Page last updated: 2024-09-26

valiolamine

Description

valiolamine: isolated from Streptomyces hygroscopicus; RN from CA Index; RN not in Chemline 2/85 [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID174312
CHEMBL ID222396
CHEMBL ID9216
MeSH IDM0127419

Synonyms (30)

Synonym
83465-22-9
AC-1555
valiolamine hydrate
d-epi-inositol, 4-amino-3,4-dideoxy-2-c-(hydroxymethyl)-, hydrate
4-amino-3,4-dideoxy-2-c-(hydroxymethyl)-d-epi-inositol hydrate
valiolamine
CHEMBL222396 ,
bdbm50241137
chembl9216
valinolamine
5-amino-1-hydroxymethyl-cyclohexane-1,2,3,4-tetraol
bdbm50024129
A840578
(1s,2s,3r,4s,5s)-5-amino-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol;valiolamine
(1s,2s,3r,4s,5s)-5-amino-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol
AKOS006287538
(1s,2s,3r,4s,5s)-5-amino-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetraol
4-amino-3,4-dideoxy-2-c-(hydroxymethyl)-d-epi-inositol
VDLOJRUTNRJDJO-ZYNSJIGGSA-N
mfcd07773061
AS-14081
C76668
5-amino-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol
DTXSID601003447
4-amino-3.4-dideoxy-2-c-(hydroxymethyl)-d-epi-inositol
w9s ,
QHW83U8Q5B
eb-0155
d-epi-inositol, 4-amino-3,4-dideoxy-2-c-(hydroxymethyl)-
eb0155

Research Excerpts

Overview

ExcerptReference
"Valiolamine is a particularly effective inhibitor of oligosaccharide glucosidases I and II and of lysosomal alpha-glucosidase."( Kamata, K; Kameda, Y; Matsui, K; Takeuchi, M; Yoshida, M, 1990)

Effects

ExcerptReference
"Valiolamine has more potent alpha-glucosidase inhibitory activity against porcine intestinal sucrase, maltase and isomaltase than valienamine, validamine and hydroxyvalidamine which were reported as building blocks of validamycins and microbial oligosaccharide alpha-glucosidase inhibitors."( Asano, N; Fukase, H; Horii, S; Kameda, Y; Matsui, K; Takeuchi, M; Yamaguchi, T; Yoshikawa, M, 1984)
"Valiolamine has more potent carbohydrase inhibitory activity than validamine or valienamine, and the apparent Ki values of valiolamine for sucrase, maltase, glucoamylase, isomaltase and trehalase activities were 3.2 x 10(-7), 2.9 x 10(-6), 1.2 x 10(-6), 9.1 x 10(-7) and 4.9 x 10(-5) M, respectively, which are 10(-5) to 10(-3) times smaller than the apparent Km values."( Asano, N; Kameda, Y; Matsui, K; Takai, N; Takeuchi, M, 1990)

Protein Targets (6)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Maltase-glucoamylase, intestinalHomo sapiens (human)IC50 (µMol)2.20000.04003.46529.0000AID104666
Lysosomal alpha-glucosidaseHomo sapiens (human)IC50 (µMol)57.00000.06002.28897.8000AID342799
Sucrase-isomaltase, intestinalHomo sapiens (human)IC50 (µMol)0.04900.04902.72947.8000AID208984
Sucrase-isomaltase, intestinalRattus norvegicus (Norway rat)IC50 (µMol)1.39500.04001.848310.0000AID342795; AID342797
Glycogen debranching enzymeOryctolagus cuniculus (rabbit)IC50 (µMol)31.00000.11000.69752.1000AID342805
Lysosomal alpha-glucosidaseRattus norvegicus (Norway rat)IC50 (µMol)18.00000.08002.50619.8500AID342793
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (22)

Processvia Protein(s)Taxonomy
maltose catabolic processMaltase-glucoamylase, intestinalHomo sapiens (human)
starch catabolic processMaltase-glucoamylase, intestinalHomo sapiens (human)
dextrin catabolic processMaltase-glucoamylase, intestinalHomo sapiens (human)
maltose metabolic processLysosomal alpha-glucosidaseHomo sapiens (human)
regulation of the force of heart contractionLysosomal alpha-glucosidaseHomo sapiens (human)
diaphragm contractionLysosomal alpha-glucosidaseHomo sapiens (human)
heart morphogenesisLysosomal alpha-glucosidaseHomo sapiens (human)
glycogen catabolic processLysosomal alpha-glucosidaseHomo sapiens (human)
sucrose metabolic processLysosomal alpha-glucosidaseHomo sapiens (human)
glucose metabolic processLysosomal alpha-glucosidaseHomo sapiens (human)
lysosome organizationLysosomal alpha-glucosidaseHomo sapiens (human)
locomotory behaviorLysosomal alpha-glucosidaseHomo sapiens (human)
tissue developmentLysosomal alpha-glucosidaseHomo sapiens (human)
aorta developmentLysosomal alpha-glucosidaseHomo sapiens (human)
vacuolar sequesteringLysosomal alpha-glucosidaseHomo sapiens (human)
muscle cell cellular homeostasisLysosomal alpha-glucosidaseHomo sapiens (human)
neuromuscular process controlling postureLysosomal alpha-glucosidaseHomo sapiens (human)
neuromuscular process controlling balanceLysosomal alpha-glucosidaseHomo sapiens (human)
cardiac muscle contractionLysosomal alpha-glucosidaseHomo sapiens (human)
glycophagyLysosomal alpha-glucosidaseHomo sapiens (human)
sucrose catabolic processSucrase-isomaltase, intestinalHomo sapiens (human)
polysaccharide digestionSucrase-isomaltase, intestinalHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (10)

Processvia Protein(s)Taxonomy
catalytic activityMaltase-glucoamylase, intestinalHomo sapiens (human)
glucan 1,4-alpha-glucosidase activityMaltase-glucoamylase, intestinalHomo sapiens (human)
alpha-1,4-glucosidase activityMaltase-glucoamylase, intestinalHomo sapiens (human)
protein bindingMaltase-glucoamylase, intestinalHomo sapiens (human)
amylase activityMaltase-glucoamylase, intestinalHomo sapiens (human)
carbohydrate bindingMaltase-glucoamylase, intestinalHomo sapiens (human)
maltose alpha-glucosidase activityMaltase-glucoamylase, intestinalHomo sapiens (human)
alpha-1,4-glucosidase activityLysosomal alpha-glucosidaseHomo sapiens (human)
carbohydrate bindingLysosomal alpha-glucosidaseHomo sapiens (human)
maltose alpha-glucosidase activityLysosomal alpha-glucosidaseHomo sapiens (human)
alpha-glucosidase activityLysosomal alpha-glucosidaseHomo sapiens (human)
oligo-1,6-glucosidase activitySucrase-isomaltase, intestinalHomo sapiens (human)
sucrose alpha-glucosidase activitySucrase-isomaltase, intestinalHomo sapiens (human)
protein bindingSucrase-isomaltase, intestinalHomo sapiens (human)
carbohydrate bindingSucrase-isomaltase, intestinalHomo sapiens (human)
alpha-1,4-glucosidase activitySucrase-isomaltase, intestinalHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (14)

Processvia Protein(s)Taxonomy
plasma membraneMaltase-glucoamylase, intestinalHomo sapiens (human)
apical plasma membraneMaltase-glucoamylase, intestinalHomo sapiens (human)
extracellular exosomeMaltase-glucoamylase, intestinalHomo sapiens (human)
tertiary granule membraneMaltase-glucoamylase, intestinalHomo sapiens (human)
ficolin-1-rich granule membraneMaltase-glucoamylase, intestinalHomo sapiens (human)
lysosomeLysosomal alpha-glucosidaseHomo sapiens (human)
lysosomal membraneLysosomal alpha-glucosidaseHomo sapiens (human)
plasma membraneLysosomal alpha-glucosidaseHomo sapiens (human)
membraneLysosomal alpha-glucosidaseHomo sapiens (human)
azurophil granule membraneLysosomal alpha-glucosidaseHomo sapiens (human)
lysosomal lumenLysosomal alpha-glucosidaseHomo sapiens (human)
intracellular membrane-bounded organelleLysosomal alpha-glucosidaseHomo sapiens (human)
extracellular exosomeLysosomal alpha-glucosidaseHomo sapiens (human)
tertiary granule membraneLysosomal alpha-glucosidaseHomo sapiens (human)
ficolin-1-rich granule membraneLysosomal alpha-glucosidaseHomo sapiens (human)
autolysosome lumenLysosomal alpha-glucosidaseHomo sapiens (human)
Golgi apparatusSucrase-isomaltase, intestinalHomo sapiens (human)
plasma membraneSucrase-isomaltase, intestinalHomo sapiens (human)
brush borderSucrase-isomaltase, intestinalHomo sapiens (human)
apical plasma membraneSucrase-isomaltase, intestinalHomo sapiens (human)
extracellular exosomeSucrase-isomaltase, intestinalHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (16)

Assay IDTitleYearJournalArticle
AID208984Alpha-D-glucosidase inhibitory activity and enzyme inhibition in vitro against porcine sucrase1986Journal of medicinal chemistry, Jun, Volume: 29, Issue:6
Synthesis and alpha-D-glucosidase inhibitory activity of N-substituted valiolamine derivatives as potential oral antidiabetic agents.
AID104666Inhibitory activity against porcine maltase1986Journal of medicinal chemistry, Jun, Volume: 29, Issue:6
Synthesis and alpha-D-glucosidase inhibitory activity of N-substituted valiolamine derivatives as potential oral antidiabetic agents.
AID342793Inhibition of rat intestinal brush border membrane maltase2008Bioorganic & medicinal chemistry, Aug-01, Volume: 16, Issue:15
In vitro inhibition of glycogen-degrading enzymes and glycosidases by six-membered sugar mimics and their evaluation in cell cultures.
AID1895992Inhibition of full length human recombinant Endoplasmic reticulum alpha-glucosidase 1 expressed in Escherichia coli using trisaccharide as substrate incubated for 60 mins2021Journal of medicinal chemistry, 12-23, Volume: 64, Issue:24
N-Substituted Valiolamine Derivatives as Potent Inhibitors of Endoplasmic Reticulum α-Glucosidases I and II with Antiviral Activity.
AID342795Inhibition of rat intestinal brush border membrane isomaltase2008Bioorganic & medicinal chemistry, Aug-01, Volume: 16, Issue:15
In vitro inhibition of glycogen-degrading enzymes and glycosidases by six-membered sugar mimics and their evaluation in cell cultures.
AID342804Inhibition of rabbit glycogen phosphorylase B at 400 uM2008Bioorganic & medicinal chemistry, Aug-01, Volume: 16, Issue:15
In vitro inhibition of glycogen-degrading enzymes and glycosidases by six-membered sugar mimics and their evaluation in cell cultures.
AID1895996Antiviral activity against SARS-CoV-2 England/2/2022 assessed as reduction in viral infection2021Journal of medicinal chemistry, 12-23, Volume: 64, Issue:24
N-Substituted Valiolamine Derivatives as Potent Inhibitors of Endoplasmic Reticulum α-Glucosidases I and II with Antiviral Activity.
AID342805Inhibition of rabbit muscle amylo-1,6-glucosidase2008Bioorganic & medicinal chemistry, Aug-01, Volume: 16, Issue:15
In vitro inhibition of glycogen-degrading enzymes and glycosidases by six-membered sugar mimics and their evaluation in cell cultures.
AID342797Inhibition of rat intestinal brush border membrane sucrase2008Bioorganic & medicinal chemistry, Aug-01, Volume: 16, Issue:15
In vitro inhibition of glycogen-degrading enzymes and glycosidases by six-membered sugar mimics and their evaluation in cell cultures.
AID342802Inhibition of human lysosomal beta-glucosidase at 1000 uM2008Bioorganic & medicinal chemistry, Aug-01, Volume: 16, Issue:15
In vitro inhibition of glycogen-degrading enzymes and glycosidases by six-membered sugar mimics and their evaluation in cell cultures.
AID1895994Cytotoxicity against African green monkey Vero cells assessed as reduction in cell viability incubated for 3 to 5 days by Cell titer-glo luminescent assay2021Journal of medicinal chemistry, 12-23, Volume: 64, Issue:24
N-Substituted Valiolamine Derivatives as Potent Inhibitors of Endoplasmic Reticulum α-Glucosidases I and II with Antiviral Activity.
AID342809Inhibition of pig intestinal maltase2008Bioorganic & medicinal chemistry, Aug-01, Volume: 16, Issue:15
In vitro inhibition of glycogen-degrading enzymes and glycosidases by six-membered sugar mimics and their evaluation in cell cultures.
AID342810Inhibition of pig intestinal sucrase2008Bioorganic & medicinal chemistry, Aug-01, Volume: 16, Issue:15
In vitro inhibition of glycogen-degrading enzymes and glycosidases by six-membered sugar mimics and their evaluation in cell cultures.
AID342799Inhibition of human lysosomal alpha-glucosidase2008Bioorganic & medicinal chemistry, Aug-01, Volume: 16, Issue:15
In vitro inhibition of glycogen-degrading enzymes and glycosidases by six-membered sugar mimics and their evaluation in cell cultures.
AID1895993Inhibition of full length N-terminal his6-tagged mouse recombinant Endoplasmic reticulum alpha-glucosidase 2 expressed in DH10 Escherichia coli using Fluorogenic 1,4-methyl-lumbelliferon as substrate preincubated for 60 mins followed by substrate addition2021Journal of medicinal chemistry, 12-23, Volume: 64, Issue:24
N-Substituted Valiolamine Derivatives as Potent Inhibitors of Endoplasmic Reticulum α-Glucosidases I and II with Antiviral Activity.
AID1895995Antiviral activity against DENV New Guinea C strain infected in African green monkey Vero cells assessed as reduction in viral infection measured after 5 days by plaque assay2021Journal of medicinal chemistry, 12-23, Volume: 64, Issue:24
N-Substituted Valiolamine Derivatives as Potent Inhibitors of Endoplasmic Reticulum α-Glucosidases I and II with Antiviral Activity.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (15)

TimeframeStudies, This Drug (%)All Drugs %
pre-19903 (20.00)18.7374
1990's2 (13.33)18.2507
2000's5 (33.33)29.6817
2010's3 (20.00)24.3611
2020's2 (13.33)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%
Reviews3 (18.75%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other13 (81.25%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]