrotron Radiation Research Center · TWNational Cheng Kung University · TWNational Yang Ming Chiao Tung University · TWProtein Research Foundation · JP

Funding

Ministry of Science and Technology (Taiwan) 105-2311-B-213-001-MY3Ministry of Science and Technology (Taiwan) 107-2923-B-213-001-MY3Ministry of Science and Technology (Taiwan) 108-2311-B-213-001-MY3Ministry of Science and Technology (Taiwan) 111-2311-B-213-001
6 · The paper itself

Abstract

The alkaline α-galactosidase AtAkαGal3 from Arabidopsis thaliana catalyzes the hydrolysis of α-D-galactose from galacto-oligosaccharides under alkaline conditions. A phylogenetic analysis based on sequence alignment classifies AtAkαGal3 as more closely related to the raffinose family of oligosaccharide (RFO) synthases than to the acidic α-galactosidases. Here, thin-layer chromatography is used to demonstrate that AtAkαGal3 exhibits a dual function and is capable of synthesizing stachyose using raffinose, instead of galactinol, as the galactose donor. Crystal structures of complexes of AtAkαGal3 and its D383A mutant with various substrates and products, including galactose, galactinol, raffinose, stachyose and sucrose, are reported as the first representative structures of an alkaline α-galactosidase. The structure of AtAkαGal3 comprises three domains: an N-terminal domain with 13 antiparallel β-strands, a catalytic domain with an (α/β)

Indexed as

alpha-GalactosidaseArabidopsisGalactoseHydrolasesPhylogenyRaffinosealpha-GalactosidaseGalactoseHydrolasesRaffinosealkaline α-galactosidasesArabidopsis thalianaraffinoseRFO synthasestransferase mechanism

Identifiers

PMID36762861
PMCPMC9912918
OpenAlexW4317583377

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.