2.4.1.5: dextransucrase
This is an abbreviated version!
For detailed information about dextransucrase, go to the full flat file.
Word Map on EC 2.4.1.5
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2.4.1.5
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streptococcus
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mutans
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glucosylation
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glucans
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leuconostoc
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dental
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mesenteroides
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caries
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udp-glucose
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oligosaccharide
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cariogenic
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sobrinus
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glucoside
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water-insoluble
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difficile
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plaque
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maltose
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glycosyltransferases
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serotype
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saliva
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tooth
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sanguis
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gordonii
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fructosyltransferase
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udp-glc
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monoglucosylated
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dextranase
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tcda
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glucansucrase
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pellicle
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salivarius
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gtases
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galactosyltransferase
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saliva-coated
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calnexin
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viscosus
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lipid-linked
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industry
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food industry
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aureobasidium
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oralis
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pharmacology
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pseudomembranous
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medicine
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3-o-glucoside
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levansucrase
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biotechnology
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alpha-1,6
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weissella
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man9glcnac2
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transglucosylation
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synthesis
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glc3man9glcnac2
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nutrition
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isomaltose
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sordellii
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holotoxins
- 2.4.1.5
- streptococcus
- mutans
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glucosylation
- glucans
- leuconostoc
-
dental
- mesenteroides
- caries
- udp-glucose
- oligosaccharide
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cariogenic
- sobrinus
- glucoside
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water-insoluble
- difficile
- plaque
- maltose
- glycosyltransferases
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serotype
- saliva
- tooth
- sanguis
- gordonii
- fructosyltransferase
- udp-glc
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monoglucosylated
- dextranase
- tcda
- glucansucrase
- pellicle
- salivarius
- gtases
-
galactosyltransferase
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saliva-coated
- calnexin
- viscosus
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lipid-linked
- industry
- food industry
- aureobasidium
- oralis
- pharmacology
-
pseudomembranous
- medicine
- 3-o-glucoside
- levansucrase
- biotechnology
-
alpha-1,6
- weissella
- man9glcnac2
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transglucosylation
- synthesis
- glc3man9glcnac2
- nutrition
- isomaltose
- sordellii
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holotoxins
Reaction
Synonyms
B-512F dextransucrase, B-512FMC dextransucrase, Cab3, CEP, DexT, dextran-sucrase, DS, DSase, DSR, Dsr S protein, DSR-F, DSR-S, DSRB742, DSRBCB4, DSRC39-2, DsrE563, DsrP, DSRS, DSRWC, DsrX, FT045B dextransucrase, glucansucrase, glucosyltransferase, glucosyltransferase, sucrose-1,6-alpha-glucan, glycosyltransferase R, Gtf, Gtf-DSM, GTFR, More, SGE, sucrose 6-glucosyltransferase, sucrose:1, 6-alpha-D-glucan 6-alpha-glucosyltransferase, sucrose:1,6-alpha-D-glucan-6-alpha-D-glucosyltransferase, Wc392-rDSR, WcCab3-DSR
ECTree
2.4.1.5 dextransucraseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 2.4.1.5 - dextransucrase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
6-Deoxy-6-fluoro-alpha-D-glucopyranoside
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very weak, noncompetitive
barium chloride
64.29% inhibition of transferase activity at 10 mM; 64.86% inhibition of transferase activity at 10 mM; 70.27% inhibition of transferase activity at 10 mM
chitosan
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various sizes of chitosans (CTSN, CTSN-P, CTSN-B, and CTSN-S) prepared as low molecular weight chitosan show significant inhibitory effect on enzyme DSase activity, antimicrobial activity of CTSNs toward Streptococcus mutans, overview
dextran derivatives
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in which 5-50% of the D-glucose units are oxidized, acts as potent and specific inhibitor. 10%-oxidized derivatives of dextran fraction ranging in MW from 10000 Da to 2000000 Da
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fructan
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the fructan of Lactobacillus sanfranciscensis has either no effect or an inhibitory effect
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gallic acid
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80-90% inhibition at 4-5 mM, mixed-type inhibition in vitro
Glutaraldehyde
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does not support enzyme stability, but inhibits the enzyme activity
manganese chloride
54.05% inhibition of transferase activity at 100 mM; 59.46% inhibition of transferase activity at 100 mM; 64.29% inhibition of transferase activity at 100 mM
methyl 6-deoxy-6-fluoro-alpha-D-glucopyranoside
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very weak, noncompetitive
NaCl
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only the hydrolytic activity of the dextransuccrase is influenced by sodium ions, whereas there is no effect on glucosyltransferase activity. 0.5 mM, 65% inhibition of hydrolytic activity, 20 mM, 90% inhibition of hydrolytic activity. The enzyme shows biphasic effects in response to Na+ ions. The enzyme activity is restored by 86% after dialysis compared to the control enzyme preparation. No effect on in presence of other monovalent cations (Rb+, Cs+, and K+). The effects of sodium ions on dextransuccrase activity are specific, thus it can be useful to block its catalytic activity, and reducing the cariogenic potential of Streptococcus mutans
Pb2+
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drastically decreases the specific activity in soluble enzyme and immobilized enzyme form
potassium chloride
30.81% inhibition of transferase activity at 100 mM; 33.33% inhibition of transferase activity at 100 mM; 35.13% inhibition of transferase activity at 100 mM
pyridoxal 5'-phosphate
98.5% inhibition at 25 mM, sucrose protects against the inhibition
sodium lauryl sulfate
51.35% inhibition of transferase activity at 100 mM; 51.35% inhibition of transferase activity at 100 mM; 52.38% inhibition of transferase activity at 100 mM
sodium metasilicate
29.73% inhibition of transferase activity at 100 mM; 35.05% inhibition of transferase activity at 100 mM; 37.84% inhibition of transferase activity at 100 mM
Ca2+
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1 mM, stimulates activity of enzyme N, enzyme I is inhibited
Co2+
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inhibition by binding to 2 types of metal ion sites, one type consists of a single site and has a low apparent affinity to Ca2+, at the remaining site(s), Ca2+ has a much higher apparent affinity than Zn2+, Ni2+ or Co2+ and prevents inhibition by these metal ions
Co2+
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1 mM, stimulates activity of enzyme N, enzyme I is inhibited
Cu2+
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drastically decreases the specific activity in soluble enzyme and immobilized enzyme form
EDTA
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addition of Ca2+ or Co2+ restores activity; addition of dextran partially protects
EDTA
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enzyme I not affected, enzyme N inhibited, inhibition overcome by Ca2+
EDTA
32.43% inhibition of transferase activity at 20 mM; 37.84% inhibition of transferase activity at 20 mM; 40.48% inhibition of transferase activity at 20 mM
Fe2+
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drastically decreases the specific activity in soluble enzyme and immobilized enzyme form
Fe2+
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1 mM, stimulates activity of enzyme N, enzyme I is inhibited
Fe2+
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slightly inhibits the native, but not the recombinant enzyme
Guanidine-HCl
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0.025 M, 65% inhibition of enzyme N, no effect on enzyme I
methyl-alpha-D-glucoside
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50 mM, activates release of D-fructose (sucrase activity), inhibits synthesis of dextran (transferase activity)
Mg2+
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1 mM, stimulates activity of enzyme N, enzyme I is inhibited
Mg2+
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slightly inhibits the native, but not the recombinant enzyme
Mn2+
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inhibits hydrolysis activity almost entirely, but activates transferase activity at 1 mM
Ni2+
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inhibition by binding to 2 types of metal ion sites, one type consists of a single site and has a low apparent affinity to Ca2+, at the remaining site(s), Ca2+ has a much higher apparent affinity than Zn2+, Ni2+ or Co2+ and prevents inhibition by these metal ions
o-phthalaldehyde
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inactivation follows pseudo-first order reaction, sucrose and glucose protect
sucrose
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the 155000 Da enzyme form is more sensitive to substrate inhibition than the 170000 Da precursor form
sucrose
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substrate inhibition at concentrations over 584 mM sucrose
Urea
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0.25 M, enzyme N completely inactivated, enzyme I retains 60% of its activity
Urea
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enzyme I loses 50% of its activity at 2.4 M urea, enzyme II is inhibited to 50% by 1.7 M urea
Urea
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denatures the enzyme and causes 45%, 90% and 98% loss of activity within 30 min when treated at 1 M, 3 M, and 5 M concentration, respectively
Zn2+
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drastically decreases the specific activity in soluble enzyme and immobilized enzyme form
Zn2+
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inhibits hydrolysis activity but has no effect on transferase activity which constitutes to more than 90% of the overall activity, Zn2+ has therefore no influence on overall activity
Zn2+
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inhibition by binding to 2 types of metal ion sites, one type consists of a single site and has a low apparent affinity to Ca2+, at the remaining site(s), Ca2+ has a much higher apparent affinity than Zn2+, Ni2+ or Co2+ and prevents inhibition by these metal ions
additional information
the compounds also inhibit the sucrase activity, overview; the compounds also inhibit the sucrase activity, overview; the compounds also inhibit the sucrase activity, overview
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additional information
the compounds also inhibit the sucrase activity, overview; the compounds also inhibit the sucrase activity, overview; the compounds also inhibit the sucrase activity, overview
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additional information
the compounds also inhibit the sucrase activity, overview; the compounds also inhibit the sucrase activity, overview; the compounds also inhibit the sucrase activity, overview
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additional information
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D-glucose has no effect on enzyme ativity; water-soluble extract of Curcuma sp., strong enzyme inhibition
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additional information
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aqueous plant extracts from wood sticks of Acacia arabica, Azadirachta indica, Pongamia pinnata, and Salvadora persica are inhibitory. 5 mg Phenolic content in aqueous extracts of chewing stem sticks produce 35-40% inhibition of the enzyme activity, best inhibition at 7-7.5 for the phenolic compounds, and at pH 5.0-6.0 for plant extracts
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