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Information on EC 2.4.1.390 - 4,3-alpha-glucanotransferase
for references in articles please use BRENDA:EC2.4.1.390
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.390 4,3-alpha-glucanotransferase
IUBMB Comments
The enzyme, characterized from the bacterium Lactobacillus fermentum NCC 2970, possesses hydrolysis and transglycosylase activities on malto-oligosaccharides with a degree of polymerization of at least 6, as well as polymers such as amylose, potato starch, and amylopectin. The enzyme, which belongs to glycoside hydrolase 70 (GH70) family, attaches the glucosyl residues by α(1→3) linkages in both linear and branched orientations. While capable of forming large polymers, the enzyme produces mainly oligosaccharides in vitro.
The expected taxonomic range for this enzyme is: Limosilactobacillus
Reaction Schemes
showformation of a mixed (1->4)/(1->3)-alpha-D-glucan from (1->4)-alpha-D-glucans
Synonyms
4,3-alpha-GTase, 4,3-alphaGT, GtfB, LACFE_CDS0221, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4,3-alpha-GTase
GtfB
GtfB
-
-
gene name, ambiguous
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formation of a mixed (1->4)/(1->3)-alpha-D-glucan from (1->4)-alpha-D-glucans
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan:(1->4)/(1->3)-alpha-D-glucan 3-alpha-D-glucosyltransferase
The enzyme, characterized from the bacterium Lactobacillus fermentum NCC 2970, possesses hydrolysis and transglycosylase activities on malto-oligosaccharides with a degree of polymerization of at least 6, as well as polymers such as amylose, potato starch, and amylopectin. The enzyme, which belongs to glycoside hydrolase 70 (GH70) family, attaches the glucosyl residues by alpha(1->3) linkages in both linear and branched orientations. While capable of forming large polymers, the enzyme produces mainly oligosaccharides in vitro.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylose V
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose
Substrates: -
Products: -
Products: -
?
amylose V
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + maltose
Substrates: -
Products: -
Products: -
?
high-amylose maize starch
?
Substrates: -
Products: -
Products: -
?
maltoheptaose
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose
Substrates: -
Products: -
Products: -
?
maltoheptaose
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + maltose
Substrates: -
Products: -
Products: -
?
maltohexaose
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose
Substrates: -
Products: -
Products: -
?
maltohexaose
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + maltose
Substrates: -
Products: -
Products: -
?
maltopentaose
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose
Substrates: -
Products: -
Products: -
?
maltopentaose
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + maltose
Substrates: -
Products: -
Products: -
?
amylose
?
Substrates: besides native (alpha1->4) and (alpha1->3) linkages, the mutant enzymes G1028R and D991N show 8 and 10% (alpha1->6) linkage increases compared to 1% for wild-type in products
Products: -
Products: -
?
amylose
?
Limosilactobacillus fermentum NCC 2970
Substrates: besides native (alpha1->4) and (alpha1->3) linkages, the mutant enzymes G1028R and D991N show 8 and 10% (alpha1->6) linkage increases compared to 1% for wild-type in products
Products: -
Products: -
?
maltoheptaose
malto-oligosaccaride
-
Substrates: -
Products: -
Products: -
?
maltoheptaose
malto-oligosaccaride
-
Substrates: -
Products: -
Products: -
?
maltohexaose
malto-oligosaccaride
-
Substrates: -
Products: -
Products: -
?
maltohexaose
malto-oligosaccaride
-
Substrates: -
Products: -
Products: -
?
maltose
malto-oligosaccaride
-
Substrates: -
Products: -
Products: -
?
starch
malto-oligosaccaride
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: GtfB displays both hydrolysis and transglycosylase (disproportionation) activity on malto-oligosaccharides of DP 6 and 7. GtfB is not active on malto-oligosaccharides of DP below 4 and shows low disproportionating activity with maltopentaose. The enzyme fails to act on sucrose, panose, nigerose, and isomalto-oligosaccharides with DP2, DP3, and DP5
Products: -
Products: -
?
additional information
?
-
Substrates: 4,3-alpha-GTase has a stronger affinity for linear starch chains than for branched glucan chains. The affinity of 4,3-alpha-GTase for alpha-1,4 linked glucan chains is positively correlated with the degree of polymerization of the substrate. Oligosaccharides are the receptor molecules of 4,3-alpha-GTase. Therefore the hydrolytic activity of the enzyme is preferentially presented when the enzyme was incubated with long-chain alpha-1,4 glucans. Longchain alpha-1,4 linked glucan chains are the preferred donor molecules for the enzymatic transglycosylation reaction, and the higher degree of polymerization value results in higher efficiency of the transglycosylation reaction
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylose V
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose
Substrates: -
Products: -
Products: -
?
maltoheptaose
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose
Substrates: -
Products: -
Products: -
?
maltohexaose
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose
Substrates: -
Products: -
Products: -
?
maltopentaose
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: GtfB displays both hydrolysis and transglycosylase (disproportionation) activity on malto-oligosaccharides of DP 6 and 7. GtfB is not active on malto-oligosaccharides of DP below 4 and shows low disproportionating activity with maltopentaose. The enzyme fails to act on sucrose, panose, nigerose, and isomalto-oligosaccharides with DP2, DP3, and DP5
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
amylose
Km: 0.61 mg/ml, pH 5.0, 40°C, wild-type enzyme
additional information
amylose
Km: 0.53 mg/ml, pH 5.0, 40°C, mutant enzyme A1398Y
additional information
amylose
Km: 3.96 mg/ml, pH 5.0, 40°C, mutant enzyme G1028R
additional information
amylose
Km: 0.39 mg/ml, pH 5.0, 40°C, mutant enzyme E1405D
additional information
amylose
Km: 0.61 mg/ml, pH 5.0, 40°C, mutant enzyme D991H
additional information
amylose
Km: 0.35 mg/ml, pH 5.0, 40°C, mutant enzyme T1400E
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 7.5
-
pH 3.5: about 45% of maximal activity, pH 7.5: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 2.4.1.5; cf. EC 2.4.1.5
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
predicted by in silico analysis, protein contains the classical Gram-positive N-terminal signal peptide of 39 amino acids
-
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
enzyme acts as a 4,3-alpha-glucanotransferase, converting amylose into a new type of alpha-glucan with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A1D7ZV76_LIMFE
1593
0
179585
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A1398Y
the mutant shows decreased total activity and slightly increased hydrolytic activity, leading to low transglucosylase efficiency
D991H
the mutant has relatively higher total activity but is more hydrolytic than the wild-type enzyme. The mutant enzyme has increased temperature optimum of 45°C
D991N
besides native (alpha1->4) and (alpha1->3) linkages,the mutant shows 10% (alpha1->6) linkage increases compared to 1% for wild-type in products. The orientation of acceptor binding in the mutant is favorable for (alpha1->6) linkage synthesis
E1405D
the mutant displays lower total activity and lower hydrolytic activity and slightly decreased transglucosylase efficiency
G1028R
T1400E
the mutant has relatively higher total activity but is more hydrolytic than the wild-type enzyme
A1398Y
Limosilactobacillus fermentum NCC 2970
-
the mutant shows decreased total activity and slightly increased hydrolytic activity, leading to low transglucosylase efficiency
-
D991H
Limosilactobacillus fermentum NCC 2970
-
the mutant has relatively higher total activity but is more hydrolytic than the wild-type enzyme. The mutant enzyme has increased temperature optimum of 45°C
-
D991N
Limosilactobacillus fermentum NCC 2970
-
besides native (alpha1->4) and (alpha1->3) linkages,the mutant shows 10% (alpha1->6) linkage increases compared to 1% for wild-type in products. The orientation of acceptor binding in the mutant is favorable for (alpha1->6) linkage synthesis
-
G1028R
Limosilactobacillus fermentum NCC 2970
-
besides native (alpha1->4) and (alpha1->3) linkages,the mutant shows 8% (alpha1->6) linkage increases compared to 1% for wild-type in products. The orientation of acceptor binding in the mutant is favorable for (alpha1->6) linkage synthesis
-
T1400E
Limosilactobacillus fermentum NCC 2970
-
the mutant has relatively higher total activity but is more hydrolytic than the wild-type enzyme
-
G1028R
besides native (alpha1->4) and (alpha1->3) linkages,the mutant shows 8% (alpha1->6) linkage increases compared to 1% for wild-type in products. The orientation of acceptor binding in the mutant is favorable for (alpha1->6) linkage synthesis
G1028R
the mutant shows decreased total activity and slightly increased hydrolytic activity, leading to low transglucosylase efficiency. The mutant enzyme has increased temperature optimum of 45°C
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
6 h, approximately 90% residual activity is retained
45
45
enzyme shows low stability at temperatures above 45°C in 20 mM Tris-HCl buffer pH 8.0
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, purification from soluble fraction by metal chelate chromatography and anion-exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
4,6-alpha-GTase (cf. EC 2.4.1.394) and 4,3-alpha-GTase genes from Limosilactobacillus reuteri E81 and Limosilactobacillus fermentum PFC282 respectively are transformed into the plasmid pLEB124 vector having the signal peptide usp45 under the P45 continuous promoter and are successfully expressed in Lactococcus lactis MG1363
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
food industry
-
4,3-alpha-GTase and 4,6-alpha-GTase (cf. EC 2.4.1.394) produced by Lactococcus lactis by extracellular secretion have technological and health functional effects in bakery products, such as bread and bun. The enzymes successfully lower the glycemic index and delayed staling
food industry
-
synthesis of alpha-glucans with alpha-1,4 and alpha-1,3 linkages by a dual enzyme reaction combining amylosucrase from Neisseria polysaccharea (cf. EC 2.4.1.4) and 4,3-alpha-glucanotransferase from Lactobacillus fermentum NCC 29704. The alpha-glucans with alpha-1,4 and alpha-1,3 linkages can be utilized as slowly digestible and prebiotic ingredients in the gastrointestinal tract due to their linkage patterns and high molecular weights
food industry
-
4,3-alpha-GTase and 4,6-alpha-GTase (cf. EC 2.4.1.394) produced by Lactococcus lactis by extracellular secretion have technological and health functional effects in bakery products, such as bread and bun. The enzymes successfully lower the glycemic index and delayed staling
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gangoiti, J.; van Leeuwen, S.S.; Gerwig, G.J.; Duboux, S.; Vafiadi, C.; Pijning, T.; Dijkhuizen, L.
4,3-alpha-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H
Sci. Rep.
7
39761
2017
Limosilactobacillus fermentum (A0A1D7ZV76)
brenda
Biyikli, A.; Nicin, R.; Dertli, E.; Simsek, O.
Extracellular recombinant production of 4,6 and 4,3 alpha-glucanotransferases in Lactococcus lactis
Enzyme Microb. Technol.
164
110175
2023
Limosilactobacillus fermentum, Limosilactobacillus fermentum PFC282
brenda
Yang, Y.; Sun, Y.; Zhang, T.; Hamaker, B.R.; Miao, M.
Insights into the catalytic properties of 4,3-alpha-glucanotransferase to guide the biofabrication of alpha-glucans with low digestibility
Food Funct.
15
8274-8285
2024
Limosilactobacillus fermentum (A0A1D7ZV76)
brenda
Nicin, R.T.; Zehir-Sentuerk, D.; Oezkan, B.; Goeksungur, Y.; Simsek, O.e.
Optimization of 4,6-alpha and 4,3-alpha-glucanotransferase production in Lactococcus lactis and determination of their effects on some quality characteristics of bakery products
Foods
13
432
2024
Limosilactobacillus reuteri, Limosilactobacillus reuteri E81
brenda
Ryu, H.J.; Song, Y.B.; Choi, W.; Yoo, S.H.; Lee, B.H.
Macromolecular alpha-glucans with alpha-1,3/alpha-1,4 branching structures produced using dual glycosyltransferases Elucidation of physicochemical and slowly digestible properties
Int. J. Biol. Macromol.
242
124921
2023
Limosilactobacillus fermentum
brenda
Chen, Y.; Dong, J.; Li, X.; Jin, Z.; Svensson, B.; Bai, Y.
Acceptor subsite mutants of Limosilactobacillus fermentum NCC 2970 GtfB 4,3-alpha-glucanotransferase regulate the ratio of (alpha1->3)/(alpha1->6) linkages in biosynthesized alpha-glucans
J. Agric. Food Chem.
72
19994-20004
2024
Limosilactobacillus fermentum (A0A1D7ZV76), Limosilactobacillus fermentum NCC 2970 (A0A1D7ZV76)
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.390)
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