Page last updated: 2024-12-08

amylodextrins

Description Research Excerpts Clinical Trials Roles Classes Pathways Study Profile Bioassays Related Drugs Related Conditions Protein Interactions Research Growth

Description

amylodextrin : A linear dextrin or short chained amylose (DP 20-30) that can be produced by enzymatic hydrolysis of the alpha-1,6 glycosidic bonds or debranching amylopectin. [Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Cross-References

ID SourceID
PubMed CID439341
CHEBI ID18167
SCHEMBL ID346806
MeSH IDM0055250

Synonyms (48)

Synonym
amylodextrins
einecs 232-686-4
glca1-4glca
glcalpha1-4glca
alpha-d-glcp-(1->4)-alpha-d-glcp
CHEBI:18167
4-o-alpha-d-glucopyranosyl-alpha-d-glucopyranose
glcalpha1-4glcalpha
alpha-d-glucopyranosyl-(1->4)-alpha-d-glucopyranose
alpha-maltose ,
4482-75-1
C00897
9050-36-6
1URG
1N3W
1ANF
1R6Z
bdbm23407
(2r,3s,4s,5r,6r)-2-(hydroxymethyl)-6-{[(2r,3s,4r,5r,6s)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy}oxane-3,4,5-triol
2D2V
(2r,3s,4s,5r,6r)-2-(hydroxymethyl)-6-[(2r,3s,4r,5r,6s)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxane-3,4,5-triol
amylodextrin
9005-84-9
unii-15sug9ad26
maltose alpha-anomer
maltose, alpha-
15sug9ad26 ,
alpha-d-glucopyranose, 4-o-alpha-d-glucopyranosyl-
AKOS015896501
SCHEMBL346806
maltose, .alpha.-
.alpha.-d-glucopyranose, 4-o-.alpha.-d-glucopyranosyl-
.alpha.-maltose
maltose .alpha.-anomer
mfcd00132834
mfcd00082026
DTXSID20196313
starkelosung
HY-N2024
CS-W019624
GUBGYTABKSRVRQ-ASMJPISFSA-N
iodine indicator
Q26914016
thyodene
CS-0226092
(2s,3r,4r,5s,6r)-6-(hydroxymethyl)-5-(((2r,3r,4s,5s,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2h-pyran-2-yl)oxy)tetrahydro-2h-pyran-2,3,4-triol
HY-N2024B
maltose solution, 20% in h2o

Research Excerpts

[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Drug Classes (1)

ClassDescription
maltoseA glycosylglucose consisting of two D-glucopyranose units connected by an alpha-(1->4)-linkage.
[compound class information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Pathways (4)

PathwayProteinsCompounds
Renz2020 - GEM of Human alveolar macrophage with SARS-CoV-20490
glycogen biosynthesis III (from u03B1-maltose 1-phosphate)818
trehalose biosynthesis IV38
starch degradation010

Protein Targets (8)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Chain A, Maltodextrin-binding ProteinEscherichia coli K-12Ki3.50000.16001.83003.5000AID977610
Chain A, X-ray structure of the sucrose-phosphatase (SPP) from Synechocystis sp.PCC6803 in complex with trehaloseSynechocystis sp. PCC 6803Ki100,000.000026,000.000063,000.0000100,000.0000AID977610
Chain A, X-ray structure of the sucrose-phosphatase (SPP) from Synechocystis sp.PCC6803 in complex with cellobioseSynechocystis sp. PCC 6803Ki100,000.000026,000.000063,000.0000100,000.0000AID977610
Chain A, X-ray structure of the sucrose-phosphatase (SPP) from Synechocystis sp.PCC6803 in complex with maltoseSynechocystis sp. PCC 6803Ki100,000.000026,000.000063,000.0000100,000.0000AID977610
Chain A, Maltodextrin-binding ProteinEscherichia coli K-12Ki3.50000.16001.83003.5000AID977610
Chain A, Maltodextrin Binding ProteinEscherichia coli K-12Ki3.50000.16001.83003.5000AID977610
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Activation Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Chain A, Maltose-binding periplasmic proteinEscherichia coliKd0.11000.11000.11000.1100AID977611
Chain Z, Chimera of Maltose-binding periplasmic protein and Argonaute 2Escherichia coliKd10.000010.000010.000010.0000AID977611
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Bioassays (8)

Assay IDTitleYearJournalArticle
AID1811Experimentally measured binding affinity data derived from PDB2003The Journal of biological chemistry, Sep-05, Volume: 278, Issue:36
Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants.
AID977611Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB2003The Journal of biological chemistry, Sep-05, Volume: 278, Issue:36
Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants.
AID977611Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB2003Nature structural biology, Dec, Volume: 10, Issue:12
The crystal structure of the Argonaute2 PAZ domain reveals an RNA binding motif in RNAi effector complexes.
AID1811Experimentally measured binding affinity data derived from PDB2003Nature structural biology, Dec, Volume: 10, Issue:12
The crystal structure of the Argonaute2 PAZ domain reveals an RNA binding motif in RNAi effector complexes.
AID977610Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB2007Proteins, Aug-15, Volume: 68, Issue:3
Crystal structure of a cyanobacterial sucrose-phosphatase in complex with glucose-containing disaccharides.
AID1811Experimentally measured binding affinity data derived from PDB2007Proteins, Aug-15, Volume: 68, Issue:3
Crystal structure of a cyanobacterial sucrose-phosphatase in complex with glucose-containing disaccharides.
AID1811Experimentally measured binding affinity data derived from PDB1997Structure (London, England : 1993), Aug-15, Volume: 5, Issue:8
Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor.
AID977610Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB1997Structure (London, England : 1993), Aug-15, Volume: 5, Issue:8
Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (25)

TimeframeStudies, This Drug (%)All Drugs %
pre-19906 (24.00)18.7374
1990's8 (32.00)18.2507
2000's6 (24.00)29.6817
2010's5 (20.00)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other25 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]