Information on EC 2.4.1.5 - dextransucrase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.4.1.5
-
RECOMMENDED NAME
GeneOntology No.
dextransucrase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sucrose + [(1->6)-alpha-D-glucosyl]n = D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
-
sucrose + [(1->6)-alpha-D-glucosyl]n = D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
involvement of the three conserved amino acids (Asp551, Glu589, and Asp662) in the organic reaction enzyme mechanism for the biosynthesis of dextran at the active site of dextransucrase by the insertion mechanism addition of D-glucose to the reducing-end of a growing dextran chain
-
sucrose + [(1->6)-alpha-D-glucosyl]n = D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
catalytic reaction mechanism for dextran elongation, overview
-
sucrose + [(1->6)-alpha-D-glucosyl]n = D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
involvement of the three conserved amino acids (Asp551, Glu589, and Asp662) in the organic reaction enzyme mechanism for the biosynthesis of dextran at the active site of dextransucrase by the insertion mechanism addition of D-glucose to the reducing-end of a growing dextran chain
Leuconostoc mesenteroides B-512FMC
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Starch and sucrose metabolism
-
SYSTEMATIC NAME
IUBMB Comments
sucrose:(1->6)-alpha-D-glucan 6-alpha-D-glucosyltransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
B-512F dextransucrase
-
-
B-512F dextransucrase
Leuconostoc mesenteroides B-512FMC
-
-
-
B-512FMC dextransucrase
-
-
B-512FMC dextransucrase
Leuconostoc mesenteroides B-512FMC, Leuconostoc mesenteroides FT045B
-
-
-
CEP
-
-
-
-
DexT
B1N0B6
-
DexT
B1N0B6
-
-
dextran-sucrase
-
-
-
-
DS
-
-
-
-
DSR
Weissella cibaria LBAE K39
-
-
-
DSR
H1X7X9
-
DSR-F
D5FS20
-
DSR-F
Leuconostoc citreum B/110-1-2
D5FS20
-
-
DSR-S
Leuconostoc mesenteroides NRRL B-512F
-
;
-
DSRB742
Leuconostoc mesenteroides B-742CB
-
-
-
DSRBCB4
Leuconostoc mesenteroides B-1299CB4
-
-
-
DSRC39-2
H1X7X9
-
DSRC39-2
H1X7X9
-
-
DSRS
-
-
-
-
DSRS
Leuconostoc mesenteroides NRRL B-512F
-
-
-
DSRWC
B9UNL6
-
DsrX
Leuconostoc mesenteroides CGMCC 1.544
-
-
-
FT045B dextransucrase
-
-
FT045B dextransucrase
Leuconostoc mesenteroides B-512FMC, Leuconostoc mesenteroides FT045B
-
-
-
glucansucrase
C7DT60
-
glucansucrase
Leuconostoc lactis EG001
C7DT60
-
-
glucansucrase
Leuconostoc mesenteroides subsp. dextranicum NRRL B-1146
-
;
-
glucansucrase
-
-
glucansucrase
B9UNL6
-
glucosyltransferase
Leuconostoc mesenteroides subsp. dextranicum NRRL B-1146
-
-
-
glucosyltransferase, sucrose-1,6-alpha-glucan
-
-
-
-
glycosyltransferase R
-
-
SGE
-
-
-
-
sucrose 6-glucosyltransferase
-
-
-
-
sucrose:1, 6-alpha-D-glucan 6-alpha-glucosyltransferase
-
-
sucrose:1, 6-alpha-D-glucan 6-alpha-glucosyltransferase
Leuconostoc mesenteroides B-512F
-
-
-
sucrose:1,6-alpha-D-glucan-6-alpha-D-glucosyltransferase
-
-
additional information
-
the enzyme belongs to the glycoside hydrolase family 70
additional information
Leuconostoc mesenteroides B-512F
-
the enzyme belongs to the glycoside hydrolase family 70
-
CAS REGISTRY NUMBER
COMMENTARY
9032-14-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene dexYG
-
-
Manually annotated by BRENDA team
strain 121
-
-
Manually annotated by BRENDA team
Lactobacillus reuteri 121
strain 121
-
-
Manually annotated by BRENDA team
formerly Leuconostoc mesenteroides B-742
-
-
Manually annotated by BRENDA team
genes HJ-P4 and HJ-P5
-
-
Manually annotated by BRENDA team
isolated from sugarcane juice
UniProt
Manually annotated by BRENDA team
strain HJ-P4, gene LcDS
UniProt
Manually annotated by BRENDA team
strain KACC 91035, isolated from dongchimi-kimchi, a watery radish kimchi
-
-
Manually annotated by BRENDA team
Leuconostoc citreum B/110-1-2
-
UniProt
Manually annotated by BRENDA team
Leuconostoc citreum B/110-1-2
isolated from sugarcane juice
UniProt
Manually annotated by BRENDA team
Leuconostoc citreum HJ-P4
strain HJ-P4, gene LcDS
UniProt
Manually annotated by BRENDA team
Leuconostoc citreum KACC 91035
strain KACC 91035, isolated from dongchimi-kimchi, a watery radish kimchi
-
-
Manually annotated by BRENDA team
Leuconostoc citreum NRRL B-742
formerly Leuconostoc mesenteroides B-742
-
-
Manually annotated by BRENDA team
strain EG001, isolated from lactic acid bacteria in Kimchi, a traditional Korean fermented food
C7DT60
UniProt
Manually annotated by BRENDA team
Leuconostoc lactis EG001
strain EG001, isolated from lactic acid bacteria in Kimchi, a traditional Korean fermented food
C7DT60
UniProt
Manually annotated by BRENDA team
a constitutive mutant of Leuconostoc mesenteroides B-512FMC; a constitutive mutant of Leuconostoc mesenteroides FT045B
-
-
Manually annotated by BRENDA team
B-1375; NRRL B-1416
-
-
Manually annotated by BRENDA team
Birmingham strain
-
-
Manually annotated by BRENDA team
gene dsrBCB4
UniProt
Manually annotated by BRENDA team
genes HJ-S7 and HJ-S13
-
-
Manually annotated by BRENDA team
isolated from fermented cabbage
-
-
Manually annotated by BRENDA team
mutants constitutive for glucansucrase
-
-
Manually annotated by BRENDA team
strain 0326, gene dexYG
UniProt
Manually annotated by BRENDA team
strain 0326, gene dexYG
-
-
Manually annotated by BRENDA team
strain B-1299
-
-
Manually annotated by BRENDA team
strain B-1299CB
-
-
Manually annotated by BRENDA team
strain B-1299CB BF563
-
-
Manually annotated by BRENDA team
strain B-1299CB4, gene dsrBCB4
-
-
Manually annotated by BRENDA team
strain B-1299CB4, gene dsrBCB4
Uniprot
Manually annotated by BRENDA team
strain B-512 FMC
-
-
Manually annotated by BRENDA team
strain B-512FMC
-
-
Manually annotated by BRENDA team
strain B-512FMCM
-
-
Manually annotated by BRENDA team
strain CGMCC 1.544, gene dsrX
-
-
Manually annotated by BRENDA team
strain FT 045 B
-
-
Manually annotated by BRENDA team
strain LM-0326, gene dexYG
-
-
Manually annotated by BRENDA team
strain NRRL B-640
-
-
Manually annotated by BRENDA team
strain NRRL B512-F
-
-
Manually annotated by BRENDA team
strains IBT-PQ and NRRL B-1299, gene dsrP
-
-
Manually annotated by BRENDA team
strains NRRL B-640 and NRRL B-512F
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides 0326
strain 0326, gene dexYG
UniProt
Manually annotated by BRENDA team
Leuconostoc mesenteroides 0326
strain 0326, gene dexYG
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-1299
strain B-1299
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-1299CB
strain B-1299CB
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-1299CB
strain B-1299CB BF563
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-1299CB4
strain B-1299CB4, gene dsrBCB4
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-1299CB4
strain B-1299CB4, gene dsrBCB4
Uniprot
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-1375
B-1375
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-512 FMC
strain B-512 FMC
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-512F
strain B-512F
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-512FM
B-512FM
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-512FMC
a constitutive mutant of Leuconostoc mesenteroides B-512FMC
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-512FMC
B-512FMC
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-512FMC
strain B-512FMC
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-512FMCM
B-512FMCM
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-512FMCM
strain B-512FMCM
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-742CB
B-742CB
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides Birmingham
Birmingham strain
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides CGMCC 1.544
strain CGMCC 1.544, gene dsrX
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides FT 045 B
strain FT 045 B
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides FT045B
a constitutive mutant of Leuconostoc mesenteroides FT045B
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides IAM 1046
IAM 1046
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides IBT-PQ
IBT-PQ
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides KIBGE IB-22
isolated from fermented cabbage
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides Lm 28
strain Lm 28
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides LM-0326
strain LM-0326, gene dexYG
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B-1299
NRRL B-1299
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B-1299
NRRL B-1299
Uniprot
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B-1416
NRRL B-1416
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRl B-512(F)
NRRl B-512(F)
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B-512F
NRRL B-512F
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B-512F
strain NRRL B-512F
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B-640
-
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B-640
strain NRRL B-640
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B512-F
strain NRRL B512-F
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides PCSIR-4
strain PCSIR-4
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides Sikhae
Sikhae
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides subsp. dextranicum NRRL B-1146
strain NRRL B-1146
-
-
Manually annotated by BRENDA team
isolated from soil from a sugarcane field in Assam, India
-
-
Manually annotated by BRENDA team
Penicillium aculeatum
strain ATCC 10409
-
-
Manually annotated by BRENDA team
Streptococcus mutans 6715
6715
-
-
Manually annotated by BRENDA team
Streptococcus mutans E49
E49
-
-
Manually annotated by BRENDA team
Streptococcus mutans HS6
HS6
-
-
Manually annotated by BRENDA team
isolated from human saliva, gene dsrWC
UniProt
Manually annotated by BRENDA team
isolated from wheat sourdough, single copy gene
-
-
Manually annotated by BRENDA team
Weissella cibaria LBAE K39
isolated from wheat sourdough, single copy gene
-
-
Manually annotated by BRENDA team
isolated from wheat sourdough, single copy gene
H1X7X9
UniProt
Manually annotated by BRENDA team
isolated from wheat sourdough, single copy gene
H1X7X9
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
dextransucrases are glucansucrases belonging to the glycoside hydrolase family GH70
evolution
H1X7X9
dextransucrases are glucansucrases belonging to the glycoside hydrolase family GH70
evolution
D5FS20
the enzyme belongs to the glycoside-hydrolase family GH70, transglucosidases that produce a-glucans from sucrose
evolution
B1N0B6, -
dextransucrase belongs to the glycohydrolase family GH 70
evolution
Leuconostoc citreum B/110-1-2
-
the enzyme belongs to the glycoside-hydrolase family GH70, transglucosidases that produce a-glucans from sucrose
-
evolution
-
dextransucrase belongs to the glycohydrolase family GH 70
-
physiological function
H1X7X9
the dextransucrase is responsible for production of dextran with predominant alpha-(1->) linkages
physiological function
D5FS20
in presence of sucrose, the strain B/110-1-2 produces two cell-associated dextransucrases (31.54% of the total glucosyltransferase activity) with molecular weights of 160 and 240 kDa and a soluble dextransucrase (68.46% of the total glucosyltransferase activity) at 160-180 kDa
physiological function
Leuconostoc citreum B/110-1-2
-
in presence of sucrose, the strain B/110-1-2 produces two cell-associated dextransucrases (31.54% of the total glucosyltransferase activity) with molecular weights of 160 and 240 kDa and a soluble dextransucrase (68.46% of the total glucosyltransferase activity) at 160-180 kDa
-
physiological function
-
the dextransucrase is responsible for production of dextran with predominant alpha-(1->) linkages
-
evolution
Weissella cibaria LBAE K39, Weissella confusa LBAE C39-2
-
dextransucrases are glucansucrases belonging to the glycoside hydrolase family GH70
-
additional information
H1X7X9
the amino acids involved in catalysis, E592, D554, D665 are conserved in the catalytic core
additional information
D5FS20
amino acid residues D557, E595, and D667 are forming the catalytic triad
additional information
Leuconostoc citreum B/110-1-2
-
amino acid residues D557, E595, and D667 are forming the catalytic triad
-
additional information
-
the amino acids involved in catalysis, E592, D554, D665 are conserved in the catalytic core
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1'-beta-D-fructofuranosyl alpha-acarbose
D-fructose + acarbose
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-512 FMC
-
-
-
-
-
alpha-D-glucopyranosyl fluoride + ?
?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRl B-512(F)
-
-
-
-
?
myricetin + sucrose
?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-512F, Leuconostoc mesenteroides NRRL B-23192
-
49% conversion
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
O52224
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
high amounts of enzyme catalyze the hydrolysis of the D-glucose residues from the ends of the dextran chains, giving a decrease in the amount of dextran
-
r
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
participates in glucan synthesis
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
native enzyme produces mainly 6-linked glucopyranosylresidues, while Escherichia coli recombinant enzyme produces a glucan consisting of 70% 6-linked glucopyranosyl residues and 15% 3,6-glucopyranosyl residues. Mutant enzyme T350K and S455K produce a glucan with 85% 6-linked glucopyranosyl residues. The mutant T350K/S455K produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
with increasing concentrations of sucrose, from 0.1 to 4.0 M, the amount of high-molecular weight dextran decreases with a concomitant increase in low-molecular weight dextran. At 0.1 M sucrose, pH 5.5, and 28C, 99.8% of the dextran had a MW of more than 1000000 Da and at 4.0 M sucrose, 69.9% have a MW below 100000 Da and 30.1% have a MW of more than 1000000 Da, giving a bimodal distribution. The degree of branching increased from 5% for 0.1 M sucrose to 16.6% for 4.0 M sucrose. The temperature has very little effect on the size of the dextran, which is above 1000000 Da, but it has a significant effect on the degree of branching, which is 4.8% at 4 C and increases to 14.7% at 45C. Both the molecular weight and the degree of branching are not significantly affected by different pH values between 4.5 and 6.0
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
-
dextransucrase preferentially produces an isomaltooligosaccharide series, whose concentration is always low because of the high ability of these products to be elongated and form high molecular weight dextran. In dextransucrase, the A repeats define anchoring zones for the growing chains, favoring their elongation. Based on these results, a semi-processive mechanism involving only one active site and an elongation by the non-reducing end is proposed
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides B-512F
-
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides B-512FM
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRL B-512F
-
native enzyme produces mainly 6-linked glucopyranosylresidues, while Escherichia coli recombinant enzyme produces a glucan consisting of 70% 6-linked glucopyranosyl residues and 15% 3,6-glucopyranosyl residues. Mutant enzyme T350K and S455K produce a glucan with 85% 6-linked glucopyranosyl residues. The mutant T350K/S455K produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRL B-512F
-
dextransucrase preferentially produces an isomaltooligosaccharide series, whose concentration is always low because of the high ability of these products to be elongated and form high molecular weight dextran. In dextransucrase, the A repeats define anchoring zones for the growing chains, favoring their elongation. Based on these results, a semi-processive mechanism involving only one active site and an elongation by the non-reducing end is proposed
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides Sikhae
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRl B-512(F)
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRl B-512(F)
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRl B-512(F)
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRl B-512(F)
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRl B-512(F)
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRl B-512(F)
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRl B-512(F)
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRl B-512(F)
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRl B-512(F)
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Streptococcus mutans E49
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Streptococcus mutans E49
-
participates in glucan synthesis
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRL B-1416
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRL B-1416
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRL B-1299
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides NRRL B-1299
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides IBT-PQ
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Streptococcus mutans 6715
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides B-512FMC
-
high amounts of enzyme catalyze the hydrolysis of the D-glucose residues from the ends of the dextran chains, giving a decrease in the amount of dextran
-
r
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides IAM 1046
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides B-742CB
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Streptococcus mutans HS6
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides B-512FMCM
-
with increasing concentrations of sucrose, from 0.1 to 4.0 M, the amount of high-molecular weight dextran decreases with a concomitant increase in low-molecular weight dextran. At 0.1 M sucrose, pH 5.5, and 28C, 99.8% of the dextran had a MW of more than 1000000 Da and at 4.0 M sucrose, 69.9% have a MW below 100000 Da and 30.1% have a MW of more than 1000000 Da, giving a bimodal distribution. The degree of branching increased from 5% for 0.1 M sucrose to 16.6% for 4.0 M sucrose. The temperature has very little effect on the size of the dextran, which is above 1000000 Da, but it has a significant effect on the degree of branching, which is 4.8% at 4 C and increases to 14.7% at 45C. Both the molecular weight and the degree of branching are not significantly affected by different pH values between 4.5 and 6.0
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides Birmingham
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Leuconostoc mesenteroides B-1375
-
-
-
?
sucrose + 1,5-anhydro-D-fructose
alpha-D-glucopyranosyl-(1,6)-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-512F
-
the amount of 1,5-anhydro-D-fructo-glucooligosaccharides produced and the average DP increases by using a high sucrose/1,5-anhydro-D-fructose molar ratio and high total sugar concentration
-
-
?
sucrose + 2-chloroethanol
2-chloroethyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + 3-methyl-1-butanol
D-fructose + 3-methylbutyl alpha-D-glucoside
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1299CB
-
-
-
-
?
sucrose + 4-chlorobutanol
4-chlorobutyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + 6-chlorohexanol
6-chlorohexyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + acceptor
?
show the reaction diagram
-
-
-
-
?
sucrose + alpha-butylglucopyranoside
alpha-D-glucopyranosyl-(1,6)-O-butyl-alpha-D-glucopyranoside + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-butyl-alpha-D-glucopyranoside
show the reaction diagram
-
-
-
-
?
sucrose + alpha-D-glucopyranoside
?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1299
-
three homologous series (S1S3) of methyl alpha-D-glucooligosaccharides. Series S2 and S3 are characterized by the presence of alpha(1,2) linkages, in combination with alpha(1,6) bonds. Two parameters, sucrose to acceptor concentration ratio (S/A) and the total sugar concentration (TSC) determine the yield of methyl alpha-D-glucooligosaccharides. The maximum concentration achieved of the first acceptor product, methyl alpha-D-isomaltoside, is 65 mM using a S/A 1:4 and a TSC of 336 g/l. When increasing temperature, a shift of selectivity towards compounds containing alpha(1,2) bonds is observed. The formation of leucrose as a side process reaches values of 32 g/l at high sucrose concentrations
-
-
?
sucrose + butan-1-ol
butyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + dextran
D-fructose + ?
show the reaction diagram
Penicillium aculeatum
-
glucose transfer reaction
-
-
?
sucrose + dextran
D-fructose + ?
show the reaction diagram
-
glucose transfer, a step in production of isomaltose, overview, glucose transfer
-
-
?
sucrose + dextran
D-fructose + ?
show the reaction diagram
Leuconostoc mesenteroides NRRL B-512F
-
glucose transfer, a step in production of isomaltose, overview, glucose transfer
-
-
?
sucrose + dextran
?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B512-F
-
glucose transfer reaction, determination of the dextransucrase minimal motif involved in dextran binding, strong interaction with dextran is localized between amino acids N1397 and A1527 of the C-terminal domain, GBD-7, and consists of six YG repeats, overview. The motif containing enzyme shows very high affinity for isomaltohexaose and longer dextrans and is involved in polymer formation, overview
-
-
?
sucrose + ethanol
ethyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + ethanol
D-fructose + ethyl alpha-D-glucoside
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1299CB
-
-
-
-
?
sucrose + gentobiose
?
show the reaction diagram
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + hydroquinone
D-fructose + 4-hydroxyphenyl-alpha-D-glucopyranoside
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1299CB
-
optimum condition for 4-hydroxyphenyl-alpha-D-glucopyranoside synthesis is 450 mM hydroquinone, 215 mM sucrose, and 0.55 U/ml dextransucrase
NMR product identification, the product shows antioxidant nitrite- and diphenylpicryl-hydrazyl scavenging activity, to a higher extent than beta-arbutin
-
?
sucrose + isomaltohexaose
?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B512-F
-
glucose transfer reaction, determination of the dextransucrase minimal motif involved in dextran binding, strong interaction with dextran is localized between amino acids N1397 and A1527 of the C-terminal domain, GBD-7, and consists of six YG repeats, overview. The motif containing enzyme shows very high affinity for isomaltohexaose and longer dextrans and is involved in polymer formation, overview
-
-
?
sucrose + isomaltose
D-fructose + isomaltotriose
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-512FMC
-
-
-
-
?
sucrose + L-ascorbic acid
D-fructose + L-ascorbic acid 2-glucoside
show the reaction diagram
C7DT60, -
recombinant glucansucrase
the glycosylated product has the potential as an antioxidant in industrial applications
-
?
sucrose + L-ascorbic acid
D-fructose + L-ascorbic acid 2-glucoside
show the reaction diagram
Leuconostoc lactis EG001
C7DT60
recombinant glucansucrase
the glycosylated product has the potential as an antioxidant in industrial applications
-
?
sucrose + maltose
?
show the reaction diagram
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + methanol
methyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + methanol
D-fructose + methyl alpha-D-glucoside
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1299CB
-
-
-
-
?
sucrose + N-(tert-butoxycarbonyl)-L-serine methyl ester
N-tert-butoxycarbonyl-3-O-alpha-D-glucopyranosyl-L-serine methyl ester + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + n-propanol
D-fructose + propyl alpha-D-glucoside
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1299CB
-
-
-
-
?
sucrose + N-tert-butoxycarbonyl-D-serine methyl ester
N-tert-butoxycarbonyl-3-O-alpha-D-glycopyranosyl-D-serine methyl ester + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + propan-1-ol
propyl alpha-D-glucopyranoside + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + salicin
?
show the reaction diagram
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + tert-butanol
D-fructose + tert-butyl alpha-D-glucoside
show the reaction diagram
-
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
-
-
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
C7DT60, -
-
-
-
-
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
B9UNL6
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
a highly processive mechanism of dextran biosynthesis, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
B9UNL6
In the presence of maltose, the most abundant reaction product is panose, i.e. MP1 or alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,4)-D-glucopyranose, with 35.3%, detailed NMR product identification and structure analysis, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
the enzyme performs dextran synthesis from sucrose, but D-glucose and sucrose are no initiator primers. Both D-glucose and dextran are covalently attached to B-512FMC dextransucrase at the active site during polymerization. The D-glucose moieties of sucrose are added to the reducing ends of the covalently linked growing dextran chains. Asp551, Glu589, and Asp 622 at the active sites of glucansucrases participate in the polymerization of dextran and related glucans from a single active site by the addition of the D-glucose moiety of sucrose to the reducing ends of the covalently linked glucan chains in a two catalytic-site, insertion mechanism overview. In the early stages of the reaction the products are D-glucose, D-fructose, leucrose, and isomaltodextrins in low, exponentially decreasing amounts from DP 2-5, with minuscule amounts of DP 6-12, but exponentially decreasing amounts of isomaltodextrins, down to minuscule amounts of DP 20-25, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc mesenteroides B-512FMC
-
a highly processive mechanism of dextran biosynthesis, overview, the enzyme performs dextran synthesis from sucrose, but D-glucose and sucrose are no initiator primers. Both D-glucose and dextran are covalently attached to B-512FMC dextransucrase at the active site during polymerization. The D-glucose moieties of sucrose are added to the reducing ends of the covalently linked growing dextran chains. Asp551, Glu589, and Asp 622 at the active sites of glucansucrases participate in the polymerization of dextran and related glucans from a single active site by the addition of the D-glucose moiety of sucrose to the reducing ends of the covalently linked glucan chains in a two catalytic-site, insertion mechanism overview. In the early stages of the reaction the products are D-glucose, D-fructose, leucrose, and isomaltodextrins in low, exponentially decreasing amounts from DP 2-5, with minuscule amounts of DP 6-12, but exponentially decreasing amounts of isomaltodextrins, down to minuscule amounts of DP 20-25, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc lactis EG001
C7DT60
-
-
-
-
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc mesenteroides subsp. dextranicum NRRL B-1146
-
-
-
-
-
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
H1X7X9
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
D5FS20
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
B1N0B6, -
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
DSase-catalyzed dextran elongation
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
B1N0B6, -
substrate is dextran
product analysis by thin layer chromatography
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc mesenteroides B-512FMC
-
-
-, the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc citreum B/110-1-2
D5FS20
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc citreum NRRL B-742
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc mesenteroides FT045B
-
-
-, the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
H1X7X9
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
Weissella cibaria LBAE K39
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
B1N0B6, -
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
B1N0B6, -
substrate is dextran
product analysis by thin layer chromatography
-
?
luteolin + sucrose
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-512F, Leuconostoc mesenteroides NRRL B-23192
-
44% conversion
luteolin-3'-O-alpha-D-glucopyranoside is the major product
-
?
additional information
?
-
-
a lysine residue is present at the active site and is essential for the activity
-
-
-
additional information
?
-
-
the enzyme also catalyzes hydrolysis of D-glucose from the non-reducing ends of dextran chains and transfer of D-glucose from the non-reducing ends of dextran chains to maltose with low efficiency
-
-
-
additional information
?
-
-
the enzyme possesses enhanced levels of sucrose hydrolyzing activity
-
-
-
additional information
?
-
-
purified dextransucrase possesses an invertase-like activity
-
-
-
additional information
?
-
Q8G9Q2
the enzyme catalyzes the formation of both alpha-1,6 and alpha1,2-glycosidic linkages. The catalytic domain CD1 is specific for the synthesis of alpha-1,6 glucosidic bonds and CD2 only catalyzes the formation of alpha-1,2 linkage
-
-
-
additional information
?
-
-
triple mutation N1134S/N1135E/S1136V converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme. Mutant enzyme P1026V/I1029V/N1134S/N1135E/S1136V synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
-
-
-
additional information
?
-
-
induced by growth on sucrose
-
-
-
additional information
?
-
-
activity assay by measurement of release of reducing sugar from sucrose by the 3,5-dinitrosalicylic acid method
-
-
-
additional information
?
-
Q2I2N5
glucose transfer from sucrose to dextran of about 68 kDa by the recombinant enzyme expressed in Escherichia coli
-
-
-
additional information
?
-
-
glucose transfer from sucrose to dextrans leading to polymerization with release of D-fructose, the enzyme contains an active site His residue as well as an essential lysine residue
-
-
-
additional information
?
-
-
glucose transfer from sucrose, synthesis of panose
-
-
-
additional information
?
-
-
keta-sucrose, produced by pyranose 2-oxidase, is polymerized to keto-dextran by the dextrasucrase
-
-
-
additional information
?
-
-
synthesis of a series of cellobio-oligosaccharides from cellobiose by dextransucrase performed transglycosylation, method optimization, overview
-
-
-
additional information
?
-
-
the dextransucrase DSRBCB4 synthesizes only alpha-1,6-linked dextran, the recombinantly expressed DSRBCB4 synthesizes oligosaccharides in the presence of maltose or isomaltose as an acceptor, the products including alpha-1,6-linked glucosyl residues in addition to the maltosyl or isomaltosyl residue, conserved amino acid residues in the catalytic core, D530, E568, and D641, that are critical for enzyme activity, NMR product analysis, overview
-
-
-
additional information
?
-
-
the enzyme synthesizes isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, overview
-
-
-
additional information
?
-
-
wild-type and mutant enzymes from strain Lm M286 produce a resistant glucan, based on endo-dextranase and amyloglucosidase hydrolysis. The extracellular enzymes from strain Lm M286 catalyse acceptor reactions and transfer the glucose unit from sucrose to maltose to produce glucooligosaccharides , synthesisis of a dextran-type polysaccharide, overview
-
-
-
additional information
?
-
-
dextransucrase can possibly transfer acarbose to various types of dextransucrase acceptors
-
-
-
additional information
?
-
O52224
engineered recombinant mutant enzyme DXSR, a fusion of dextransucrase and dextranase, produces linear isomalto-oligosaccharides with DP2-DP10 using sucrose as a sole substrate. DXSR gives 30fold higher production of isomalto-oligosaccharides than that of an equal activity mixture of the two enzymes such as dextranase and dextransucrase
-
-
-
additional information
?
-
-
measurement of liberation of D-fructose from sucrose
-
-
-
additional information
?
-
-
no activity with 2-propanol, MALDI-TOF-mass spectrometry and NMR, structures and HMBC correlations, product analysis
-
-
-
additional information
?
-
B9UNL6
the recombinant DSRWC synthesizes oligosaccharides in the presence of maltose or isomaltose as an acceptor and the synthesized products include alpha-1,6-linked glucosyl residues in addition to the maltosyl or isomaltosyl residue. rDSRWC synthesizes water-soluble polymers using sucrose as substrate, and rDSRBWC synthesizes dextran and leucrose [alpha-D-glucopyranosyl-(1,5)-beta-D-fructofuranose]
-
-
-
additional information
?
-
A9ZRX3, -
the recombinant enzyme successfully produces a series of isomaltooligosaccharides from sucrose and maltose, on the basis of its transglycosylation activity
-
-
-
additional information
?
-
B1N0B6, -
DexT catalyzes the polymerization of sucrose to dextran via a transglucosyl reaction
-
-
-
additional information
?
-
D5FS20
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching
-
-
-
additional information
?
-
-
dextransucrase promotes the sucrose cleavage polymerizing the glucose into dextran chain and releasing the fructose moiety
-
-
-
additional information
?
-
D5FS20
structural analysis, by HPAEC-PAD, HPSEC, and 13C-NMR, of the polymer and oligodextrans produced by the B/110-1-2 dextransucrases, overview
-
-
-
additional information
?
-
-
DSase can quickly proceed to elongation because the decomposition rate of the ESdex complex is very small
-
-
-
additional information
?
-
-
optimization of conditions for dextransucrase activity assay
-
-
-
additional information
?
-
D5FS20
the recombinant enzyme catalyzes oligosaccharides synthesis from sucrose as donor and maltose acceptor
-
-
-
additional information
?
-
Leuconostoc mesenteroides B-512F
-
glucose transfer from sucrose to dextrans leading to polymerization with release of D-fructose, the enzyme contains an active site His residue as well as an essential lysine residue
-
-
-
additional information
?
-
Leuconostoc mesenteroides B-512F
-
the enzyme synthesizes isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, overview
-
-
-
additional information
?
-
Leuconostoc mesenteroides 0326
Q2I2N5
glucose transfer from sucrose to dextran of about 68 kDa by the recombinant enzyme expressed in Escherichia coli
-
-
-
additional information
?
-
Leuconostoc mesenteroides B-1299CB4
-
the dextransucrase DSRBCB4 synthesizes only alpha-1,6-linked dextran, the recombinantly expressed DSRBCB4 synthesizes oligosaccharides in the presence of maltose or isomaltose as an acceptor, the products including alpha-1,6-linked glucosyl residues in addition to the maltosyl or isomaltosyl residue, conserved amino acid residues in the catalytic core, D530, E568, and D641, that are critical for enzyme activity, NMR product analysis, overview
-
-
-
additional information
?
-
Leuconostoc mesenteroides NRRl B-512(F)
-
the enzyme possesses enhanced levels of sucrose hydrolyzing activity
-
-
-
additional information
?
-
Leuconostoc mesenteroides NRRl B-512(F)
-
a lysine residue is present at the active site and is essential for the activity
-
-
-
additional information
?
-
Lactobacillus reuteri 121
-
triple mutation N1134S/N1135E/S1136V converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme. Mutant enzyme P1026V/I1029V/N1134S/N1135E/S1136V synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
-
-
-
additional information
?
-
Leuconostoc mesenteroides B-1299CB
-
no activity with 2-propanol, MALDI-TOF-mass spectrometry and NMR, structures and HMBC correlations, product analysis
-
-
-
additional information
?
-
Leuconostoc mesenteroides B-512FMC
-
the enzyme also catalyzes hydrolysis of D-glucose from the non-reducing ends of dextran chains and transfer of D-glucose from the non-reducing ends of dextran chains to maltose with low efficiency
-
-
-
additional information
?
-
Streptococcus mutans HS6
-
purified dextransucrase possesses an invertase-like activity
-
-
-
additional information
?
-
Leuconostoc citreum B/110-1-2
D5FS20
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching, the recombinant enzyme catalyzes oligosaccharides synthesis from sucrose as donor and maltose acceptor
-
-
-
additional information
?
-
Leuconostoc citreum B/110-1-2
D5FS20
structural analysis, by HPAEC-PAD, HPSEC, and 13C-NMR, of the polymer and oligodextrans produced by the B/110-1-2 dextransucrases, overview
-
-
-
additional information
?
-
Leuconostoc mesenteroides B-512FMCM
-
synthesis of a series of cellobio-oligosaccharides from cellobiose by dextransucrase performed transglycosylation, method optimization, overview
-
-
-
additional information
?
-
Leuconostoc citreum NRRL B-742
-
dextransucrase promotes the sucrose cleavage polymerizing the glucose into dextran chain and releasing the fructose moiety
-
-
-
additional information
?
-
Leuconostoc mesenteroides Lm 28
-
wild-type and mutant enzymes from strain Lm M286 produce a resistant glucan, based on endo-dextranase and amyloglucosidase hydrolysis. The extracellular enzymes from strain Lm M286 catalyse acceptor reactions and transfer the glucose unit from sucrose to maltose to produce glucooligosaccharides , synthesisis of a dextran-type polysaccharide, overview
-
-
-
additional information
?
-
B1N0B6, -
DexT catalyzes the polymerization of sucrose to dextran via a transglucosyl reaction
-
-
-
additional information
?
-
Leuconostoc citreum HJ-P4
A9ZRX3
the recombinant enzyme successfully produces a series of isomaltooligosaccharides from sucrose and maltose, on the basis of its transglycosylation activity
-
-
-
additional information
?
-
Leuconostoc mesenteroides B-512 FMC
-
dextransucrase can possibly transfer acarbose to various types of dextransucrase acceptors
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
show the reaction diagram
Streptococcus mutans, Streptococcus mutans E49
-
participates in glucan synthesis
-
-
?
sucrose + dextran
D-fructose + ?
show the reaction diagram
Penicillium aculeatum
-
glucose transfer reaction
-
-
?
sucrose + dextran
D-fructose + ?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-512F
-
glucose transfer, a step in production of isomaltose, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
B9UNL6
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-512FMC
-
a highly processive mechanism of dextran biosynthesis, overview
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
H1X7X9
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
D5FS20
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
B1N0B6, -
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc mesenteroides B-512FMC
-
-
the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc citreum B/110-1-2
D5FS20
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc citreum NRRL B-742
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
Leuconostoc mesenteroides FT045B
-
-
the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
H1X7X9
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
Weissella cibaria LBAE K39
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
show the reaction diagram
B1N0B6, -
-
-
-
?
additional information
?
-
-
induced by growth on sucrose
-
-
-
additional information
?
-
B1N0B6, -
DexT catalyzes the polymerization of sucrose to dextran via a transglucosyl reaction
-
-
-
additional information
?
-
D5FS20
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching
-
-
-
additional information
?
-
-
dextransucrase promotes the sucrose cleavage polymerizing the glucose into dextran chain and releasing the fructose moiety
-
-
-
additional information
?
-
D5FS20
structural analysis, by HPAEC-PAD, HPSEC, and 13C-NMR, of the polymer and oligodextrans produced by the B/110-1-2 dextransucrases, overview
-
-
-
additional information
?
-
Leuconostoc citreum B/110-1-2
D5FS20
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching
-
-
-
additional information
?
-
Leuconostoc citreum B/110-1-2
D5FS20
structural analysis, by HPAEC-PAD, HPSEC, and 13C-NMR, of the polymer and oligodextrans produced by the B/110-1-2 dextransucrases, overview
-
-
-
additional information
?
-
Leuconostoc citreum NRRL B-742
-
dextransucrase promotes the sucrose cleavage polymerizing the glucose into dextran chain and releasing the fructose moiety
-
-
-
additional information
?
-
B1N0B6, -
DexT catalyzes the polymerization of sucrose to dextran via a transglucosyl reaction
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
restores activity after EDTA treatment
Ca2+
-
activation below 1 mM
Ca2+
-
1 mM, slight activation
Ca2+
-
stimulates activity of enzyme N
Ca2+
-
low levels required for activity
Ca2+
B9UNL6
-
Ca2+
-
increases the enzyme activity in the fermentation culture 2fold at 0.005% CaCl2, and increases the enzyme stability to up to 120 days
Ca2+
A9ZRX3
activates 2.1fold at 0.1 mM, no activation at 5 mM
Ca2+
-
strong activation at 1 mM
Ca2+
-
required
Ca2+
-
enhances activity
CaCl2
-
activates 1.5fold at 0.5%, more ffective than CaCO3
CaCl2
-
activates 150% at 6 mM
CaCl2
-
activates slightly by 8% at 1 mM
Co2+
-
1 mM, stimulates activity of enzyme N, enzyme I is inhibited
Co2+
-
1 mM slight activation of enzyme I and II
Co2+
-
slightly activates the native and the recombinant enzyme
CoCl2
-
activates 22% at 4 mM
Fe2+
-
1 mM, stimulates activity of enzyme N
Fe2+
O52224
activates by 20.7% at 2 mM
FeSO4
-
inhibits 26.5% at 0.1 mM, but activates 39.5% at 0.05 mM
K+
O52224
activates by 13.6% at 2 mM
Li+
O52224
activates by 15.8% at 2 mM
Mg2+
-
1 mM, stimulates activity of enzyme N
MgCl2
-
activates 5% at 1 mM
MgCl2
-
activates slightly by 6% at 1 mM
MgSO4
-
activates 115.6% at 0.1 mM, 20% at 0.05 mM
Mn2+
-
activates the native and the recombinant enzyme
NaCl
-
activates 11% at 0.1 mM
Ni2+
O52224
activates by 7% at 2 mM
MnSO4
-
activates 68% at 0.1 mM, but inhibits at 0.05 mM by 26%
additional information
-
2 enzyme forms: I and N, enzyme I is gradually converted into enzyme N upon ageing, conversion is stimulated in the presence of NaCl
additional information
-
the enzyme is not or poorly affected by Ca2+, K+, and pepstatin
additional information
-
DSRBCB4 activity is not affected by Mg2+, K+, or Na+
additional information
-
little effect by 1 mM Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1'-beta-D-fructofuranosyl alpha-acarbose
-
strong inhibition
2,4,6-trinitrobenzene-sulphonic acid
-
inactivation
2-deoxy-2-fluoro-alpha-D-glucopyranosyl fluoride
-
competitive
2-mercaptoethanol
-
120 mM, 17% inhibition
3-Deoxy-3-fluoro-alpha-D-glucopyranosyl fluoride
-
competitive
3-deoxy-3-thio-alpha-D-glucopyranosyl fluoride
-
competitive
6'-Amino-6'-deoxysucrose
-
competitive
6-Deoxy-6-fluoro-alpha-D-glucopyranoside
-
very weak, noncompetitive
acarbose
-
strong inhibition
Ag+
-
1 mM, 94% inhibition
Ag+
O52224
99% inhibition at 2 mM
Al3+
-
strongly inhibits the native and the recombinant enzyme
alpha-D-glucopyranosyl fluoride
-
-
Ba2+
O52224
10% inhibition at 2 mM
Ca2+
-
weak competitive inhibition above 1 mM
Ca2+
-
1 mM, stimulates activity of enzyme N, enzyme I is inhibited
CaCl2
-
inhibits at 0.1 mM by 64%
Cd2+
O52224
23% inhibition at 2 mM
Co2+
-
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+
-
1 mM, stimulates activity of enzyme N, enzyme I is inhibited
Co2+
O52224
14% inhibition at 2 mM
Cu2+
-
strongly inhibits the native and the recombinant enzyme
Cu2+
O52224
65.5% inhibition at 2 mM
Cu2+
-
strong inhibition at 1 mM
D-fructose
-
competitive
D-glucono-1,5-lactone
-
competitive
D-glucuronic acid
-
reduced, noncompetitive
dextran derivatives
-
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
-
diethyldicarbonate
-
-
dithiothreitol
-
100 mM, 41% inhibition
EDTA
-
restored by Ca2+
EDTA
-
noncompetitive
EDTA
-
addition of Ca2+ or Co2+ restores activity; addition of dextran partially protects
EDTA
-
enzyme I not affected, enzyme N inhibited, inhibition overcome by Ca2+
EDTA
-
inactivation, reversible by Ca2+
EDTA
-
inhibits the native and the recombinant enzyme
EDTA
-
20% inhibition at 1 mM
EDTA
-
50% inhibition at 1 mM
Fe2+
-
1 mM, stimulates activity of enzyme N, enzyme I is inhibited
-
Fe2+
-
slightly inhibits the native, but not the recombinant enzyme
-
Fe3+
-
enzyme I
-
FeSO4
-
inhibits 26.5% at 0.1 mM, but activates 39.5% at 0.05 mM
Glutaraldehyde
-
does not support enzyme stability, but inhibits the enzyme activity
Guanidine-HCl
-
0.025 M, 65% inhibition of enzyme N, no effect on enzyme I
Guanidine-HCl
-
0.05 M, 60% inhibition
Hg2+
-
1 mM, 35% inhibition
Hg2+
O52224
complete inhibition at 2 mM
methyl 6-amino-6-deoxyglucoside
-
competitive
methyl 6-deoxy-6-fluoro-alpha-D-glucopyranoside
-
very weak, noncompetitive
methyl 6-deoxy-alpha-D-glucopyranoside
-
weak competitive
methyl alpha-D-glucopyranoside
-
-
methyl-alpha-D-glucoside
-
weak competitive
methyl-alpha-D-glucoside
-
competitive
methyl-alpha-D-glucoside
-
50 mM, activates release of D-fructose (sucrase activity), inhibits synthesis of dextran (transferase activity)
Methyl-deoxy-alpha-D-glucopyranoside
-
weak, competitive
Mg2+
-
1 mM, stimulates activity of enzyme N, enzyme I is inhibited
Mg2+
-
slightly inhibits the native, but not the recombinant enzyme
Mg2+
O52224
5.7% inhibition at 2 mM
Mn2+
-
enzyme I and N, strong inhibition
Mn2+
-
enzyme I and II
Mn2+
O52224
41% inhibition at 2 mM
N-Methyl-D-glucamine
-
competitive
Na+
-
slightly inhibits the native, but not the recombinant enzyme
Ni2+
-
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
Ni2+
-
slightly inhibits the native and the recombinant enzyme
Nojirimycin
-
noncompetitive
o-phthalaldehyde
-
inactivation follows pseudo-first order reaction, sucrose and glucose protect
o-phthalaldehyde
-
inactivation
Periodate-oxidized dextrans
-
-
-
phenylmercuric acetate
-
-
phenylmercuric acetate
-
1.0 mM, strong inhibition
pyridoxal-5'-phosphate
-
inactivation
Rb+
O52224
56% inhibition at 2 mM
SDS
-
1.0 mM, strong inhibition
SDS
-
3.5 M; complete inhibition
SDS
-
inhibits the native and the recombinant enzyme
SDS
-
strong inhibition
Sn2+
O52224
34% inhibition at 2 mM
Sucrose
-
the 155000 Da enzyme form is more sensitive to substrate inhibition than the 170000 Da precursor form
Tris
-
competitive with sucrose
Urea
-
0.25 M, enzyme N completely inactivated, enzyme I retains 60% of its activity
Urea
-
enzyme I loses 50% of its activity at 2.4 M urea, enzyme II is inhibited to 50% by 1.7 M urea
Urea
-
8 M, complete inhibition
Urea
-
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+
-
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
Zn2+
-
slightly inhibits the native and the recombinant enzyme
Zn2+
O52224
47% inhibition at 2 mM
ZnSO4
-
inhibits 27% at 0.05 mM and 24.5% at 0.1 mM
MnSO4
-
activates 68% at 0.1 mM, but inhibits at 0.05 mM by 26%
additional information
-
no effect by 7 M urea on enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Dextrans
-
stimulation
Dextrans
-
activity of enzyme N is more effectively stimulated than enzyme I
Dextrans
-
stimulates reducing sugar production 1.3fold and dextran synthesis 9.6fold
Dextrans
-
addition of the B-1299 water-soluble dextan stimulates activity of enzyme I, no effect on activity of enzyme II
Dextrans
-
addition of 0.5% exogenous dextran activates B-1416 enzyme 4.35fold, B-1375 enzyme is activated 2.76fold
methyl-alpha-D-glucoside
-
50 mM, activates release of D-fructose, sucrase activity, inhibits synthesis of dextran, transferase activity
additional information
-
citrate buffer at 0.3 M results in highest activity of wild-type and mutant strains, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
189
-
1'-beta-D-fructofuranosyl alpha-acarbose
-
-
0.0086
-
Sucrose
H1X7X9
pH 5.4, 30C, recombinant enzyme
1.4
-
Sucrose
-
pH 7.0, 30C, mutant R624G
1.6
-
Sucrose
-
pH 7.0, 30C, mutant V630I
1.8
-
Sucrose
C7DT60, -
pH 5.0, 30C, recombinant enzyme
2
-
Sucrose
-
pH 7.0, 30C, wild-type enzyme
3
-
Sucrose
-
enzyme in bulk solution, pH 5.2, 25C
3.1
-
Sucrose
-
pH 7.0, 30C, mutant S628D
3.4
-
Sucrose
-
dextran-QCM-immobilized enzyme, pH 5.2, 25C
3.5
-
Sucrose
-
pH 7.0, 30C, mutant R624G/V630I
5
-
Sucrose
-
pH 7.0, 30C, mutant S628R
7.2
-
Sucrose
-
directly QCM-immobilized enzyme, pH 5.2, 25C
9.8
-
Sucrose
-
pH 7.0, 30C, mutant R624G/V630I/D717A
10.7
-
Sucrose
-
enzyme I
13.1
-
Sucrose
-
glucosyl transfer from sucrose to maltose
13.2
-
Sucrose
-
synthesis of dextran
18
-
Sucrose
-
pH 5.2, 28C, recombinant mutant DRN1
29
-
Sucrose
-
30C, pH 5.2, 170000 Da precursor
34
-
Sucrose
-
30C, pH 5.2, 155000 Da enzyme form
48
-
Sucrose
-
pH 5.2, 28C, recombinant mutant DRN3
77.09
-
Sucrose
-
partially purified wild-type enzyme, pH 4.5, 30C
79
-
Sucrose
-
pH 5.2, 28C, recombinant mutant DRN4
83
-
Sucrose
-
pH 5.2, 28C, recombinant mutant DRN2
88
-
Sucrose
-
pH 5.2, 28C, recombinant wild-type enzyme
101.7
-
Sucrose
-
partially purified mutant enzyme, pH 5.0, 35C
26
-
alpha-D-glucopyranosyl fluoride
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
effect of temperature on KM-value
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Km for dextran T-500 is 1.57 mg/ml in glucosyl transfer from dextran T-500 to maltose. The Km-value for dextran T-500 is 0.019 mg/ml in hydrolysis of dextran T-500
-
additional information
-
additional information
-
kinetic modeling of fed-batch isomaltose production in a bi-enzymic system with immobolized enzymes, overview
-
additional information
-
additional information
-
kinetic analysis of the low-molecular-weight products D-glucose, D-fructose, leucrose and isomaltodextrins formed during the synthesis of dextran by B-512FMC dextransucrase, overview
-
additional information
-
additional information
H1X7X9
rDSRC39-2 shows Michaelis-Menten-type kinetics
-
additional information
-
additional information
-
enzyme deactivation follows fi rst order rate kinetics
-
additional information
-
additional information
-
DSase has a high affinity for dextran as first substrate with Kd of 18 nM, kinetic analysis of 27 MHz quartz crystal microbalance, QCM, plate-immobilized enzyme, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.085
-
Dextran
-
hydrolysis of D-glucose from the non-reducing ends of dextran chains
3.2
-
Dextran
-
transfer of D-glucose from the non-reducing ends of dextran chains to maltose
0.4
-
Sucrose
-
pH 5.2, 28C, recombinant mutant DRN4
0.6
-
Sucrose
-
pH 5.2, 28C, recombinant mutant DRN2
1.6
-
Sucrose
-
pH 7.0, 30C, mutant S628R
1.8
-
Sucrose
-
pH 5.2, 28C, recombinant wild-type enzyme
2.4
-
Sucrose
-
pH 5.2, 28C, recombinant mutant DRN1
2.8
-
Sucrose
-
pH 5.2, 28C, recombinant mutant DRN3
3.1
-
Sucrose
-
directly QCM-immobilized enzyme, pH 5.2, 25C
3.5
-
Sucrose
-
dextran-QCM-immobilized enzyme, pH 5.2, 25C
5.2
-
Sucrose
-
pH 7.0, 30C, mutant R624G
14.5
-
Sucrose
-
pH 7.0, 30C, mutant R624G/V630I
22.4
-
Sucrose
-
pH 7.0, 30C, wild-type enzyme
25.6
-
Sucrose
-
pH 7.0, 30C, mutant R624G/V630I/D717A
29.8
-
Sucrose
-
pH 7.0, 30C, mutant S628D
32.6
-
Sucrose
-
pH 7.0, 30C, mutant V630I
60
-
Sucrose
H1X7X9
pH 5.4, 30C, recombinant enzyme
641
-
Sucrose
-
synthesis of dextran from sucrose
1070
-
Sucrose
-
transfer of D-glucose from sucrose to maltose
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.35
-
1'-beta-D-fructofuranosyl alpha-acarbose
-
-
63
-
2-deoxy-2-fluoro-alpha-D-glucopyranosyl fluoride
-
-
93
-
3-Deoxy-3-fluoro-alpha-D-glucopyranosyl fluoride
-
-
53
-
3-deoxy-3-thio-alpha-D-glucopyranosyl fluoride
-
-
6.6
-
6'-Amino-6'-deoxysucrose
-
sucrose concentration 12.2-97.4 mM
18
-
6'-Amino-6'-deoxysucrose
-
sucrose concentration 1.2-4.9 mM
1.6
-
6-Deoxysucrose
-
-
36
-
alpha-D-glucopyranosyl fluoride
-
-
6.3
-
D-gluconic acid
-
sucrose concentration 1.2-4.9 mM
7.5
-
D-gluconic acid
-
sucrose concentration 12.2-97.4 mM
0.2
-
EDTA
-
sucrose concentration 1.2-4.9 mM
1.1
-
EDTA
-
sucrose concentration 12.2-97.4 mM
9.4
-
glucono-delta-lactone
-
sucrose concentration 12.2-97.4 mM
9.5
-
glucuronic acid
-
sucrose concentration 1.2-4.9 mM
13.9
-
glucuronic acid
-
sucrose concentration 12.2-97.4 mM
400
-
methyl 6-deoxy-6-fluoro-alpha-D-glucopyranoside
-
-
267
-
methyl 6-deoxy-alpha-D-glucopyranoside
-
-
97
-
methyl alpha-D-glucopyranoside
-
-
27.3
-
Methyl-6-amino-6-deoxyglucoside
-
sucrose concentration 1.2-4.9 mM
30
-
N-Methyl-D-glucamine
-
sucrose concentration 12.2-97.4 mM
68.3
-
N-Methyl-D-glucamine
-
sucrose concentration 1.2-4.9 mM
1.5
-
Nojirimycin
-
sucrose concentration 12.2-97.4 mM
12
-
methyl-alpha-D-glucoside
-
sucrose concentration 12.2-97.4 mM
additional information
-
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.012
-
-
purified recombinant mutant DRN4
0.027
-
-
purified recombinant mutant DRN2
0.037
-
-
purified recombinant wild-type DSRB742
0.185
-
-
purified recombinant mutant DRN3
0.287
-
-
purified recombinant mutant DRN1
0.6
-
-
crude enzyme, culture supernatant, pH 5.4, 30C
1.2
-
D2CFL0
purified recombinant chimeric DSXR, dextransucrase activity, pH 5.8, 28C
13.9
-
-
purified recombinant wild-type DSRBCB4
18
-
-
PEG 400-purified enzyme, pH 5.4, 30C
23
-
-
purified enzyme, pH 5.4, 30C
23.8
-
-
enzyme purified by the phase-partition using PEG 400
31.3
-
-
partially purified wild-type enzyme, pH 4.5, 30C
35.3
-
-
purified native enzyme
36
-
-
PEG 1500-purified enzyme, pH 5.4, 30C
42.1
-
-
enzyme purified by the phase-partition using PEG 600
54
-
-
cellobio-oligosaccharides synthesis
97.37
-
-
recombinant enzyme in crude enzyme extract
126
-
C7DT60, -
purified recombinant enzyme
141
-
-
155000 Da enzyme form
145
-
-
170000 Da precursor
173.2
-
-
partially purified mutant enzyme, pH 5.0, 35C
250
-
-
enzyme II
686
-
A9ZRX3
purified recombinant enzyme, in presence of 0.1 mM Ca2+
additional information
-
-
-
additional information
-
-
-
additional information
-
-
dextran binding capacity of recombinant wild-type and truncated mutant C-terminal domain GBD-7, overview
additional information
-
-
substrate specificity of recombinant enzymes, overview
additional information
-
-
mutant activities
additional information
-
-
Vmax with 1'-beta-D-fructofuranosyl alpha-acarbose is 0.0085 mM/min*mg protein
additional information
-
D2CFL0
120.1 U/ml, recombinant dextransucrase activity of recombinant DSXR chimeric enzyme, pH 5.8, 28C
additional information
-
-
21 U/ml, pH 5.2, 30C; 89 U/ml, pH 5.2, 30C
additional information
-
-
dextransucrae activity in different strains, i.e. KIBGE IB-06, KIBGE IB-07, KIBGE IB-08, KIBGE IB-09, KIBGE IB-10, KIBGE IB-11, KIBGE IB-12, KIBGE IB-13, KIBGE IB-19, and KIBGE IB-22, all isolated from different sources, phylogenetic tree, overview. Strain KIBGE IB-22 exhibits the highest enzyme activity
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
wild-type enzyme
5
-
-
soluble and immobilized enzyme
5
-
C7DT60, -
-
5
-
-
mutant enzyme
5.2
-
-
free and immobilized
5.2
-
-
cellobio-oligosaccharides synthesis
5.2
-
O52224
recombinant wild-type and mutant fusion enzymes
5.2
-
B9UNL6
-
5.4
-
Penicillium aculeatum
-
assay at
5.4
-
-
native and recombinant enzyme
5.4
-
-
recombinant enzyme
5.4
-
H1X7X9
-
5.4
-
D5FS20
assay at
5.5
6.9
-
enzyme II
5.5
-
A9ZRX3
-
5.5
-
B1N0B6, -
recombinant enzyme
6.3
6.5
-
enzyme I
6.5
-
-
assay at
7
-
-
assay at
7.4
8.1
Q2I2N5
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
6.8
C7DT60, -
activity range of the recombinant enzyme, profile, overview
3.5
8
B9UNL6
activity range
3.5
8
A9ZRX3
activity range, dependent on the buffer system
4
7
-
pH 4.0: about 40% of maximal activity, pH 7.0: about 60% of maximal activity
4
7.5
-
mutant enzyme, maximal activity at pH 5.0, 25% of maximal activity at pH 4.0, and 7.5% of maximal activity at pH 7.5
4.5
6.5
-
activity range analyzed
4.6
5.6
-
measurement range, 85% of maximal activity at pH 4.6
5
6.4
D2CFL0
highly reduced activity below pH 5.0 and above pH 6.4
5
7
-
about 40% of maximal activity at pH 5.0 and pH 7.0
additional information
-
-
no enzyme activity at neutral pH by the wild-type strain
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
30
-
recombinant enzyme
25
-
Q2I2N5
assay at
28
-
O52224
assay at
28
-
D2CFL0
assay at
30
-
-
free and immobilized
30
-
-
B-1375 enzyme with dextran
30
-
-
cellobio-oligosaccharides synthesis
30
-
-
assay at
30
-
Penicillium aculeatum
-
assay at
30
-
-
recombinant enzyme
30
-
B9UNL6
-
30
-
C7DT60, -
-
30
-
-
wild-type enzyme
30
-
-
assay at
30
-
D5FS20
assay at
30
-
B1N0B6, -
recombinant enzyme
35
40
-
enzyme II
35
40
H1X7X9
-
35
-
-
enzyme I is stable for 10 min
35
-
-
B-1416 enzyme with and without dextran, B-1375 enzyme without dextran
35
-
-
soluble and immobilized enzyme
35
-
A9ZRX3
-
35
-
-
mutant enzyme
40
-
-
native enzyme
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
45
-
mutant enzyme, activity range
8
36
-
8C: 22% of activity maximum, 36C: 30% of activity maximum
10
42
C7DT60, -
activity range of the recombinant enzyme, profile, overview
15
30
-
62% of maximal activity at 15C
15
40
-
wild-type enzyme, activity range
20
40
-
20C: about 60% of maximal activity, 40C: about 50% of maximal activity
20
50
B9UNL6
62% at 20C, activity range
22
30
-
measurement range
25
35
-
activity range analyzed
37
51
-
80% of activity maximum at 37C and 51C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
DsrP, sequence calculation
4.6
-
H1X7X9
sequence calculation
5.26
-
D5FS20
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
dextransucrase is produced in a fermentation medium using cashew apple, Anacardium occidentale, juice as substrate, method evaluation, overview
Manually annotated by BRENDA team
-
the dextransucrase from the organism shows maximum production with addition of 0.005% CaCl2, production method optimization, overview
Manually annotated by BRENDA team
-
optimization of culture conditions for dextransucrase production, optimum in a shaking flask culture at pH 5.4, 25C, overview
Manually annotated by BRENDA team
-
the enzyme production and activity is highest at pH 6.5 and 25C, high stability at room temperature of 30C, condition evaluation, overview
Manually annotated by BRENDA team
Leuconostoc citreum NRRL B-742
-
the enzyme production and activity is highest at pH 6.5 and 25C, high stability at room temperature of 30C, condition evaluation, overview
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B-512F
-
dextransucrase is produced in a fermentation medium using cashew apple, Anacardium occidentale, juice as substrate, method evaluation, overview
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides PCSIR-4
-
the dextransucrase from the organism shows maximum production with addition of 0.005% CaCl2, production method optimization, overview
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B-512F
-
-
-
Manually annotated by BRENDA team
Penicillium aculeatum
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides IAM 1046, Leuconostoc mesenteroides NRRL B-1299, Leuconostoc mesenteroides NRRl B-512(F), Leuconostoc mesenteroides Sikhae, Streptococcus mutans 6715, Streptococcus mutans HS6
-
-
-
Manually annotated by BRENDA team
additional information
-
review of cultural conditions and nutritional requirements for the production of dextransucrase
Manually annotated by BRENDA team
additional information
-
optimizing of dextransucrase production
Manually annotated by BRENDA team
additional information
-
optimization of enzyme production in strain NRRL B-640. Sucrose, K2HPO4, yeast extract and beef extract show above 90% confidence levels for dextransucrase production and are considered as significant factors for optimization, modelling, overview
Manually annotated by BRENDA team
additional information
-
correlation of cell growth wilth enzyme activity, overview
Manually annotated by BRENDA team
additional information
-
correlation of cell growth with enzyme activity, overview
Manually annotated by BRENDA team
additional information
-
optimization of the medium and fermentation for the enzyme production of by strain NRRL B-1146, calculations and statistical analysis, overview. Maximized activity is 6.4 U/ml
Manually annotated by BRENDA team
additional information
A9ZRX3
induced recombinant enzyme production is 330fold higher at 15C compared to 37C
Manually annotated by BRENDA team
additional information
Leuconostoc citreum HJ-P4
-
induced recombinant enzyme production is 330fold higher at 15C compared to 37C
-
Manually annotated by BRENDA team
additional information
Leuconostoc mesenteroides FT 045 B
-
optimizing of dextransucrase production
-
Manually annotated by BRENDA team
additional information
Leuconostoc mesenteroides NRRL B-512F
-
review of cultural conditions and nutritional requirements for the production of dextransucrase
-
Manually annotated by BRENDA team
additional information
Leuconostoc mesenteroides NRRL B-640
-
optimization of enzyme production in strain NRRL B-640. Sucrose, K2HPO4, yeast extract and beef extract show above 90% confidence levels for dextransucrase production and are considered as significant factors for optimization, modelling, overview
-
Manually annotated by BRENDA team
additional information
Leuconostoc mesenteroides subsp. dextranicum NRRL B-1146
-
optimization of the medium and fermentation for the enzyme production of by strain NRRL B-1146, calculations and statistical analysis, overview. Maximized activity is 6.4 U/ml
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
DsrP is anchoring to the cell wall
Manually annotated by BRENDA team
D5FS20
DSR-F C-terminal glucan binding domain might be involved in enzyme anchoring at the cell wall surface
Manually annotated by BRENDA team
Leuconostoc citreum B/110-1-2
-
DSR-F C-terminal glucan binding domain might be involved in enzyme anchoring at the cell wall surface
-
Manually annotated by BRENDA team
Penicillium aculeatum
-
-
-
Manually annotated by BRENDA team
-
DsrP is anchoring to the cell wall
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
Leuconostoc citreum B/110-1-2
-
-
-
-
Manually annotated by BRENDA team
Leuconostoc citreum KACC 91035
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides 0326, Leuconostoc mesenteroides B-512FMC, Leuconostoc mesenteroides FT045B, Leuconostoc mesenteroides IBT-PQ, Leuconostoc mesenteroides KIBGE IB-22, Leuconostoc mesenteroides Lm 28, Leuconostoc mesenteroides NRRL B-1299
-
-
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B-512F
-
;
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRl B-512(F), Leuconostoc mesenteroides NRRL B-640
-
-
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides subsp. dextranicum NRRL B-1146
-
; the enzyme is secreted
-
-
Manually annotated by BRENDA team
Leuconostoc citreum B/110-1-2
-
-
-
Manually annotated by BRENDA team
Weissella cibaria LBAE K39, Weissella confusa LBAE C39-2
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
65000
-
-
enzyme I and II, disc gel electrophoresis
94000
-
-
gel filtration
100000
-
-
about
100000
-
-
enzyme III, disc gel electrophoresis
130000
133000
-
disc gel electrophoresis
160000
180000
D5FS20
intracellular dextransucrase 1 and extracellular dextransucrase
180000
-
-
native PAGE
220000
240000
D5FS20
intracellular dextransucrse 2
additional information
-
-
the enzyme has two major forms: MW 177000 Da and MW 158000 Da
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 48000, enzyme I, SDS-PAGE
?
-
x * 65000, enzyme II, SDS-PAGE
?
-
x * 170000, SDS-PAGE
?
-
x * 184000, the native enzyme is believed to be a trimer of two 63000 Da and one 59000 Da monomers, SDS-PAGE
?
-
x * 168600, calculation from nucleotide sequence; x * 170000, nondenaturing SDS-PAGE
?
-
x * 180000, SDS-PAGE
?
Q2I2N5
x * 170000, SDS-PAGE
?
-
x * 167570, recombinant His6-tagged DsrX, sequence calculation
?
-
x * 160586, DsrP, sequence calculation
?
O52224
x * 240000, recombinant fusion protein DXSR, SDS-PAGE
?
B9UNL6
x * 161998, sequence calculation
?
C7DT60, -
x * 165000, recombinant enzyme, SDS-PAGE
?
-
x * 170000, recombinant enzyme, SDS-PAGE
?
-
x * 221000, partially purified enzyme, SDS-PAGE
?
D5FS20
x * 170448, DSRF, sequence calculation
?
B1N0B6, -
x * 160000, recombinant enzyme, SDS-PAGE, x * 167000, about, sequence calculation
?
Leuconostoc citreum B/110-1-2
-
x * 170448, DSRF, sequence calculation
-
?
-
x * 160000, recombinant enzyme, SDS-PAGE, x * 167000, about, sequence calculation
-
?
Leuconostoc lactis EG001
-
x * 165000, recombinant enzyme, SDS-PAGE
-
?
Leuconostoc mesenteroides 0326
-
x * 170000, SDS-PAGE
-
?
Leuconostoc mesenteroides B-742CB
-
x * 168600, calculation from nucleotide sequence; x * 170000, nondenaturing SDS-PAGE
-
?
Leuconostoc mesenteroides CGMCC 1.544
-
x * 167570, recombinant His6-tagged DsrX, sequence calculation
-
?
Leuconostoc mesenteroides KIBGE IB-22
-
x * 221000, partially purified enzyme, SDS-PAGE
-
?
Leuconostoc mesenteroides NRRL B-1299
-
x * 48000, enzyme I, SDS-PAGE
-
?
Leuconostoc mesenteroides NRRl B-512(F)
-
x * 65000, enzyme II, SDS-PAGE
-
?
Leuconostoc mesenteroides NRRL B-640
-
x * 180000, SDS-PAGE
-
?
Streptococcus mutans HS6
-
x * 170000, SDS-PAGE
-
dimer
-
2 * 64000-68000, SDS-PAGE after alkaline treatment, pH 10.5
dimer
Leuconostoc mesenteroides B-1375, Leuconostoc mesenteroides NRRL B-1416
-
2 * 64000-68000, SDS-PAGE after alkaline treatment, pH 10.5
-
monomer
-
1 * 69000, enzyme I, SDS-PAGE; 1 * 79000, enzyme II, SDS-PAGE
monomer
Leuconostoc mesenteroides NRRL B-1299
-
1 * 69000, enzyme I, SDS-PAGE; 1 * 79000, enzyme II, SDS-PAGE
-
additional information
-
the purified native enzyme shows multiple molecular forms on SDS-PAGE, however the same sample shows a single band on non-denaturing native-PAGE
additional information
-
modelling of the C-terminal domain
additional information
D5FS20
the C-terminus, also named glucan binding domain, GBD, begins at position 1171 and is 358 residues in size, the DSR-F C-terminal GBD also contains the unusual repeats named APY 2 times
additional information
Leuconostoc citreum B/110-1-2
-
the C-terminus, also named glucan binding domain, GBD, begins at position 1171 and is 358 residues in size, the DSR-F C-terminal GBD also contains the unusual repeats named APY 2 times
-
additional information
Leuconostoc mesenteroides NRRL B-640
-
the purified native enzyme shows multiple molecular forms on SDS-PAGE, however the same sample shows a single band on non-denaturing native-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
17% carbohydrate
no glycoprotein
-
enzyme is not a glycoprotein
proteolytic modification
-
change of molecular mass of the enzymeincubated for 60 days at room temperature. After storage, the 170000 Da dextransucrase precursor decreases in concentration as a consequence of proteolysis. Initially a mixture of the precursor and a 155000 Da form are found. After 60 days of incubation, the 155000 form is further digested to lower molecular mass species, particularly a 129000 Da form, which still retains dextransucrase activity
proteolytic modification
Leuconostoc mesenteroides B-512F
-
change of molecular mass of the enzymeincubated for 60 days at room temperature. After storage, the 170000 Da dextransucrase precursor decreases in concentration as a consequence of proteolysis. Initially a mixture of the precursor and a 155000 Da form are found. After 60 days of incubation, the 155000 form is further digested to lower molecular mass species, particularly a 129000 Da form, which still retains dextransucrase activity
-
glycoprotein
Leuconostoc mesenteroides Birmingham
-
-
-
glycoprotein
Leuconostoc mesenteroides NRRl B-512(F)
-
17% carbohydrate
-
no glycoprotein
Leuconostoc mesenteroides NRRL B-512F
-
enzyme is not a glycoprotein
-
glycoprotein
Leuconostoc mesenteroides Sikhae
-
-
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
5
-
purified recombinant enzyme, quite stable
4
7.5
B1N0B6, -
purified recombinant enzyme, stable
4
8.5
A9ZRX3
LcDS is very stable within that pH range
4
-
-
B-512(F) enzyme unstable, Sikhae enzyme more stable
4.5
5.5
-
the crude enzyme is stable at 30 C for 30 h at pH ranging from 4.5 to 5.5, partially purified enzyme is stable in non-fermented cashew apple juice at pH 5.0 for 96 h at 30 C, overview
4.6
7.2
-
4C, 24 h, 50% loss of activity at pH 4.6 and 7.2, enzyme II
4.7
8.5
-
4C, 24 h, 50% loss of activity at pH 4.7 and 8.5, enzyme I
5
6
-
80% remaining activity, rapid decrease outside this range
5
6
O52224
partially purified recombinant wild-type DSRBCB4, stable with above 80% of maximal activity
5
6
B9UNL6
over 80% of maximal activity within this range, but the activity decreases rapidly outside this pH range
5
6.4
O52224
partially purified recombinant fusion enzyme DXSR, stable with above 80% of maximal activity
5
6.5
-
stability optimum, free enzyme
5
7
-
recombinant enzyme, quite stable
5.2
8.5
-
4C, 0.1% bovine serum albumin, stable for 24 h, rapid inactivation below pH 5.0
5.2
-
-
stability optimum, immobilized enzyme
5.3
5.8
-
4C, 24 h, enzyme II stable
5.4
-
-
30C, native enzyme loses 90% of its inital activity in only 2 h
5.5
-
-
4C, 24 h, enzyme N is stable
6
9
-
4C, stable at 4C for 24 h, 4 mg/ml dextrans
6
-
-
4C, 24 h, enzyme I is stable
6.2
6.9
-
4C, 24 h, enzyme I stable
7
9
-
4C, stable for 24 h, without dextran in solution
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
60
-
the native DsrX shows higher stability than the recombinant DsrX at the temperature range from 4C to 60C for 2 h, native enzyme shows 84% remaining activity at 40C after 2 h, while recombinant enzyme shows only 3.1%
10
30
-
purified enzyme, stable at, rapid loss of activity above. Loss of 65% activity within 20 h at 30C without added stabilizer, in presence of Tween 80 the enzyme loses only 8% activity. Loss of 92% activity at 30C within 4 days
15
37
A9ZRX3
stable, rapid decrease in activity above 37C
20
30
H1X7X9
purified recombinant enzyme, in 20 mM sodium acetate, pH 5.4, 30 min, stable, rapid loss of activity above 30C
25
-
-
immobilized enzyme, 60 min, maximally stable
28
-
O52224
partially purified recombinant fusion enzyme DXSR, stable
30
-
-
pH 5.4, native enzyme loses 90% of its inital activity in only 2 h, immobilization on Eupergit C 250L significantly stabilizes dextransucrase. Despite a fast partial inactivation in the first 2 h, the enzyme immobilized on Eupergit C 250L maintains more than 40% of the initial activity over the following 2 days, the enzyme immobilized on Eupergit C maintains about 15% of the initial activity after 1 day
30
-
-
the crude enzyme is stable at 30 C for 30 h at pH ranging from 4.5 to 5.5, partially purified enzyme is stable in non-fermented cashew apple juice at pH 5.0 for 96 h at 30 C, overview
30
-
-
240 min, crude enzyme, loss of 26% activity
35
-
-
10 min, enzyme I and N stable
35
-
-
10 min, enzyme I stable
35
-
-
B-1375 enzyme stable
35
-
-
half-life: 137 min
35
-
-
instable above
35
-
B1N0B6, -
purified recombinant enzyme, stable up to
40
-
-
10 min, 80% loss of activity without dextran, 30% loss of activity with addition of dextran
40
-
-
B-1416 enzyme is stable up to
40
-
-
240 min, crude enzyme, loss of 86% activity
45
-
-
10 min, 80% loss of activity, enzyme I
45
-
-
20 min, substantial loss of activity above
45
-
-
40 min, recombinant strains, inactivation
50
-
-
240 min, crude enzyme, inactivation
additional information
-
-
stability of immobilized enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stability of crude dextransucrase from Leuconostoc citreum strain B-742 in synthetic and in cashew apple juice culture broth, evaluation, overview
-
Ca2+ significantly stabilizes the soluble enzyme
-
Ca2+ stabilizes the enzyme
-
dextran T10 stabilizes
-
enzyme deactivation follows first order rate kinetics
-
glutaraldehyde does not support the stability, rather it inhibits the enzyme activity, also glycerol, PEG 8000, and dextran (500 kDa) do not stabilize the enzyme
-
maximal stabilization of soluble enzyme by 5 mM Ca2+
-
native enzyme loses 90% of its inital activity in only 2 h at pH 5.4, 30C, immobilization on Eupergit C 250L significantly stabilizes dextransucrase. Despite a fast partial inactivation in the first 2 h, the enzyme immobilized on Eupergit C 250L maintains more than 40% of the initial activity over the following 2 days, the enzyme immobilized on Eupergit C maintains about 15% of the initial activity after 1 day
-
stability is significantly increased by 33% glycerol and 0.1% bovine serum albumin
-
the best conditions for the enzyme are 50% v/v dimethyl sulfoxide and immobilization in alginate beads
-
the enzyme can be stabilized by high-molecular-weight dextran, polyethyleneglycol or nonionic detergents such as Tween 80
-
Tween 80 stabilizes the purified enzyme, maximally at 30C
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acetone
-
at 50%, reduces the enzyme activity by 94%
acetonitrile
-
at 20%, reduces the enzyme activity by 80%
dimethyl sulfoxide
-
the best conditions for the enzyme are 50% v/v dimethyl sulfoxide and immobilization in alginate beads
DMSO
-
at 90%, reduces the enzyme activity by 91%
Ethanol
-
at 50%, reduces the enzyme activity by 80%
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
25C, purified recombinant enzyme, 59% activity remaining after 4 days
-
4C, purified recombinant enzyme, 50% activity remaining after 7 weeks
-
25C, crude enzyme in cashew apple juice, pH 6.5, 48 h , quite stable
-
-20C, purified enzyme, loss of 25% activity within 14 days at 30C
-
4C, 0.1% bovine serum albumin, pH 5.2-8.5, stable for 24 h
-
4C, pH 6.0-9.0, 4 mg/ml dextran, 24 h stable, without dextran the stable range is narrowed to pH 7.0-9.0
-
4C, purified enzyme, loss of 92% activity within 4 days at 30C
-
in a deep-freezer, 33% glycerol, 0.1% bovine serum albumin, less than 20% loss of activity after several months
-
on standing at 4C for 30 days the native enzyme is dissociated into three inactive proteins
-
storage stability decreased by addition of dextranase
-
4C or -70C, stable during extended storage
-
4C, purified recombinant enzyme, in 20 mM sodium acetate, pH 5.4, about 10% activity loss after 6 days, and about 35% activity loss after 20 days
H1X7X9
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme 11.4fold from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation and nickel affinity chromatography
-
extracellular enzyme from kimchi by anion exchange chromatography
-
recombinant His-tagged glucansucrase 2.4fold from Escherichia coli by nickel affinity chromatography
C7DT60, -
2 forms: I and II
O52224
2 forms: I and II; NRRL B-1299
-
2 forms: I and N, enzyme I is gradually converted into enzyme N upon ageing, conversion is stimulated in the presence of NaCl; NRRL B-1299
-
2 forms: MW 177000 and MW 158000; NRRL B-512(F)
-
dextransucrase II; NRRL B-512(F)
-
multiple forms: I, II and III; NRRL B-512(F)
-
native enzyme 61fold from strain NRRL B-640 by repeated polyethylene glycol fractionation and gel filtration; native enzyme from strain nRRL-B 640 by polyethylene glycol fractionation and gel filtration, with 23-40fold purification by 10% w/v PEG 1500 and 35-60fold of total purification, method optimization, overview
-
native enzyme by PEG 1500 fractionation
-
native enzyme partially by ammonium sulfate fractionation and dialysis, recombinant N-terminally His6-tagged DsrX from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
native enzyme partially from strain PCSIR-4 2.5fold by ethanol
-
NRRL B-512(F); partial; Sikhae
-
recombiant His-tagged enzyme from Escherichia coli by metal affinity chromatography. Various methods such as precipitation by ammonium sulphate, ethanol, or polyethylene glycol, phase partitioning, ultrafiltration and chromatography are used to purify the enzyme, detailed overview. Purification of dextransucrase is rendered difficult by the presence of viscous dextran in the medium
-
recombiant His-tagged wild-type and mutant enzymes about 6fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant
Q9L466
recombinant enzyme
-
recombinant thioredoxin-His-tagged wild-type and truncated mutant C-terminal domain GBD-7 about 6fold by nickel affinity chromatography
-
recombinant wild-type and DRN1-DRN4 mutant enzymes from Escherichia coli by nickel affinity chromatography
-
recombinant wild-type DSRBCB4 and mutant fusion enzyme DXSR, partially from Escherichia coli by anion exchange chromatography and ultrafiltration
O52224
wild-type and mutant extracellular enzymes 11.35fold and 10.27fold, respectively, by PEG 4000 fractionation
-
wild-type native DsrP and DsrE from strains IBT-PQ and NRRL B-1299
-
native extracellular enzyme by a single-step fractionation using polyethylene glycols of different molecular mass, 31fold purification by PEG 400 and 45fold purification by PEG 1500
-
recombinant enzyme 5.1fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
B9UNL6
recombinant His-tagged DSRC39-2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatogaphy
H1X7X9
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene dexYG, overexpression in Escherichia coli strain BL21(DE3)
-
enzyme expression in the periplasmic space of seven different Escherichia coli strains with inducer molecules such as lactose or IPTG. Escherichia coli strain BL21-CodonPlus(DE3)-RIL exhibits the highest enzyme activity with lactose, method optimization with respect to culture conditions results in a 12fold increase in activity at 17C and 7.5 mM lactose
B1N0B6, -
gene dsrF, DNA and amino acid sequence determination and analysis, sequence comparison, expression of DSR-F in Escherichia coli strain JM109
D5FS20
gene LcDS, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain MC1061, expression in Escherichia coli strain BL21
A9ZRX3
genes HJ-P4 and HJ-P5, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
-
two ORFs coding for strain B/110-1-2 dextransucrases, DNA and amino acid sequence determination and analysis, sequence comparisons
D5FS20
DNA and amino acid sequence determination and analysis, sequence comparisons, expression of His-tagged glucansucrase in Escherichia coli
C7DT60, -
DSR-S protein is fused to a thioredoxin tag at the N-terminal extremity, and a 6*His tag at the C-terminal end and expressed in Escherichia coli
-
expressed in Bacillus megaterium strain MS941 and strain WH320. At high cell density conditions and low growth rates MS941, in contrast to WH320, does not maintain a vegetative growth which is essential for the expression of the foreign dsrS gene by using the xylA promoter. It is conceivable that applications of a promoter which is highly active under nutrient-limited cultivation conditions is necessary, at least for MS941, for the overexpression of recombinant genes in such Bacillus megaterium fed-batch cultivation process
-
expression in Escherichia coli
-
expression in Escherichia coli. Native enzyme produces mainly 6-linked glucopyranosylresidues, while Escherichia coli recombinant enzyme produces a glucan consisting of 70% 6-linked glucopyranosyl residues and 15% 3,6-glucopyranosyl residues
-
expression in the industrially relevant lactic acid bacterium Lactococcus lactis
O52224
expression of the His-tagged enzyme from strain B-512F in Escherichia coli
-
expression of the truncated mutant enzyme, B-512FMC dextransucrase, in Escherichia coli
-
expression of thioredoxin-His-tagged wild-type and trunacted mutant C-terminal domain GBD-7
-
expression of wild-type enzyme DSRBCB4 and of mutant fusion enzyme of dextransucrase and dextranase, DXSR, in Escherichia coli
O52224
gene dexYG, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
Q2I2N5
gene dexYG, expression in Escherichia coli strain BL21(DE3)
-
gene dexYG, lactose-inducible expresssion of the enzyme in Escherichia coli strain BL21(DE3). Method optimization, highest activity at 25C and 1% lactose, overview
-
gene DSRB742, expression of wild-type and DRN1-DRN4 mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
-
gene dsrBCB4, DNA and amino acid sequence determination and analysis, sequence comparisons, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene dsrP, DNA and amino acid sequence determination and analysis, the enzyme sequence possess seven repeat units in the N-terminal region as well as five cell wall binding repeats in the C-terminal region, expression in Escherichia coli
-
gene dsrX, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain DH5alpha, expressed as a N-terminal His6-tagged protein Escherichia coli strain BL21(DE3), optimization of the recombinant expression system
-
gene dsxr, the recombinant chimeric dsxr encodes dextranase-dextransucrase, DXSR, is sequentially composed of the dextransucrase-encoding gene dsrBCB4 and the gene dex2, encoding the dextranase from Arthrobacter oxidans, UniProt ID A9UKG4, expression in Escherichia coli strain BL21(DE3)pLysS
D2CFL0
genes HJ-S7 and HJ-S13, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
-
recombinantly produced in Bacillus megaterium and exported into the growth medium. For this purpose a plasmid-based xylose-inducible gene expression system is optimized via introduction of a multiple cloning site and an encoded optimal Bacillus megaterium ribosome binding site
-
truncated forms of dsrE are cloned and expressed in Escherichia coli. The catalytic domain CD1 is specific for the synthesis of alpha-1,6 glucosidic bonds and CD2 only catalyzes the formation of alpha-1,2 linkage
Q8G9Q2
gene gtfR, expression of wild-type and mutant enzymes in Escherichia coli strain XL10-Gold
-
DNA and amino acid sequence determination and analysis
-
gene dsrWC, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain Top10F' and expression in Escherichia coli strain BL21(DE3)
B9UNL6
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged DSRC39-2 in Escherichia coli strain BL21(DE3)
H1X7X9
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme is induced by sucrose
-
the enzyme is induced by sucrose
Leuconostoc citreum NRRL B-742
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
N1134S/N1135E/S1136V
-
mutation converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme
P1026V/I1029V/N1134S/N1135E/S1136V
-
mutant enzyme synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
N1134S/N1135E/S1136V
Lactobacillus reuteri 121
-
mutation converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme
-
D511N
-
mutant protein shows no dextran formation
D513N
-
mutant enzyme shows reduced dextran formation
D530N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D533A
-
mutant enzyme with 2.3% of wild-type activity
D533N
-
complete suppression of dextran synthesis activity
D536A
-
mutant enzyme with 40.8% of wild-type activity
D536N
-
complete suppression of dextran synthesis activity
D551N
-
mutant protein shows no dextran formation
D641N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E568Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
F196S
-
site-directed mutagenesis, the mutant DRN1 shows a higher expression level in Escherichia coli and increased activity compared to DSRB742
H161R
-
mutant protein retains a very low dextran synthesis activity
H643A
-
complete suppression of dextran synthesis activity
H643N
-
complete suppression of dextran synthesis activity
P980T
-
site-directed mutagenesis, the mutant DRN4 shows a lower expression level in Escherichia coli compared to DSRB742
S455K
-
produces a glucan with 85% 6-linked glucopyranosyl residues
T350K
-
produces a glucan with 85% 6-linked glucopyranosyl residues
T350K/S455K
-
mutant enzyme exhibits a 10fold increase in glucosyltransferase activity over those of the parental DSRS-His6 and its T350K and S455K mutants; produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
D530N
Leuconostoc mesenteroides B-1299CB4
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
D641N
Leuconostoc mesenteroides B-1299CB4
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
D533A
Leuconostoc mesenteroides B-742CB
-
mutant enzyme with 2.3% of wild-type activity
-
D533N
Leuconostoc mesenteroides B-742CB
-
complete suppression of dextran synthesis activity
-
D536A
Leuconostoc mesenteroides B-742CB
-
mutant enzyme with 40.8% of wild-type activity
-
D536N
Leuconostoc mesenteroides B-742CB
-
complete suppression of dextran synthesis activity
-
D511N
Leuconostoc mesenteroides NRRl B-512(F)
-
mutant protein shows no dextran formation
-
D513N
Leuconostoc mesenteroides NRRl B-512(F)
-
mutant enzyme shows reduced dextran formation
-
D551N
Leuconostoc mesenteroides NRRl B-512(F)
-
mutant protein shows no dextran formation
-
S455K
Leuconostoc mesenteroides NRRL B-512F
-
produces a glucan with 85% 6-linked glucopyranosyl residues
-
T350K
Leuconostoc mesenteroides NRRL B-512F
-
produces a glucan with 85% 6-linked glucopyranosyl residues
-
N1134S
-
the mutation in GTFA results in a drastically changed specificity but no major changes in polymer versus oligosaccharide formation
R624G
-
the R624G mutations near the transition state stabilizer is involved in the phenotype which exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages
R624G/V630I
-
the mutant exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages, both mutations near the transition state stabilizer, R624G and V630I, are contributing to this alteration
R624G/V630I/D717A
-
the mutant exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages, both mutations near the transition state stabilizer, R624G and V630I, are contributing to this alteration
S628D
-
saturation mutagenesis, the mutation guides the reaction toward the synthesis of short chain oligosaccharides with a drastically increased yield of 47% isomaltose or 64% leucrose
S628R
-
saturation mutagenesis, the mutation guides the reaction toward the synthesis of short chain oligosaccharides with a drastically increased yield of 47% isomaltose or 64% leucrose
V630I
-
the V630I mutations near the transition state stabilizer is involved in the phenotype which exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages
P1026V/I1029V/N1134S/N1135E/S1136V
Lactobacillus reuteri 121
-
mutant enzyme synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
-
additional information
D5FS20
construction of a truncated active variant DSR-F-DELTASPDELTAGBD of 1251 amino acids, with a molecular mass of 145544 Da, the mutant lacks the sequence encoding signal peptide and a portion of the C-terminal domain, i.e. the glucan binding domain
additional information
Leuconostoc citreum B/110-1-2
-
construction of a truncated active variant DSR-F-DELTASPDELTAGBD of 1251 amino acids, with a molecular mass of 145544 Da, the mutant lacks the sequence encoding signal peptide and a portion of the C-terminal domain, i.e. the glucan binding domain
-
K395T
-
site-directed mutagenesis, the mutant DRN3 shows a higher expression level in Escherichia coli and increased activity compared to DSRB742
additional information
Q9L466
directed evolution of a B-742CB dextransucrase gene (dsrB742) that elaborates a novel extracellular dextransucrase gene (dsrB742ck) after ultrasoft X-ray irradiation, producing a dextransucrase of increased activity and synthesis of a highly branched dextran
additional information
-
rational deletions of the signal peptide, the beginning of the variable region and the last four repeats of the C-terminal end cause no loss of activity. The new variant successfully purified is remarkably stable. With a kcat of 584 per s, it is the most efficient recombinant glucansucrase described to date. The synthesized polymer possesses more than 95% of alpha-1,6 links, like the dextran produced by the native enzyme
additional information
-
co-immobilization of dextransucrase and dextranase on calcium alginate for the facilitated synthesis of isomalto-oligosaccharides, reaction scheme, method optimization, and modeling, overview
additional information
-
construction of engineered enzyme variants for production of isomalto-oligosaccharides and dextrans of controlled molecular weight of about 10-40 kDa in a one-step process, method optimization, overview
additional information
-
construction of fourteen truncated forms of strain NRRL B512-F dextransucrase by N-, C- or N- plus C-terminal domain truncations, dextran binding properties of mutant enzymes, overview
additional information
-
the partially purified native enzyme from strain PCSIR-4 is immobilized on alginate for application in the production of dextran from sucrose, method optimization, overview
additional information
-
construction of constitutive mutants by chemical mutagenesis using ethyl methane sulfonate in strain Lm M281, overview
additional information
-
the enzyme is usable in the production of isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, alteration of the ratio of sucrose to maltose and the amount of each sugar, overview
additional information
-
construction of a truncated mutant of enzyme B-512F, the mutant shows sigmoidal shaped curves when the initial velocities are plotted against the concentration of added dextran. The increase in the reaction rate and the decrease in the sigmoidal curve with increasing dextran concentrations indicate that dextran binds at a noncatalytic or allosteric site to give a more active enzyme
additional information
O52224
construction of a fusion enzyme DXSR of dextransucrase, encoded by gene dsrBCB4, and dextranase, encoded by gene dex2, for one-step synthesis of isomalto-oligosaccharides. DXSR shows 150% increased endo-dextranase activity and 98% decreased dextransucrase activity. The engineered recombinant mutant enzyme DXSR, a fusion of dextransucrase and dextranase, produces linear isomalto-oligosaccharides with DP2-DP10 using sucrose as a sole substrate. DXSR gives 30fold higher production of isomalto-oligosaccharides than that of an equal activity mixture of the two enzymes such as dextranase and dextransucrase
additional information
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optimization of culture conditions for high-level lactose-inducible expression of Leuconostoc mesenteroides dextransucrase in recombinant Escherichia coli strain BL 21(DE3), overview. Maximal activity of 60.18 U/ml from a fed-batch culture at 5 g/l lactose, added at an OD600 of 3.0, at 25C for 7 h
additional information
D2CFL0
construction and optimal expression of a fusion enzyme DSXR having dextransucrase and dextranase activities, for optimization of protein expression, response surface methodology is used
additional information
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generation of diverse mutant enzymes using UV irradiation random mutagensis, mutant screeening, overview. Mutant KIBGE IB-22M20 exhibits 6.75fold increased dextransucrase activity compared to the wild-type enzyme
additional information
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immobilisation of the enzyme directly on a 27 MHz quartz crystal microbalance, QCM, plate, or on a dextran-acceptor-QCM plate, method evaluation and binding kinetics,overview. The enzymatic activity of DSase is not affected by immobilization, possibly due to the use of a long PEG spacer group. Typical frequency changes of the dextran-immobilized QCM as a function of time in response to the addition of DSase and sucrose substrate in 50 mM acetate buffer pH 5.2, 150 mM NaCl, and 1 mM CaCl2 at 25C
Y346N
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site-directed mutagenesis, the mutant DRN2 shows a lower expression level in Escherichia coli compared to DSRB742
additional information
Leuconostoc mesenteroides 0326
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optimization of culture conditions for high-level lactose-inducible expression of Leuconostoc mesenteroides dextransucrase in recombinant Escherichia coli strain BL 21(DE3), overview. Maximal activity of 60.18 U/ml from a fed-batch culture at 5 g/l lactose, added at an OD600 of 3.0, at 25C for 7 h
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E568Q
Leuconostoc mesenteroides B-1299CB4
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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additional information
Leuconostoc mesenteroides B-512F
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the enzyme is usable in the production of isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, alteration of the ratio of sucrose to maltose and the amount of each sugar, overview
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additional information
Leuconostoc mesenteroides B-512FMC
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construction of a truncated mutant of enzyme B-512F, the mutant shows sigmoidal shaped curves when the initial velocities are plotted against the concentration of added dextran. The increase in the reaction rate and the decrease in the sigmoidal curve with increasing dextran concentrations indicate that dextran binds at a noncatalytic or allosteric site to give a more active enzyme
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H643A
Leuconostoc mesenteroides B-742CB
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complete suppression of dextran synthesis activity
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additional information
Leuconostoc mesenteroides KIBGE IB-22
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generation of diverse mutant enzymes using UV irradiation random mutagensis, mutant screeening, overview. Mutant KIBGE IB-22M20 exhibits 6.75fold increased dextransucrase activity compared to the wild-type enzyme
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additional information
Leuconostoc mesenteroides Lm 28
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construction of constitutive mutants by chemical mutagenesis using ethyl methane sulfonate in strain Lm M281, overview
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H161R
Leuconostoc mesenteroides NRRl B-512(F)
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mutant protein retains a very low dextran synthesis activity
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additional information
Leuconostoc mesenteroides NRRL B-512F
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co-immobilization of dextransucrase and dextranase on calcium alginate for the facilitated synthesis of isomalto-oligosaccharides, reaction scheme, method optimization, and modeling, overview; construction of engineered enzyme variants for production of isomalto-oligosaccharides and dextrans of controlled molecular weight of about 10-40 kDa in a one-step process, method optimization, overview, rational deletions of the signal peptide, the beginning of the variable region and the last four repeats of the C-terminal end cause no loss of activity. The new variant successfully purified is remarkably stable. With a kcat of 584 per s, it is the most efficient recombinant glucansucrase described to date. The synthesized polymer possesses more than 95% of alpha-1,6 links, like the dextran produced by the native enzyme
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T350K/S455K
Leuconostoc mesenteroides NRRL B-512F
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mutant enzyme exhibits a 10fold increase in glucosyltransferase activity over those of the parental DSRS-His6 and its T350K and S455K mutants; produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
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additional information
Leuconostoc mesenteroides NRRL B512-F
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construction of fourteen truncated forms of strain NRRL B512-F dextransucrase by N-, C- or N- plus C-terminal domain truncations, dextran binding properties of mutant enzymes, overview
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additional information
Leuconostoc mesenteroides PCSIR-4
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the partially purified native enzyme from strain PCSIR-4 is immobilized on alginate for application in the production of dextran from sucrose, method optimization, overview
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additional information
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usage of two different artificial intelligence techniques, artificial neural network and genetic algorithm, for optimizing fermentation medium for the production of glucansucrase resulting in production of 6.75 U/ml, method development, overview
additional information
Leuconostoc mesenteroides subsp. dextranicum NRRL B-1146
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usage of two different artificial intelligence techniques, artificial neural network and genetic algorithm, for optimizing fermentation medium for the production of glucansucrase resulting in production of 6.75 U/ml, method development, overview
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additional information
Penicillium aculeatum
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co-immobilization of the enzyme with dextranase, EC 3.2.1.11, on calcium alginate, optimization of isomalto-oligosacchrides by the system, overview
additional information
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random mutagenesis of the most conserved motif around the transition state stabilizer in glucansucrase GTFR of Streptococcus oralis, yielding different variants with altered reaction specificity, generation of a mutant gtfR library, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
food industry
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the enzyme is used to produce kimchi in a fermentation process, which is improved by addition of Ca2+ salts that reduce lactic acid and elevate the pH for optimal activity of Leuconostoc bacteria
synthesis
D5FS20
the strain Leuconostoc citreum strain B/110-1-2 is used for industrial production of dextran and dextran derivatives
synthesis
Leuconostoc citreum B/110-1-2
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the strain Leuconostoc citreum strain B/110-1-2 is used for industrial production of dextran and dextran derivatives
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food industry
Leuconostoc citreum KACC 91035
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the enzyme is used to produce kimchi in a fermentation process, which is improved by addition of Ca2+ salts that reduce lactic acid and elevate the pH for optimal activity of Leuconostoc bacteria
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synthesis
C7DT60, -
the enzyme is useful for production of L-ascorbic acid 2-glucoside for use as an antioxidant in industrial applications
synthesis
Leuconostoc lactis EG001
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the enzyme is useful for production of L-ascorbic acid 2-glucoside for use as an antioxidant in industrial applications
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biotechnology
-
potential application of the C-terminal enzyme domain GBD-7 as an affinity tag onto cheap resins like for rapid purification of dextrans
medicine
O52224
industrial production of dextrans, that have important medical application in the production of fine chemicals such as plasma substitutes and Sephadex
nutrition
O52224
industrial production of dextrans, that find use for texture improvement in the food industry, e.g. milk drinks, yogurts and ice cream
nutrition
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production of controlled molecular weight isomaltooligosaccharides and oligodextrans from sucrose using the combined activity of a dextransucrase, EC 2.4.1.5, from Leuconostoc mesenteroides and endodextranase, EC 3.2.1.11, from Penicillium lilacinum. Higher substrate and dextranase concentrations give rise to products with lower molecular sizes and a dextransucrase/dextranase ratio of 1:1 or 1:2 appears to produce a polymer with a molecular weight which is desirable for prebiotic use
nutrition
-
immobilisation of dextransucrase from Leuconostoc mesenteroides NRRL B-512F in alginate is optimised for applications in a fluidised bed reactor with high concentrated sugar solutions, in order to allow a continuous formation of defined oligosaccharides as prebiotic isomalto-oligosaccharides
synthesis
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enzymatic synthesis of salicin prodrugs by the reaction of cyclomaltodextrin glucanyltransferase from Bacillus macerans with cyclomaltohexaose and salicyl alcohol which gives a salicin as a major product and the reaction of Leuconostoc mesenteroides B-742CB dextransucrase with sucrose and salicyl alcohol which gives a isosalicin as the major product
synthesis
-
the use of cashew apple juice as substrate is an interesting alternative to grow Leconostoc mesenteroides and to produce dextransucrase. High enzyme activities are obtained even when the substrate is used without yeast extract or phosphate addition
synthesis
-
potential use of the enzyme in production of glucooligosaccharides containing alpha(1,2) bonds for the dermocosmetic industry
synthesis
-
production of dextran
synthesis
-
engineered enzyme variants are capable to produce isomalto-oligosaccharides and dextrans of controlled molecular weight of about 10-40 kDa in a one-step process, overview
synthesis
-
the enzyme is usable in the production of isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, overview
synthesis
-
Leuconostoc mesenteroides dextransucrase is useful for enzymatic synthesis of alkyl alpha-D-glucosides, best yield is 50% using 1-butyl alpha-D-glucoside with 0.9 M 1-butanol
synthesis
O52224
one-step synthesis of isomalto-oligosaccharides by a fusion enzyme of dextransucrase and dextranase
synthesis
Leuconostoc mesenteroides B-1299
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potential use of the enzyme in production of glucooligosaccharides containing alpha(1,2) bonds for the dermocosmetic industry
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synthesis
Leuconostoc mesenteroides B-1299CB
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Leuconostoc mesenteroides dextransucrase is useful for enzymatic synthesis of alkyl alpha-D-glucosides, best yield is 50% using 1-butyl alpha-D-glucoside with 0.9 M 1-butanol
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synthesis
Leuconostoc mesenteroides B-512F
-
the enzyme is usable in the production of isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, overview
-
synthesis
Leuconostoc mesenteroides B-742CB
-
enzymatic synthesis of salicin prodrugs by the reaction of cyclomaltodextrin glucanyltransferase from Bacillus macerans with cyclomaltohexaose and salicyl alcohol which gives a salicin as a major product and the reaction of Leuconostoc mesenteroides B-742CB dextransucrase with sucrose and salicyl alcohol which gives a isosalicin as the major product
-
nutrition
Leuconostoc mesenteroides NRRL B-512F
-
immobilisation of dextransucrase from Leuconostoc mesenteroides NRRL B-512F in alginate is optimised for applications in a fluidised bed reactor with high concentrated sugar solutions, in order to allow a continuous formation of defined oligosaccharides as prebiotic isomalto-oligosaccharides; production of controlled molecular weight isomaltooligosaccharides and oligodextrans from sucrose using the combined activity of a dextransucrase, EC 2.4.1.5, from Leuconostoc mesenteroides and endodextranase, EC 3.2.1.11, from Penicillium lilacinum. Higher substrate and dextranase concentrations give rise to products with lower molecular sizes and a dextransucrase/dextranase ratio of 1:1 or 1:2 appears to produce a polymer with a molecular weight which is desirable for prebiotic use
-
synthesis
Leuconostoc mesenteroides NRRL B-512F
-
engineered enzyme variants are capable to produce isomalto-oligosaccharides and dextrans of controlled molecular weight of about 10-40 kDa in a one-step process, overview
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biotechnology
Leuconostoc mesenteroides NRRL B512-F
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potential application of the C-terminal enzyme domain GBD-7 as an affinity tag onto cheap resins like for rapid purification of dextrans
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synthesis
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alpha-glycosylation by GTFR with sucrose and different alcohols and amino acid derivatives for the synthesis of glycoethers and glycosylated amino acids, which are not easy to obtain by chemical or enzymatic synthetic methods. These products can be used for solid-phase synthesis to generate glycopeptides
food industry
H1X7X9
the dextransucrase is responsible for production of dextran with predominant alpha-(1->6) linkages that might find applications as food hydrocolloids
food industry
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the dextransucrase is responsible for production of dextran with predominant alpha-(1->6) linkages that might find applications as food hydrocolloids
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