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Enzyme Nomenclature
Information on EC 2.4.1.18 - 1,4-alpha-glucan branching enzyme
Word Map on EC 2.4.1.18
- 2.4.1.18
- amylopectin
- endosperm
- maize
- grain
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pyrophosphorylase
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granule-bound
- glucans
-
debranching
- adp-glucose
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polyglucosan
- amyloplasts
- ssiia
- kernel
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chain-length
- isoamylase
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waxy
- andersen
- glycogenosis
- agpase
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high-amylose
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amylopectin-like
- alpha-glucans
- pullulanase
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alpha-1,6
- glycogenin
- food industry
- medicine
- nutrition
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
2.4.1.18
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RECOMMENDED NAME
GeneOntology No.
1,4-alpha-glucan branching enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain
Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyclization
glycosyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan:(1->4)-alpha-D-glucan 6-alpha-D-[(1->4)-alpha-D-glucano]-transferase
Converts amylose into amylopectin. The accepted name requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme. The latter has frequently been termed Q-enzyme.
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CAS REGISTRY NUMBER
COMMENTARY
9001-97-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the protein consists of 613 amino acids. The branching enzyme of Anaerobranca gottschalkii lacks the N-terminal extension of approximately 100 amino acids found in the branching enzymes of Escherichia coli and its close phylogenetic relatives. The absence of a signal sequence indicates that the branching enzyme is an intracellular enzyme.
Swissprot
Cyanobacterium sp.
multiple isoforms: starch-branching enzymes IIa and starch-branching enzymes IIb
SwissProt
sweet potato IbSBEI gene. Full-length cDNA is 2870 bp long, this cDNA is closest to that of potato gene (StSBEI), they are 80.1% identical.; sweet potato, Kokei 14
Swissprot
the primary amino acid sequence has four cysteine residues at position: 95, 193, 617 and 658, therefore there is a possibility of forming intramoleculare disulfide bonds. The two closely migrating bands of purified protein on a non-reducing SDS-PAGE might be due to the presence of two populations of different confomations of the same protein: the oxidized and the reduced.; H37Rv
Swissprot
the primary amino acid sequence has four cysteine residues at position: 95, 193, 617 and 658, therefore there is a possibility of forming intramoleculare disulfide bonds. The two closely migrating bands of purified protein on a non-reducing SDS-PAGE might be due to the presence of two populations of different confomations of the same protein: the oxidized and the reduced.; H37Rv
Swissprot
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TK1436 encodes a protein of 675 aa; hyperthermophilic archaeon
Swissprot
cultivar BY535 with a high starch content and culitvar JM20 with a low starch content
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the glycoside hydrolase family GH13
evolution
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great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
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great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes; great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes; great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
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great variation exists as to the preference of branching enzymes of different species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
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the branching enzyme is an unusual member of the alpha-amylase family because it has both alpha-1,4-amylase activity and alpha-1,6-transferase activity
evolution
Cyanobacterium sp.
Cyanobacterium sp. NBRC 102756 belongs to the cyanobacteria that accumulate water-insoluble alpha-glucan similar to amylopectin rather than glycogen, the latter of which is more commonly produced in these organisms. The amylopectin-producing species invariably have three branching enzyme (BE) homologues, BE1, BE2, and BE3, all belonging to the glycoside hydrolase family 13, GH13, phylogenetic tree. The specific activity of BE3 is much lower than those of BE1 and BE2. Isozymes BE1 and BE2 show similar chain-length preference to BEIIb isoform of Oryza sativa, while the catalytic specificity of BE3 is similar to that of Oryza sativa BEI. These results indicate that starch-producing cyanobacteria have both type-I BE (BE3) and type-II BEs (BE1 and BE2) in terms of chain-length preferences, as is the case of plants; Cyanobacterium sp. NBRC 102756 belongs to the cyanobacteria that accumulate water-insoluble alpha-glucan similar to amylopectin rather than glycogen, the latter ofwhich is more commonly produced in these organisms. The amylopectin-producing species invariably have three branching enzyme (BE) homologues, BE1, BE2, and BE3, all belonging to the glycoside hydrolase family 13, GH13, phylogenetic tree. The specific activity of BE3 is much lower than those of BE1 and BE2. Isozymes BE1 and BE2 show similar chain-length preference to BEIIb isoform of Oryza sativa, while the catalytic specificity of BE3 is similar to that of Oryza sativa BEI. These results indicate that starch-producing cyanobacteria have both type-I BE (BE3) and type-II BEs (BE1 and BE2) in terms of chain-length preferences, as is the case of plants; Cyanobacterium sp. NBRC 102756 belongs to the cyanobacteria that accumulate water-insoluble alpha-glucan similar to amylopectin rather than glycogen, the latter ofwhich is more commonly produced in these organisms. The amylopectin-producing species invariably have three branching enzyme (BE) homologues, BE1, BE2, and BE3, all belonging to the glycoside hydrolase family 13, GH13, phylogenetic tree. The specific activity of BE3 is much lower than those of BE1 and BE2. Isozymes BE1 and BE2 show similar chain-length preference to BEIIb isoform of Oryza sativa, while the catalytic specificity of BE3 is similar to that of Oryza sativa BEI. These results indicate that starch-producing cyanobacteria have both type-I BE (BE3) and type-II BEs (BE1 and BE2) in terms of chain-length preferences, as is the case of plants
evolution
the enzyme belongs to the glycoside hydrolase family 13, GH13. Phylogenetic analysis groups VvGBE with other Vibrio GBEs and closely related to GBEs of enteric bacteria. VvGBE and Escherichia coli GBE are type I bacterial GBEs and share 57% sequence similarity
evolution
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Cyanobacterium sp. NBRC 102756 belongs to the cyanobacteria that accumulate water-insoluble alpha-glucan similar to amylopectin rather than glycogen, the latter of which is more commonly produced in these organisms. The amylopectin-producing species invariably have three branching enzyme (BE) homologues, BE1, BE2, and BE3, all belonging to the glycoside hydrolase family 13, GH13, phylogenetic tree. The specific activity of BE3 is much lower than those of BE1 and BE2. Isozymes BE1 and BE2 show similar chain-length preference to BEIIb isoform of Oryza sativa, while the catalytic specificity of BE3 is similar to that of Oryza sativa BEI. These results indicate that starch-producing cyanobacteria have both type-I BE (BE3) and type-II BEs (BE1 and BE2) in terms of chain-length preferences, as is the case of plants; Cyanobacterium sp. NBRC 102756 belongs to the cyanobacteria that accumulate water-insoluble alpha-glucan similar to amylopectin rather than glycogen, the latter ofwhich is more commonly produced in these organisms. The amylopectin-producing species invariably have three branching enzyme (BE) homologues, BE1, BE2, and BE3, all belonging to the glycoside hydrolase family 13, GH13, phylogenetic tree. The specific activity of BE3 is much lower than those of BE1 and BE2. Isozymes BE1 and BE2 show similar chain-length preference to BEIIb isoform of Oryza sativa, while the catalytic specificity of BE3 is similar to that of Oryza sativa BEI. These results indicate that starch-producing cyanobacteria have both type-I BE (BE3) and type-II BEs (BE1 and BE2) in terms of chain-length preferences, as is the case of plants; Cyanobacterium sp. NBRC 102756 belongs to the cyanobacteria that accumulate water-insoluble alpha-glucan similar to amylopectin rather than glycogen, the latter ofwhich is more commonly produced in these organisms. The amylopectin-producing species invariably have three branching enzyme (BE) homologues, BE1, BE2, and BE3, all belonging to the glycoside hydrolase family 13, GH13, phylogenetic tree. The specific activity of BE3 is much lower than those of BE1 and BE2. Isozymes BE1 and BE2 show similar chain-length preference to BEIIb isoform of Oryza sativa, while the catalytic specificity of BE3 is similar to that of Oryza sativa BEI. These results indicate that starch-producing cyanobacteria have both type-I BE (BE3) and type-II BEs (BE1 and BE2) in terms of chain-length preferences, as is the case of plants
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evolution
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the enzyme belongs to the glycoside hydrolase family 13, GH13. Phylogenetic analysis groups VvGBE with other Vibrio GBEs and closely related to GBEs of enteric bacteria. VvGBE and Escherichia coli GBE are type I bacterial GBEs and share 57% sequence similarity
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malfunction
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mutations of conserved residues in binding sites I and VI have a debilitating effect on the activity of the enzyme
malfunction
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starch from tubers of enzyme overexpressing plants posses an increased degree of amylopectin branching, with more short chains of degree of polymerisation (DP) 6-12 and particularly of DP6. Construction of transgenic lines expressing a GRANULE-BOUND STARCH SYNTHASE (GBSS) RNAi, which exhibit post-transcriptional gene silencing of GBSS and reduced amylose content in the starch. Both transgenic modifications do not affect granule morphology but reduce starch peak viscosity. In starch from SBEII-overexpressing lines, the increased ratio of short to long amylopectin branches facilitates gelatinisation, which occurs at a reduced temperature (by up to 3°C) or lower urea concentration. In contrast, silencing of GBSS increases the gelatinisation temperature by 4°C, and starch requires a higher urea concentration for gelatinisation. In lines with a range of SBEII overexpression, the magnitude of the increase in SBEII activity, reduction in onset of gelatinisation temperature and increase in starch swollen pellet volume are highly correlated, consistent with reports that starch swelling is greatly dependent upon the amylopectin branching pattern
malfunction
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inhibitory effects of these hpSBEIIRNA constructs on the expression of SBEIIa and SBEIIb in maize endosperm, levels of ZmSBEII transcription and SBE activity in kernels of transgenic plants, overview. The transgenic maize lines show increased content of amylopectin chains with high-molecular weight compared to decreased low-molecular weight chains; inhibitory effects of these hpSBEIIRNA constructs on the expression of SBEIIa and SBEIIb in maize endosperm, levels of ZmSBEII transcription and SBE activity in kernels of transgenic plants, overview. The transgenic maize lines show increased content of amylopectin chains with high-molecular weight compared to decreased low-molecular weight chains
metabolism
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granule-bound proteins involved in amylopectin synthesis are partitioned into the starch granule as a result of their association within protein complexes, and strach synthase IIa plays a crucial role in trafficking starch synthase I and starch branching enzyme IIb into the granule matrix. A mutant starch synthase IIa that has lost catalytic activity and is inable to bind to starch additionally leads to greatly reduced activities of starch synthase I and starch branching enzyme IIb
metabolism
glycogen and starch branching enzymes catalyze the formation of alpha(1->6) linkages in storage polysaccharides by rearrangement of preexisting alpha-glucans. This reaction occurs through the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position. These enzymes define major elements that control the structure of both glycogen and starch
metabolism
the balance between branching and debranching is crucial for the synthesis of starch, as an excess of branching activity results in the formation of highly branched, water-soluble, poorly crystalline polyglucan
metabolism
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starch synthase and branching enzyme establish the two glycosidic linkages existing in starch. Both enzymes exist as several isoforms. Starch synthase I activity in native PAGE without addition of glucans is dependent on at least one of the two branching enzyme isoforms active in Arabidopsis leaves. This interaction is most likely not based on a physical association of the enzymes. All starch synthase isoforms I-IV are able to interact with branching enzymes and form branched glucans
metabolism
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key biocatalyst in synthesis of polysaccharides
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physiological function
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the synthesis of maltodextrins by alpha-glucan phosphorylase Pho1 is markedly accelerated by branching enzyme isozymes, with the greatest effect being exhibited by the presence of branching isozyme BEI rather than by isozyme BEIIa or isozyme BEIIb. The enhancement of the activity of Pho1 by branching enzymes is not merely due to the supply of a non-reducing ends. At the same time, Pho1 greatly enhances the branching enzyme activity, possibly by generating a branched carbohydrate substrate which is used by branching enzyme with a higher affinity. The interaction between Pho1 and branching enzyme is not merely due to chain-elongating and chain-branching reactions, but occurs in a physically and catalytically synergistic manner by each activating the mutual capacity of the other, presumably forming a physical association of Pho1, isoform BEI and branched maltodextrins
physiological function
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the branching enzyme is responsible for all branching of glycogen and starch. It has both alpha-1,4-amylase activity and alpha-1,6-transferase activity
physiological function
glycogen is a major polysaccharide of energy reservoir in animals and microorganisms. It is a highly branched polysaccharide, in which glucose residues are linked by alpha-1,4 glycosidic bonds to from linear chains and at every 10 residues, other linear chains are linked by alpha-1,6-glycosidic bonds to form side chains. Formation of side chains in glycogen is catalyzed by glycogen branching enzyme (GBE) or branching enzyme (BE). GBE catalyzes formation of alpha-1,6-glycosidic linkage by cleaving alpha-1,4 linkages of substrate and transferring the non-reducing end of the chain to an acceptor
physiological function
starch branching enzyme IIb plays a crucial role in amylopectin biosynthesis in maize endosperm by defining the structural and functional properties of storage starch and is regulated by protein phosphorylation
physiological function
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the enzyme GlgB is essential for the biosynthesis of branched glucan and modulates pathogenesis and survival, it is the key enzyme involved in the biosynthesis of alpha-glucan, which plays a significant role in the virulence and pathogenesis of Mycobacterium tuberculosis
physiological function
starch synthesis requires several enzymatic activities including branching enzymes (BEs) responsible for the formation of alpha(1->6) linkages. Distribution and number of these linkages are further controlled by debranching enzymes that cleave some of them, rendering the polyglucan water-insoluble and semi-crystalline. The activity of BEs and debranching enzymes is mandatory to sustain normal starch synthesis
physiological function
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rice branching enzyme isozymes BEI, BEIIa, or BEIIb accelerate the reaction velocity of starch synthase SSI, but not of SSIIa or SSIIIa, in rice. The interaction between starch synthase I (SSI) and branching enzyme (BE) is established by stimulation of SSI activity with BE and by activation of the BE activity by SSI; rice branching enzyme isozymes BEI, BEIIa, or BEIIb accelerate the reaction velocity of starch synthase SSI, but not of SSIIa or SSIIIa, in rice. The interaction between starch synthase I (SSI) and branching enzyme (BE) is established by stimulation of SSI activity with BE and by activation of the BE activity by SSI
physiological function
SBE is the only enzyme that generates glucan branches, i.e. it is the only chain-stopping substance for branch growth, and as a consequence SBE has a significant effect on the final structure of the resulting starch
physiological function
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glycogen is a major polysaccharide of energy reservoir in animals and microorganisms. It is a highly branched polysaccharide, in which glucose residues are linked by alpha-1,4 glycosidic bonds to from linear chains and at every 10 residues, other linear chains are linked by alpha-1,6-glycosidic bonds to form side chains. Formation of side chains in glycogen is catalyzed by glycogen branching enzyme (GBE) or branching enzyme (BE). GBE catalyzes formation of alpha-1,6-glycosidic linkage by cleaving alpha-1,4 linkages of substrate and transferring the non-reducing end of the chain to an acceptor
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physiological function
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starch branching enzyme IIb plays a crucial role in amylopectin biosynthesis in maize endosperm by defining the structural and functional properties of storage starch and is regulated by protein phosphorylation
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additional information
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six distinct oligosaccharide binding sites on the surface of the branching enzyme, most of which surround the edge of the beta-barrel domain and are quite far from the active site. No evidence of oligosaccharide binding in the active site of the enzyme, the closest bound oligosaccharide resides almost 18 A from the active site
additional information
branching patterns of the truncation mutants and the swapping mutant. Branching patterns of VvGBE wild-type
additional information
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branching patterns of the truncation mutants and the swapping mutant. Branching patterns of VvGBE wild-type
additional information
molecular dynamics simulation and modeling of phosphorylation of enzyme mutants
additional information
the branching enzyme's origin has only a limited impact on establishing essential characteristics of starch
additional information
Tyr352, Glu513, and Ser349 are important for mSBEIIa activity while Arg456 is important for determining the position at which the linear glucan is cut, enzyme active site structure, molecular dynamics simulations and modeling, overview
additional information
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branching patterns of the truncation mutants and the swapping mutant. Branching patterns of VvGBE wild-type
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additional information
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molecular dynamics simulation and modeling of phosphorylation of enzyme mutants
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylose
branched polyglucan
using linear amylose synthesized in a tandem reaction by potato phosphorylase
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?
amylopectin
?
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the amount of short chains with a degree of polymerization of 6-8 is significantly increased in the product of Bacillus cereus
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?
amylopectin
?
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enzyme efficiently cyclizes the inner chain of amylopectin to degrade the molecule. The degradation stopps when the molecular mass of the product reaches about 150 kDa
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?
amylopectin
?
assay at 30°C, reaction terminated by heating at 95°C for 5 min
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?
amylopectin
?
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enzyme catalyzes cyclization of amylopectin, the amount of short chains with a degree of polymerization of 6-8 is significantly increased compared to reaction products of Bacillus stearothermophilus enzyme
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?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
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the enzyme cyclizes the B-chain which connects the cluster structures of amylopectin. The product, highly branched cyclic dextrin, has a ring structure with DPw 50 and non-cyclic chains with an average unit chain length of 16 connected to the ring
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amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
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?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
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the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, the mutant enzyme DELTA1-112 transfers a greater propertion of chains with higher degree of polymerization, 15-20. Mutant DELTA1-63 and mutant DELTA1-83 have an intermediate pattern of transferred chains, 10-20. A progressive shortening of the N-terminus leads to a gradual increase in the length of the transferred chains
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?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
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?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
the C-terminal regions of isoenzyme PvSBE1 and PvSBE2 have different roles in branching enzyme activity. The C-terminal region of PvSBE1 confers specificity to amylose while that of PvSBE2 confers specificity to the transfer of short chains
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?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
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-
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?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
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enzyme form SBE II is more active than enzyme form SBE I. The enzyme forms SBE I and SBE II mainly branch the dextrins by intrachain branching.The products of SBE I show distinct populations at DP11-12 and DP29-30. The products of enzyme form SBE II habe one, broader, population with a peak at DP13-14. An accumulation of 6-7 chains is seen with both isoforms
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amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
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-
-
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?
amylose
?
branching assay, at pH 8.0, reaction stopped by boiling for 5 min
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?
amylose
?
branching assay, at pH 8.0, reaction stopped by boiling for 5 min
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-
?
amylose
?
branching assay, at pH 8.0, reaction stopped by boiling for 5 min
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?
amylose
?
assay at 30°C, reaction terminated by heating at 95°C for 5 min
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?
amylose
amylose containing alpha-1,6-glucosidic linkages
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characterization of products, smallest chains transferred contain 5-7 glucose units
?
amylose
amylose containing alpha-1,6-glucosidic linkages
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wild-type enzyme and mutant enzyme Y300F both preferentially transfer chains between DP5 and DP16, with a chain of DP11 being transferred at the highest frequency
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amylose
amylose containing alpha-1,6-glucosidic linkages
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the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, the mutant enzyme DELTA1-112 transfers a greater proportion of chains with higher degree of polymerization, 15-20. Mutant DELTA1-63 and mutant DELTA1-83 have an intermediate pattern of transferred chains, 10-20. A progressive shortening of the N-terminus leads to a gradual increase in the length of the transferred chains
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?
amylose
amylose containing alpha-1,6-glucosidic linkages
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-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
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-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
the C-terminal regions of isoenzyme PvSBE1 and PvSBE2 have different roles in branching enzyme activity. The C-terminal region of PvSBE1 confers specificity to amylose while that of PvSBE2 confers specificity to the transfer of short chains
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?
amylose
amylose containing alpha-1,6-glucosidic linkages
potato type III amylose
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?
amylose
amylose containing alpha-1,6-glucosidic linkages
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at 35°C the enzyme does not act rapidly on such chains unless they are about 40 glucose units or more in length, at 4°C the minimum length falls to about 10
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?
amylose
amylose containing alpha-1,6-glucosidic linkages
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enzyme SBE I is more active than enzyme SBE II. The enzyme forms SBE I and SBE II mainly branch the dextrins by intrachain branching. The products of SBE I show distinct populations at DP11-12 and DP29-30. The products of enzyme form SBE II have one, broader, population with a peak at DP13-14. An accumulation of 6-7 chains is seen with both isoforms
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-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
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the enzyme acts on native and synthetic amyloses to give products resembling amylopectin in terms of average unit chain length, degree of beta-amylolysis and iodine stain. The profiles of the unit chains of theses synthetic products are, however, different from that of native amylopectin
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-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
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initially the three isoenzymes BE I, BE IIa and BE IIb produce chains of various sizes, DP approximately 8 to 200. Isoenzyme BE I preferentially transfers longer chains than isoenzyme IIa and IIb
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starch
starch containing alpha-1,6-glucosidic linkages
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?
starch
starch containing alpha-1,6-glucosidic linkages
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-
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?
additional information
?
-
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cyclodextrins neither serve as donors nor as acceptors
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-
-
additional information
?
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cyclodextrins neither serve as donors nor as acceptors
-
-
-
additional information
?
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Starch synthase I activity in native PAGE without addition of glucans is dependent on at least one of the two branching enzyme isoforms active in Arabidopsis leaves. This interaction is most likely not based on a physical association of the enzymes. Chain length distribution patterns of the formed glucans are irrespective of enzyme isoforms origin and still independent of assay conditions. All starch synthase isoforms I-IV are able to interact with branching enzymes and form branched glucans, product analysis, overview
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-
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additional information
?
-
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the branching enzyme converts any sizes of amyloses to a highly branched glucan with the same molecular size
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additional information
?
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the enzyme performs branching of amylose from Oryza sative starch, product identification and determination, overview
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additional information
?
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the enzyme performs branching of amylose from Oryza sative starch, product identification and determination, overview
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-
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additional information
?
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Cyanobacterium sp.
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
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additional information
?
-
Cyanobacterium sp.
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
-
additional information
?
-
Cyanobacterium sp.
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
-
additional information
?
-
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
-
additional information
?
-
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
-
additional information
?
-
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
-
additional information
?
-
glycogen branching enzyme GBE1 mutation causing equine glycogen storage disease IV.A C to A substitution at base 102 results in a tyrosine (Y) to stop (X) mutation in codon 34 of exon of exon 1. All 11 affected foals are homozygous for the X34 allele, all 16 control horses are homozygous for the Y34 allele. Poorly branched glycogen, abnormal polysaccharide accumulation, lack of measurable GBE1 enzyme activity and immunodetectable GBE1 protein, coupled with the present observation of abundant GBE1 mRNA in affected foals, are consistent with the nonsense mutation in the 699 amino acid GBE1 protein
-
-
-
additional information
?
-
-
the enzyme is responsible for the formation of the alpha-1,6 linkages in the glycogen molecule
-
-
-
additional information
?
-
the Escherichia coli enzyme specifically forms the branch linkages at the third glucose residue from the reducing end of the acceptor chain. The enzyme recognizes the location of branching points in its acceptor chain during their branching reaction
-
-
-
additional information
?
-
-
a fatal form of glycogen storage disease IV affects Norwegian Florest Cat, in which striated muscles and the nervous system are primarily affected, while the liver remains unaffected. This form of GSD IV is caused by a 6.1-kb deletion that eliminates exon 12 of the feline GBE1 gene
-
-
-
additional information
?
-
-
each isoform of the Q-enzyme plays a distinct role in starch biosynthesis
-
-
-
additional information
?
-
two-step reaction mechanism for the amylase activity, i.e. 1-4 bond breakage, and isomerization, i.e. 1-6 bond formation, which occur in the same catalytic pocket
-
-
-
additional information
?
-
two-step reaction mechanism for the amylase activity, i.e. 1-4 bond breakage, and isomerization, i.e. 1-6 bond formation, which occur in the same catalytic pocket
-
-
-
additional information
?
-
-
The activities of the isozymes BEi, BEIIa and BEIIb with a linear glucan amylose decrease with a decrease in the molar size of amylose, and no activities of BEIIa and BEIIb are found when the degree of polymerization of amylose is lower than at least 80, whereas BEI had an activity with amylose of a degree of polymerization higher than approximately 50. Isoform BEIIb almost exclusively transfers chains with degree of polymerization of 7 and 6 while isoform BEIIa forms a wide range of short chains with degree of polymerization of 6 to around 15 from outer chains of amylopectin and amylose. Isoform BEI forms a variety of short chains and intermediate chains of a degree of polymerization below 40 by attacking not only outer chains but also inner chains of branched glucan. Isoforms BEIIa or BEIIb can only scarcely or can not attack inner chains, respectively
-
-
-
additional information
?
-
-
interactions between rice SS isozymes and BE isozymes in the synthesis of unprimed glucan, overview
-
-
-
additional information
?
-
-
interactions between rice starch synthase isozymes and branching enzyme isozymes in the synthesis of unprimed glucan, overview
-
-
-
additional information
?
-
-
differences in properties between isoforms of SBE are not the main factors that determine the polymodal distribution of branch lengths in amylopectin
-
-
-
additional information
?
-
a minimal chain length of ten glucosyl units is required for the donor substrate to be recognized by Rhodothermus marinus branching enzyme that essentially produces branches with a degree of polymerization of 3-8. The enzyme preferentially creates new branches by intermolecular mechanism. Branched glucans define better substrates for the enzyme leading to the formation of hyper-branched particles of 30-70 nm in diameter, dextrins. The enzyme catalyzes an additional alpha-4-glucanotransferase activity
-
-
-
additional information
?
-
the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview
-
-
-
additional information
?
-
-
increased branching of the starch from maize and potato following BE treatment, short chains increase whereas the number of long chains decrease after BE treatment, molecular size distribution of branching enzyme-treated and control starch, granular structure, NMR analysis, overview
-
-
-
additional information
?
-
-
the enzyme forms SBE I and SBE II mainly branch the dextrins by intrachain branching
-
-
-
additional information
?
-
-
each branching enzyme isoform is involved in a different phase of glycogen synthesis
-
-
-
additional information
?
-
-
each branching enzyme isoform is involved in a different phase of glycogen synthesis
-
-
-
additional information
?
-
the Synechococcus elongatus enzyme specifically forms the branch linkages at the third glucose residue from the reducing end of the acceptor chain. The enzyme recognizes the location of branching points in its acceptor chain during their branching reaction
-
-
-
additional information
?
-
-
the Synechococcus elongatus enzyme specifically forms the branch linkages at the third glucose residue from the reducing end of the acceptor chain. The enzyme recognizes the location of branching points in its acceptor chain during their branching reaction
-
-
-
additional information
?
-
loop 220-245, named as catalytic loop, acts as a lid retaining the intermediate reaction product for subsequent transfer to a new a-1,6 position. The active site comprises two acidic catalytic residues, Glu183 and Asp354, the polarizer His10, aromatic gate-keepers Trp28, Trp270, Trp407, and Trp416 and the residue Tyr233
-
-
-
additional information
?
-
-
szubstrates are 0.5%, w/v of amylose, corn starch, potato starch, wheat starch and waxy corn starch, all gelatinized by a high temperature (121°C) and pressure (100 KPa) prior treatment. The recombinant enzyme shows the highest specificity to amylose. The recombinant enzyme can act on maize starch, and starch treated with TcGBE is observed to have a lower amylose content and molecular weight. Chain length distribution of amylopectin products by anion exchange chromatography
-
-
-
additional information
?
-
-
szubstrates are 0.5%, w/v of amylose, corn starch, potato starch, wheat starch and waxy corn starch, all gelatinized by a high temperature (121°C) and pressure (100 KPa) prior treatment. The recombinant enzyme shows the highest specificity to amylose. The recombinant enzyme can act on maize starch, and starch treated with TcGBE is observed to have a lower amylose content and molecular weight. Chain length distribution of amylopectin products by anion exchange chromatography
-
-
-
additional information
?
-
Multiple isoforms of starch branching enzyme-I exist in wheat. Lack of the major SBE-I isoform does not alter starch phenotype
-
-
-
additional information
?
-
-
no major difference in the amylose/amylopectin ratio is detectected by reducing the expression of SBE-I using antisense constructs
-
-
-
additional information
?
-
starch structure in the two accessions, overview
-
-
-
additional information
?
-
the glycogen branching enzyme from Vibrio vulnificus transfers short side chains (DP 3-5) significantly greater than any other bacterial glycogen branching enzyme. The N1-domain of the enzyme has a crucial role in the determination of the branching pattern of glycogen, degrees of polymerization in enzyme reaction products compared to enzymes from other origin, overview
-
-
-
additional information
?
-
-
the glycogen branching enzyme from Vibrio vulnificus transfers short side chains (DP 3-5) significantly greater than any other bacterial glycogen branching enzyme. The N1-domain of the enzyme has a crucial role in the determination of the branching pattern of glycogen, degrees of polymerization in enzyme reaction products compared to enzymes from other origin, overview
-
-
-
additional information
?
-
the glycogen branching enzyme from Vibrio vulnificus transfers short side chains (DP 3-5) significantly greater than any other bacterial glycogen branching enzyme. The N1-domain of the enzyme has a crucial role in the determination of the branching pattern of glycogen, degrees of polymerization in enzyme reaction products compared to enzymes from other origin, overview
-
-
-
additional information
?
-
-
the catalytic center is exclusively located in the central position of the enzyme
-
-
-
additional information
?
-
-
chain-length distribution and branch linkage frequence of the 3 isoenymes
-
-
-
additional information
?
-
-
the conserved Arg residue 384 plays an important role in the catalytic function but may not be directly involved in substrate binding
-
-
-
additional information
?
-
-
starch-branching enzyme and glycogen synthase work in a cyclically interdependent fashion
-
-
-
additional information
?
-
in absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
-
-
-
additional information
?
-
in absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
-
-
-
additional information
?
-
-
the enzyme performs branching of two linear alpha-(1,4)-D-glucans substrates of degrees of polymerization about 150 and 6000, product identification by NMR and gel filtration, determination of chain-length distributions and hydrodynamic volume distributions, interchain mechanism, overview
-
-
-
additional information
?
-
molecular weight distribution of starch, amylose and amylopectin, overview. SBE is the only enzyme that generates glucan branches, i.e. it is the only chain-stopping substance for branch growth, and as a consequence SBE has a significant effect on the final structure of the resulting starch
-
-
-
phosphorylated alpha-1,4-glucan
additional information
-
-
33P-labeled phosphorylated and 3H-end-labeled nonphosphorylated
formation of dual-labeled phosphorylated branched polysaccharides with an average degree of polymerization of 80 to 85
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Q6EAS5
glycogen branching enzyme GBE1 mutation causing equine glycogen storage disease IV.A C to A substitution at base 102 results in a tyrosine (Y) to stop (X) mutation in codon 34 of exon of exon 1. All 11 affected foals are homozygous for the X34 allele, all 16 control horses are homozygous for the Y34 allele. Poorly branched glycogen, abnormal polysaccharide accumulation, lack of measurable GBE1 enzyme activity and immunodetectable GBE1 protein, coupled with the present observation of abundant GBE1 mRNA in affected foals, are consistent with the nonsense mutation in the 699 amino acid GBE1 protein
-
-
-
additional information
?
-
-
the enzyme is responsible for the formation of the alpha-1,6 linkages in the glycogen molecule
-
-
-
additional information
?
-
-
a fatal form of glycogen storage disease IV affects Norwegian Florest Cat, in which striated muscles and the nervous system are primarily affected, while the liver remains unaffected. This form of GSD IV is caused by a 6.1-kb deletion that eliminates exon 12 of the feline GBE1 gene
-
-
-
additional information
?
-
-
each isoform of the Q-enzyme plays a distinct role in starch biosynthesis
-
-
-
additional information
?
-
-
differences in properties between isoforms of SBE are not the main factors that determine the polymodal distribution of branch lengths in amylopectin
-
-
-
additional information
?
-
Q93HU3
the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview
-
-
-
additional information
?
-
-
each branching enzyme isoform is involved in a different phase of glycogen synthesis
-
-
-
additional information
?
-
-
each branching enzyme isoform is involved in a different phase of glycogen synthesis
-
-
-
additional information
?
-
O04074
Multiple isoforms of starch branching enzyme-I exist in wheat. Lack of the major SBE-I isoform does not alter starch phenotype
-
-
-
additional information
?
-
-
no major difference in the amylose/amylopectin ratio is detectected by reducing the expression of SBE-I using antisense constructs
-
-
-
additional information
?
-
A0A0F6QDD4
starch structure in the two accessions, overview
-
-
-
additional information
?
-
Q7MG90
the glycogen branching enzyme from Vibrio vulnificus transfers short side chains (DP 3-5) significantly greater than any other bacterial glycogen branching enzyme. The N1-domain of the enzyme has a crucial role in the determination of the branching pattern of glycogen, degrees of polymerization in enzyme reaction products compared to enzymes from other origin, overview
-
-
-
additional information
?
-
-
the glycogen branching enzyme from Vibrio vulnificus transfers short side chains (DP 3-5) significantly greater than any other bacterial glycogen branching enzyme. The N1-domain of the enzyme has a crucial role in the determination of the branching pattern of glycogen, degrees of polymerization in enzyme reaction products compared to enzymes from other origin, overview
-
-
-
additional information
?
-
Q7MG90
the glycogen branching enzyme from Vibrio vulnificus transfers short side chains (DP 3-5) significantly greater than any other bacterial glycogen branching enzyme. The N1-domain of the enzyme has a crucial role in the determination of the branching pattern of glycogen, degrees of polymerization in enzyme reaction products compared to enzymes from other origin, overview
-
-
-
additional information
?
-
-
starch-branching enzyme and glycogen synthase work in a cyclically interdependent fashion
-
-
-
additional information
?
-
O24421
in absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu2+
Mg2+
Ni2+
Zn2+
Ca2+
the cation has no effect on the activity. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min
Cu2+
maximum inhibition is observed, where about 40% of the activity is retained. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min
Mg2+
the cation has no effect on the activity. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min
Ni2+
-
upregulates the GBE1 gene both in vitro and in vivo, in PW cell line, liver, lung, kidney and spleen. Ni2+ mimics hypoxia, GBE1 is upregulated by hypoxia
Zn2+
about 70% activity retained. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R)-2-[(4-methoxyphenyl)methyl]-3,3-dimethylpiperidin-4-one
-
40.5% inhibition at 2 mM
-
(3R)-N-[(2S)-1-hydroxypropan-2-yl]-5-oxo-1-(propan-2-yl)pyrrolidine-3-carboxamide
-
-
-
(3S,5S)-5-[hydroxy(methoxy)methyl]pyrrolidin-3-ol
-
35.2% inhibition at 3 mM
-
(4R)-4-(azepan-1-yl)-1-[(1H-benzimidazol-2-yl)methyl]piperidin-3-ol
-
-
-
1'-(propan-2-yl)-3,3a,5,6,7,7a-hexahydrospiro[imidazo[4,5-c]pyridine-4,4'-piperidine]
-
-
-
1'H-spiro[piperidine-4,2'-quinazolin]-4'(3'H)-one
-
37.5% inhibition at 1 mM
-
1-(1H-benzimidazol-2-yl)ethan-1-amine
-
36.5% inhibition at 3 mM
-
1-(1H-benzimidazol-6-yl)-2-methylpropan-2-amine
-
36.5% inhibition at 2 mM
-
1-(3-methoxyphenyl)-2-[[(pyridin-3-yl)methyl]amino]ethan-1-ol
-
-
-
1-acetyl-2-hydroxy-4-methyl-2,5-dihydro-1H-pyrrole-3-carbonitrile
-
-
-
1-benzyl-5-oxopyrrolidine-3-carboxylic acid
-
37.6% inhibition at 2 mM
-
2-([[5-hydroxy-4-(hydroxymethyl)-6-methylpyridin-3-yl]methyl]sulfanyl)pyrimidin-4(1H)-one
-
-
-
5-(piperazin-1-yl)[1,2]thiazolo[2,3-c]pyrimidin-8-ium
-
34.2% inhibition at 3 mM
-
5-oxo-1-(propan-2-yl)pyrrolidine-3-carboxylic acid
-
40.2% inhibition at 3 mM
-
Ca2+
the additon of 2.5 mM of Ca2+ slightly inhibits the enzyme
Co2+
the additon of 2.5 mM of Co2+ slightly inhibits the enzyme
Fe3+
enzymatic activity is abolished in the presence of Fe3+
methyl (6S)-5-methyl-4,5,6,7-tetrahydro-1H-imidazo[4,5-c]pyridine-6-carboxylate
-
-
-
Mg2+
the additon of 2.5 mM of Mg2+ slightly inhibits the enzyme
Mn2+
the additon of 2.5 mM of Mn2+ slightly inhibits the enzyme
N-[2-chloro-5-(trifluoromethyl)phenyl]triimidodicarbonic diamide
-
-
-
Urea
-
50% inhibition at 0.4 M, complete inhibition at 2 M. Up to 2 M, reversible inhibition
Zn2+
enzymatic activity is abolished in the presence of Zn2+
EDTA
enzymatic activity is abolished in the presence of EDTA
additional information
not inhibitory: ADP, ADP glucose, tunicamycin, castenospermine, nojirimycin, or acarbose
-
additional information
-
small molecule inhibitor identification, high throughput virtual screening and molecular docking
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
polyvinyl alcohol
-
dilution of purified enzyme with a glycine buffer, pH 8.5, containing 1.0 mM DTT, and 0.04% w/v polyvinyl alcohol 50000, produces a striking and significant increase in enzyme activity when diluted 1:2 to 1:10
starch synthase I
-
interaction between starch synthase I (SSI) and branching enzyme (BE) is established by stimulation of SSI activity with BE and by activation of the BE activity by SSI; interaction between starch synthase I (SSI) and branching enzyme (BE) is established by stimulation of SSI activity with BE and by activation of the BE activity by SSI
-
additional information
-
peak of activities at the 28th day post anthesis, higher activity in the cultivar with a high starch content
-
citrate
-
3.3fold activation at 0.3 M, enzyme form KBE1 and KBE2; activation
citrate
-
0.3 M, more than 3fold stimulation of activity of isoenzyme SBE2, no effect on activity of isoenzyme SBE1
citrate
-
in the presence of 0.1 M citrate, the activity of the active enzyme increases
dithiothreitol
addition of dithiothreitol results in an increase in the branching enzyme activity up to 2.4fold at concentrations greater than 1 mM. This activation is not observed if idoacetamide is simultaneously present.
dithiothreitol
-
dilution of purified enzyme with a glycine buffer, pH 8.5, containing 1.0 mM DTT, and 0.04% w/v polyvinyl alcohol 50000, produces a striking and significant increase in enzyme activity when diluted 1:2 to 1:10
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00018
amylose
-
amylose AS-1160, degree of polymerization of approximately 6,510, isoform BEI, pH 7.5, 30°C
0.0009
amylose
-
amylose AS-1160, degree of polymerization of approximately 6,510, isoform BEI, pH 7.5, 30°C
0.0012
amylose
-
amylose AS-1160, degree of polymerization of approximately 6,510, isoform BEI, pH 7.5, 30°C
10
amylose
-
reduced amylose of an average chain-length 405, enzyme isoenzyme BE IIa
11
amylose
-
reduced amylose of an average chain-length 405, enzyme isoenzyme BE IIb
additional information
additional information
-
Km-value for amylose, enzyme form KBE1: 1.27 mg/ml. Km-value for amylose, enzyme form KBE2: 0.74 mg/ml
-
additional information
additional information
-
Km-value for amylose, enzyme form WBE-IB: 0.11 mg/ml, Km-value for amylose, enzyme form WBE-IAD: 0.3 mg/ml, Km-value for amylose, enzyme form WBE-II: 0.65 mg/ml
-
additional information
additional information
-
Km-value for amylose, isoenzyme SBE2: 1.27 mg/ml. Km-value for amylose, isoenzyme SBE1: 0.46 mg/ml
-
additional information
additional information
-
Km value of the chimeric enzyme (1Na/2Nb)-II is 0.63 mg/ml. The Km value of D15A-PvSBE2 is 1.3 mg/ml, 1.52 mg/ml for D15E-PvSBE2, 1.57 mg/ml for R28A-PvSBE2, 1.55 mg/ml for R28K-PvSBE2 and 1.59 mg/ml for H24A-PvSBE2.
-
additional information
additional information
enzyme reaction kinetics with different branched or unbranched alpha-glucans of controlled structure; Km-value for amylose is 0.7 mg/ml, 30°C, pH 7.0
-
additional information
additional information
Km-value for amylose is 0.56 mg/ml, wild-type, 25°C, pH 7.0. Km value for mutant lacking N1 domain is 0.33 mg/ml
-
additional information
additional information
-
Km-value for amylopectin is 3.0 mg/ml for isoform BEI, 2.7 mg/ml for isoform BEIIa, and 0.9 mg/ml for isoform BEIIb, 30°C, pH 7.0
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.001
-
be1-1 be2-1, T-DNA insertion double mutant in enzyme BE1 and BE2, in vitro assay of starch-branching enzyme activity; be2-2 (DSA16), T-DNA insertion mutant line for BE2, in vitro assay of starch-branching enzyme activity
0.002
-
be2-1 be3-2, T-DNA insertion double mutant in enzyme BE2 and BE3, in vitro assay of starch-branching enzyme activity; be2-1 (EFH20), T-DNA insertion mutant line for BE2, in vitro assay of starch-branching enzyme activity
0.051
-
be1-1 be3-2, T-DNA insertion double mutant in enzyme BE1 and BE3, in vitro assay of starch-branching enzyme activity
0.082
-
be3-1 (N548089), T-DNA insertion mutant line for BE3, in vitro assay of starch-branching enzyme activity
0.096
-
be1-1 (DYK140), T-DNA insertion mutant line for BE1, in vitro assay of starch-branching enzyme activity
0.102
-
be3-2 (EQJ13), T-DNA insertion mutant line for BE3, in vitro assay of starch-branching enzyme activity
0.107
-
wild type enzyme, Col-0; wild type enzyme, Wassilewskija genetic background
0.13
-
be1-2 (N637880), T-DNA insertion mutant line for BE1, in vitro assay of starch-branching enzyme activity
10.7
purified recombinant enzyme, pH 7.5, 25°C, substrate amylose
28.5
-
mutant enzyme DELTA1-63, micromol Glc incorporated into alpha-D-glucan per min at 30°C
42
mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, pH 7.0, 25°C
47.3
Cyanobacterium sp.
purified recombinant His-tagged isozyme BE1, pH 7.0, 30°C
535.4
-
mutant enzyme DELTA1-83, micromol Glc incorporated into alpha-D-glucan per min at 30°C
951.4
Cyanobacterium sp.
purified recombinant His-tagged isozyme BE1, pH 7.0, 30°C
988.8
Cyanobacterium sp.
purified recombinant His-tagged isozyme BE1, pH 7.0, 30°C
additional information
additional information
-
the branching enzyme has a spesific actvity of 0.4 U/mg. Amylose is used as substrate. The methods defines one unit of branching enzyme activity as 1 micromol of alpha-1,6 linkages synthesized per minute.
additional information
the branching enzyme has a spesific actvity of 0.4 U/mg. Amylose is used as substrate. The methods defines one unit of branching enzyme activity as 1 micromol of alpha-1,6 linkages synthesized per minute.
additional information
-
specific activity on amylopectin 342.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RGG, iodine assay; specific activity on amylopectin 359.2 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GGR, iodine assay; specific activity on amylopectin 474.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, wild-type enzyme, iodine assay; specific activity on amylopectin 505.6 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RRG, iodine assay; specific activity on amylopectin less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GRR, iodine assay; specific activity on amylose 411.7 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RRG, iodine assay; specific activity on amylose 468.8 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GGR, iodine assay; specific activity on amylose 621.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, wild-type enzyme, iodine assay; specific activity on amylose 624.1 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RGG, iodine assay; specific activity on amylose less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GRR, iodine assay
additional information
specific activity on amylopectin 342.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RGG, iodine assay; specific activity on amylopectin 359.2 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GGR, iodine assay; specific activity on amylopectin 474.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, wild-type enzyme, iodine assay; specific activity on amylopectin 505.6 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RRG, iodine assay; specific activity on amylopectin less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GRR, iodine assay; specific activity on amylose 411.7 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RRG, iodine assay; specific activity on amylose 468.8 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GGR, iodine assay; specific activity on amylose 621.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, wild-type enzyme, iodine assay; specific activity on amylose 624.1 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RGG, iodine assay; specific activity on amylose less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GRR, iodine assay
additional information
-
specific activity on amylopectin 342.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RGG, iodine assay; specific activity on amylopectin 359.2 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GGR, iodine assay; specific activity on amylopectin 505.6 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RRG, iodine assay; specific activity on amylopectin 538.0 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, wild-type enzyme, iodine assay; specific activity on amylopectin 556.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant CTT Dr, iodine assay; specific activity on amylopectin less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GRR, iodine assay; specific activity on amylose 404.2 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, wild-type enzyme, iodine assay; specific activity on amylose 411.7 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RRG, iodine assay; specific activity on amylose 442.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant CTT Dr, iodine assay; specific activity on amylose 468.8 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GGR, iodine assay; specific activity on amylose 624.1 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RGG, iodine assay; specific activity on amylose less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GRR, iodine assay
additional information
specific activity on amylopectin 342.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RGG, iodine assay; specific activity on amylopectin 359.2 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GGR, iodine assay; specific activity on amylopectin 505.6 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RRG, iodine assay; specific activity on amylopectin 538.0 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, wild-type enzyme, iodine assay; specific activity on amylopectin 556.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant CTT Dr, iodine assay; specific activity on amylopectin less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GRR, iodine assay; specific activity on amylose 404.2 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, wild-type enzyme, iodine assay; specific activity on amylose 411.7 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RRG, iodine assay; specific activity on amylose 442.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant CTT Dr, iodine assay; specific activity on amylose 468.8 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GGR, iodine assay; specific activity on amylose 624.1 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RGG, iodine assay; specific activity on amylose less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GRR, iodine assay
additional information
-
20.8 U/mg for amylose, 1 U = decrease of one absorbance unit at 660 nm at 30°C; 2.5 U/mg for amylopectin, 1 U = decrease of one absorbance unit at 660 nm at 30°C
additional information
-
12.258 U/mg for amylose, 1 U = 1% decrease of the absorbance/min; 1.229 U/mg for amylopectin, 1 U = 1% decrease of the absorbance/min
additional information
-
the chimeric (1Na/2Nb)II enzyme has a specific activity of 13 U/mg in the presence of 0.1 M citrate or 6.1 U/mg in the absence of citrate. The iodine-staining assay is performed by monitoring the decrease in absorbance at 660 nm for amylose, one unit of enzyme activity is defined as the amount of enzyme yielding a decrease in A660 of 0.1 per minute at 30°C.
additional information
-
0.29 U/mg for the crude cell extract, 1 U = change in the absorbance of 1 unit; 1.00 U/mg for the purified enzyme , 1 U = change in the absorbance of 1 unit
additional information
0.252 U/mg for the crude enzyme, 1 U = decrease of 1.0 units of absorbance per minute; 6.402 U/mg for the purified enzyme, 1 U = decrease of 1.0 units of absorbance per minute
additional information
-
0.252 U/mg for the crude enzyme, 1 U = decrease of 1.0 units of absorbance per minute; 6.402 U/mg for the purified enzyme, 1 U = decrease of 1.0 units of absorbance per minute
additional information
-
186 U/mg after ammonium sulfate fractionation, 1 unit = incorporation of 1 nmol glucose into the ethanol-insoluble glucan polymer per minute; 39 U/mg for crude extract, 1 unit = incorporation of 1 nmol glucose into the ethanol-insoluble glucan polymer per minute; 483 U/mg after DEAE fast flow, 1 unit = incorporation of 1 nmol glucose into the ethanol-insoluble glucan polymer per minute; 744 to 4001 U/mg for enzyme after purification, 1 unit = incorporation of 1 nmol glucose into the ethanol-insoluble glucan polymer per minute
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
8.5
7
all assays are perfomed at 30°C with 0.5 microM of protein
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
pH 5.0: about 40% of maximal activity, pH 9.0: about 50% of maximal activity
7 - 9
8 - 10
Cyanobacterium sp.
isozyme BE2 shows nearly half of the maximum activity at pH 10.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
34
37
50
30
incubated at different temperatures for 30 min at pH 7 in 50 mM citrate buffer
50
the branching enzyme is optimally active at 50°C and pH 7
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 30
the enzyme displays excellent cold adaptation over a low temperature range of 10-30°C, retaining over 85% of its relative activity
22 - 45
-
22°C: about 50% of maximal activity, 45°C: about 60% of maximal activity
30 - 40
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
of transgenic rice, expression of Escherichia coli branching enzyme in caryopses of transgenic Oryza sativa
-
enzyme produced by pure culture manufacture of a genetically modified strain of Bacillus subtilis containing a synthetic gene coding for glycogen BE from Rhodothermus obamensis
additional information
specific expression of starch-branching enzymes IIb; specific expression of starch-branching enzymes IIb
-
developing hexaploid. Enzyme form WBE-II is expressed at a constant level through mid and late endosperm development. Enzyme forms WBE-IAD and WBE-IB are preferentially expressed in late endosperm development
starch branching enzyme IIb is expressed at low levels in the endosperm compared to other cereals and encoded at a non-syntenic locus
SBE enzyme activity in endosperm of accession Y59 is obviously higher than that in Y63 at early developmental stag. Accumulation rates of both amylopectin and starch are significantly correlated to the SBE activities in the two accessions. Expression of SBE I in Y59 is higher than that in Y63 from 5 days after pollination to day 23. The higher starch and amylopectin contents of Y59 than that of Y63 maybe result from that Y59 has and earlier initiating accumulation time and a greater accumulation rate
-
activity and expression level of branching enzyme 1 and branching enzyme 3 are lower at 29°C/35°C than those at 22°C/28°C. The decreased activity of starch branching enzyme reduces the branching frequency of the branches of amylopectin, which results in the increased amount of long chains of amylopectin of endosperm in rice grain at high temperature
-
developing seeds contain several isoforms. The major forms are KBE1 and KBE2
endosperm and embryo, activity exhibits a late onset with a peak of transcription at around 22 days after pollination
-
isoform SBE A mRNA is expressed at very low levels in tubers. Expression of isoform SBE B increases with tuber size and is greatest in the largest tubers
additional information
the two genes encoding starch-branching enzymes IIa and IIb are differentially expressed; the two genes encoding starch-branching enzymes IIa and IIb are differentially expressed
additional information
the two genes encoding starch-branching enzymes IIa and IIb are differentially expressed; the two genes encoding starch-branching enzymes IIa and IIb are differentially expressed
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoform SBE A is found predominantly in the soluble phase of the tuber extracts, indicating a stromal location within the plastid
additional information
-
more than 95% of the recombinant enzyme is present within the cells as insoluble but catalytically active aggregate. Heat treatment of the aggregate suspension at 70°C results in about 30% solubilization of the enzyme activity
-
-
the purified full-length enzyme is poorly soluble and forms aggregates, which are inactive, at concentrations above 1 mg/ml. In contrast, the truncated form can be concentrated to 6 mg/ml without a visible sign of aggregation or loss of activity on concentration
-
-
SBE2 is present in the soluble fraction, SBE1 is associated with the starch granule fraction
-
in the soluble fraction, the amount of SBE IIa protein is two to three fold higher than SBIIb
-
-
SBE2 is present in the soluble fraction, SBE1 is associated with the starch granule fraction
-
soluble isoforms of starch synthase and starch-branching enzyme also occur within starch granules in developing pea embryos
two to three fold more SBE IIb protein amount than SBE IIa
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli O139:H28 (strain E24377A / ETEC)
Escherichia coli O139:H28 (strain E24377A / ETEC)
Escherichia coli O139:H28 (strain E24377A / ETEC)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66000
Cyanobacterium sp.
x * 77262, sequence calculation of His-tagged isozyme BE3, x * 66000, recombinant His-tagged isozyme BE3, SDS-PAGE
69000
Cyanobacterium sp.
x * 78781, sequence calculation of His-tagged isozyme BE2, x * 69000, recombinant His-tagged isozyme BE2, SDS-PAGE
77000
77262
Cyanobacterium sp.
x * 77262, sequence calculation of His-tagged isozyme BE3, x * 66000, recombinant His-tagged isozyme BE3, SDS-PAGE
78200
1 * 81030, sequence calculaiton, 1 * 78200, recombinant enzyme, SDS-PAGE
78781
Cyanobacterium sp.
x * 78781, sequence calculation of His-tagged isozyme BE2, x * 69000, recombinant His-tagged isozyme BE2, SDS-PAGE
80000
81030
1 * 81030, sequence calculaiton, 1 * 78200, recombinant enzyme, SDS-PAGE
82000
84000
85000
86060
theoretical mass of the recombinant branching enzyme with N-terminal S-tag and C-terminal His-tag
87000
88000
Cyanobacterium sp.
x * 94125, sequence calculation of His-tagged isozyme BE1, x * 88000, recombinant His-tagged isozyme BE1, SDS-PAGE
94125
Cyanobacterium sp.
x * 94125, sequence calculation of His-tagged isozyme BE1, x * 88000, recombinant His-tagged isozyme BE1, SDS-PAGE
558000
TK1436deltaH protein, gel filtration on a Superdex 200 HR 10/30 column
80000
gel filtration chromatography using Superdex 200 HR10/30 column
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
Cyanobacterium sp.
x * 77262, sequence calculation of His-tagged isozyme BE3, x * 66000, recombinant His-tagged isozyme BE3, SDS-PAGE; x * 78781, sequence calculation of His-tagged isozyme BE2, x * 69000, recombinant His-tagged isozyme BE2, SDS-PAGE; x * 94125, sequence calculation of His-tagged isozyme BE1, x * 88000, recombinant His-tagged isozyme BE1, SDS-PAGE
?
-
x * 77262, sequence calculation of His-tagged isozyme BE3, x * 66000, recombinant His-tagged isozyme BE3, SDS-PAGE; x * 78781, sequence calculation of His-tagged isozyme BE2, x * 69000, recombinant His-tagged isozyme BE2, SDS-PAGE; x * 94125, sequence calculation of His-tagged isozyme BE1, x * 88000, recombinant His-tagged isozyme BE1, SDS-PAGE
-
monomer
-
1 * 77000, enzyme KBE2, SDS-PAGE; 1 * 80000, enzyme KBE1, SDS-PAGE
monomer
-
1 * 100000, isoenzyme SBE1, SDS-PAGE; 1 * 81932, isoenzyme SBE2, calculation from nucleotide sequence; 1 * 82000, isoenzyme SBE2, SDS-PAGE; 1 * 88590, isoenzyme SBE1, calculation from nucleotide sequence
monomer
1 * 81030, sequence calculaiton, 1 * 78200, recombinant enzyme, SDS-PAGE
monomer
-
1 * 81030, sequence calculaiton, 1 * 78200, recombinant enzyme, SDS-PAGE
-
additional information
Cyanobacterium sp.
branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview; branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview; branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview
additional information
Cyanobacterium sp.
branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview; branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview; branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview
additional information
Cyanobacterium sp.
branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview; branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview; branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview
additional information
-
branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview; branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview; branching enzymes are multidomain proteins, GH13-type BEs contain (from N- to C-terminal end) carbohydrate binding module 48 (CBM48), catalytic domain (i.e. domain A), and domain C, isozyme domain structure comparisons, overview
-
additional information
-
six distinct oligosaccharide binding sites on the surface of the branching enzyme, most of which surround the edge of the beta-barrel domain and are quite far from the active site
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
enzyme contains 0.03 mg of carbohydrate in 1 mg of enzyme protein
phosphoprotein
proteolytic modification
phosphoprotein
native and recombinant maize SBEIIb are used as substrates for amyloplast protein kinases to identify phosphorylation sites on the protein, bioinformatics, site-directed mutagenesis, and mass spectrometry identify three phosphorylation sites at Ser residues: Ser649, Ser286, and Ser297. Ca2+-dependent protein kinases from amyloplasts, termed K1, responsible for Ser649 and Ser286 phosphorylation, and K2, responsible for Ser649 and Ser297 phosphorylation. The Ser286 and Ser297 phosphorylation sites are conserved in all plant branching enzymes and are located at opposite openings of the 8-stranded parallel beta-barrel of the active site, which is involved with substrate binding and catalysis. Molecular dynamics simulation analysis indicates that phospho-Ser297 forms a stable salt bridge with Arg665, part of a conserved Cys-containing domain in plant branching enzymes. Ser649 conservation appears confined to the enzyme in cereals and is not universal, and is presumably associated with functions specific to seed storage
phosphoprotein
-
native and recombinant maize SBEIIb are used as substrates for amyloplast protein kinases to identify phosphorylation sites on the protein, bioinformatics, site-directed mutagenesis, and mass spectrometry identify three phosphorylation sites at Ser residues: Ser649, Ser286, and Ser297. Ca2+-dependent protein kinases from amyloplasts, termed K1, responsible for Ser649 and Ser286 phosphorylation, and K2, responsible for Ser649 and Ser297 phosphorylation. The Ser286 and Ser297 phosphorylation sites are conserved in all plant branching enzymes and are located at opposite openings of the 8-stranded parallel beta-barrel of the active site, which is involved with substrate binding and catalysis. Molecular dynamics simulation analysis indicates that phospho-Ser297 forms a stable salt bridge with Arg665, part of a conserved Cys-containing domain in plant branching enzymes. Ser649 conservation appears confined to the enzyme in cereals and is not universal, and is presumably associated with functions specific to seed storage
-
proteolytic modification
after removal of the transit peptide sequence the sbeI cDNA encodes a 762 amino acid-long mature protein
proteolytic modification
-
RBE4 is initially produced as a precursor protein of 841 amino acids, including a 53 residue transit peptide at the N-terminus
proteolytic modification
removal of the transit peptide yields a 746 amino acids-long mature protein
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of truncated branching enzyme mutant DELTA112 in complex with linear oligosaccharides maltoheptaose and maltohexaose, X-ray diffraction structure determination and analysis
-
hanging drop method, active N-terminally truncated form missing the first 107 amino acids
-
crystal structure of full-length protein at 2.33 A resolution. The enzyme contains four domains: N1 beta-sandwich, N2 beta-sandwich, a central (beta/alpha)8 domain that houses the catalytic site, and a C-terminal beta-sandwich. The N1 beta-sandwich, which is formed by the first 105 amino acids and superimposes well with the N2 beta-sandwich, has an influence in substrate binding in the amylase assay
determination of the crystal structure of branching enzyme I at a resolution of 1.9 A by molecular replacement using the Escherichia coli glycogen branching enzyme as a search model. Branching enzyme I is roughly ellipsoidal in shape with two globular domains that form a prominent groove proposed to serve as the alphha-polyglucan-binding site. Amino acid residues Asp344 and Glu399, postulated to play an essential role in catalysis, are located at a central cleft in the groove
-
mutant E399Q in complex with maltopentaose at a resolution of 2.2 A. Maltopentaose binds to a hydrophobic pocket formed by the N-terminal helix, carbohydrate-binding module 48, and alpha-amylase domain. In addition, glucose moieties can be observed at molecular surfaces on the N-terminal helix alpha2 and carbohydrate-binding module 48
in the native state and in complex with glucose and substrate mimetics, to 2.4 A, 2.9 A, and 1.9 A resolution, respectively. The structure encompasses a distorted (beta/alpha)7-barrel juxtaposed to a C-terminal alpha-helical domain, which also participates in the formation of the active-site cleft. The active site comprises two acidic catalytic residues, Glu183 and Asp354, the polarizer His10, aromatic gate-keepers Trp28, Trp270, Trp407, and Trp416 and the residue Tyr233, which is fully conserved among GH13- and GH57-type branching enzymes
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9.5
purified recombinant His-tagged enzyme, fairly stable over the broad pH range, retaining more than 80% of its activity
736135
7 - 9.5
-
4°C, 16 h, less than 10% loss of activity, enzyme form KBE1 and KBE2; stable
636945
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 45
-
no apparent inactivation up to 30°C, about 10% loss of activity at 35°C, about 90% loss of enzyme activity at 50°C
10 - 30
pre-incubation of the enzyme for 2 h at different temperatures, following enzyme assay is conducted at 30°C. About 80% activity is retained after pre-incubation at 37°C and 45°C
10 - 40
purified recombinant enzyme, the enzyme retains about 80% of its activity at 40°C for 30 min, the enzyme displays excellent cold adaptation over a low temperature range of 10-30°C, retaining over 85% of its relative activity within this range
35
40
45
50 - 55
in the absence of substrates the branching enzyme is stable at 50°C for more than 6 h. At 55°C the half-life of the branching enzyme is 50 min.
50
60 - 65
after 1 h incubation at 60°C fully active, after 1 h incubation at 65°C only 80% residual activity
70
-
pH 7.0, 30 min, 10% loss of the soluble enzyme form, 50% loss of the insoluble enzyme form
75
-
fully active after 100 min incubation, half-life time at 80°C 73.7 min, half-life time at 85°C 16.7 min
90
the protein is stable up to 90°C, the activity decreases gradually during the incubation at 100°C
additional information
35
Cyanobacterium sp.
purified recombinant His-tagged isozyme BE3, stable up to
40
Cyanobacterium sp.
purified recombinant His-tagged isozyme BE1, stable up to
45
Cyanobacterium sp.
purified recombinant His-tagged isozyme BE2, stable up to
45
with a direct enzyme assay at 45°C the enzyme retains about 45% activity
additional information
-
the activity is lost after incubation at 50°C for 30 min
additional information
-
when the enzymes are maintained for 15 min at various temperatures ranging from 30°C to 60°C, more than 80% of the original activity was retained up to 47.5°C for PvSBE2, up to 40°C for D15A- and D15E-PvSBE2, up to 42.5°C for R28A- and H24A-PvSBE2, and up to 45°C for R28K-PvSBE2.
additional information
high thermal tolerance even at boiling temperatures
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable protein even at high concentrations of chaotropic agents
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM glycylglycine buffer, pH 8.0, 5 mM mercaptoethanol, 1 mM EDTA, 0.02% NaN3, 25% glycerol
-
4°C, 10 mM Tris/HCl buffer, pH 7.0, 15 mM mercaptoethanol, stable for several months
-
addition of 0.04% (w/v) polyvinyl alcohol 50 K and 1 mM dithiothreitol to the glycine buffer, pH 8.4, leads to long-term stability and
-
higher yields of both starch synthase and starch branching enzyme, due to activation of inactive enzymes
-
the TK1436 protein shows rapid degradation within 2 to 3 days of storage at 4°C, while the TK1436deltaH protein is stable unter the same conditions
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isozymes
about 19.0 to 101.9fold after Sephacryl S-200 gel filtration and Q2-sepharose anion exchange chromatography
-
ammonium sulfate, Q-Sepharose column, ultrafiltration, gel filtration with Superdex 200 column, native polyacrylamide gel elektrophoresis
-
chimeric and N-terminal truncated enzymes: DEAE-Sepharose Cl6B column, Bio-Gel P-200 and Gigapite column all at 4°C and pH 7.5. Site-directed mutant enzymes: chelating Sepharose FF column and DEAE-Sepharose CL-6B column, all at 4°C.
-
His tag affinity chromatography
HitrapQ HP anion exchange column
Phenyl Sepharose 6 Fast Flow column and Superdex 200 gel filtration column
recombinant His-tagged isozyme BE1 from Escherichia coli by nickel affinity chromatography, gel filtration, and ultrafiltration; recombinant His-tagged isozyme BE2 from Escherichia coli by nickel affinity chromatography, gel filtration, and ultrafiltration; recombinant His-tagged isozyme BE3 from Escherichia coli by nickel affinity chromatography, gel filtration, and ultrafiltration
Cyanobacterium sp.
recombinant His-tagged isozymes rBE2 and rBE3 from Escherichia coli strains by nickel affinity chromatography
-
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complete cDNA sequence for the wild-type gene and the nonsense mutation in which a C to A substitution at base 102 results in a tyrosine (Y) to stop (X) mutation in codon 34 of exon of exon 1
expressed in Escherichia coli Bl21-CodonPlus(DE3)-RIL and pET21a(+)
expression in Bacillus subtilis
expression in Escherichia coli
expression in Escherichia coli BL21
expression in Escherichia coli, chimeric enzymes consisting of part mBE I and mBE II
-
expression in Escherichia coli, full-length enzyme and a truncated enzyme form missing the first 107 amino acids
-
expression in Escherichia coli, glycogen branching enzyme gene existing in tandem with the glycogen debranching enzyme
-
expression in Escherichia coli. Multiple forms of the enzyme exist which differ mainly in the length of a polyglutamic acid repeat at the C-terminus of the protein, SBE A1 to SBE A-6. Expression of an antisense SBE A RNA in transgenic potato
-
expression in mosquito C6/36 cells; expression in mosquito C6/36 cells
expression in Saccharomyces cerevisiae, each of the three isoforms is functional in yeast cells
-
expression of Escherichia coli branching enzyme in caryopses of transgenic Oryza satica results in amylopectin with an increased degree of branching. Expression of Escgerichia coli glgB in rice results in an increase in the short-chain fractions with DP between 6 and 10, which should have a significant effect on retrogradation
-
gene gkgB, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene glgB, functional recombinant expression of the bacterial enzyme in Arabidopsis thaliana be2 be3 double mutant leaves, ecotype WS, which is devoid of BE activity and consequently free of starch. The synthesis of a water-insoluble, partly crystalline, amylose-containing starch-like polyglucan is restored in GlgB-expressing transgenic plants, morphology of purified insoluble and soluble polyglucans, phenotype, overview
gene nbrc_glgB1, functional recombinant expression of N-terminally His-tagged isozyme BE1 in Escherichia coli; gene nbrc_glgB2, functional recombinant expression of His-tagged isozyme BE2 in Escherichia coli; gene nbrc_glgB3, functional recombinant expression of His-tagged isozyme BE3 in Escherichia coli
Cyanobacterium sp.
gene RmGBE, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21
gene SBE I, DNA and amino acid sequence determination and analysis of SBE I from two accessions, Y59 and Y63, genetic structure, sequence comparisons and phylogenetic analysis, enzyme expression analysis by real-time quantitative PCR
gene Sbe2a, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
gene TcGBE, recombinant expression in Escherichia coli strain BL21(DE3)
-
isolation of a cDNA encoding a granule-bound 152-kilodalton starch-branching enzyme, a non-full-length cDNA clone
-
recombinant expression of His-tagged isozymes rBE2 and rBE3 in Escherichia coli strain BL21(DE3) and in strain DELTAglgCAP with BL21(DE3) background
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recombinant overexpression of endogenaous enzyme SBEII in Solanum tuberosum. A complete cDNA of potato SBEII is unable to be propagated in Escherichia coli, therefore a complete but hybrid SBEII intragene containing a single intron to prevent bacterial translation is assembled from cDNA and genomic DNA fragments
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the barley clone encodes the complete mature SBEI but is truncated by approximately 150 bases at the 5'-end
the gene encoding the branching enzyme from Anaerobranca gottschalkii is fused with a twin arginine translocation protein secretory-pathway-dependent siganl sequence from Escherichia coli and expressed in Staphylococcus carnosus
transformed to Agrobacterium tumefaciens EHA 105, generation of transgenic Oryza sativa, expression in Escherichia coli AD494
two closely related cDNAs encode starch branching enzyme from Arabidopsis thaliana
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in mutants with suppression of expression SBE IIa; in mutants with suppression of expression SBE IIb or with concominant reduction in SBE IIb
lower expression in amylose-extender mutant of rice
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA1-112
DELTA1-63
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the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, mutant enzyme has a pattern of transferred chains, 10-20
DELTA1-83
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the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, mutant enzyme has a pattern of transferred chains, 10-20
truncated enzyme form missing the first 107 amino-
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the purified full-length enzyme is poorly soluble and forms aggregates, which are inactive, at concentrations above 1 mg/ml. In contrast, the truncated form can be concentrated to 6 mg/ml without a visible signs of aggregation or loss of activity on concentration
Y300F
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mutant enzyme shows 25% of the wild-type activity, no effect on Km-value, heat stability is lowered significantly compared to that of the wild-type enzyme, lower relative activity at elevated temperatures compared to wild-type enzyme
D270A
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mutant with about 10% relative enzyme activity compared to wild-type enzyme
E399A
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mutant with about 5% relative enzyme activity compared to wild-type enzyme
G468D
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mutant with about 95% relative enzyme activity compared to wild-type enzyme
R342A
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mutant with about 15% relative enzyme activity compared to wild-type enzyme
Y235A
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mutant with about 15% relative enzyme activity compared to wild-type enzyme
D15A
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D15A-PvSBE2 enzyme shows 13.1% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value.
D15E
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D15E-PvSBE2 enzyme shows 31.3% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value.
H24A
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H24A-PvSBE2 enzyme shows 38.3% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value.
R28A
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R28A-PvSBE2 enzyme shows 10.7% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value.
R28K
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R28K-PvSBE2 enzyme shows 93.5% of the specific activity of the wild type enzyme.
E513D
site-directed mutagenesis, the mutant shows a much lower activity compared to wild-type enzyme mSBEIIa
R363K
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme mSBEIIa
R456K
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme mSBEIIa
S349F
site-directed mutagenesis, creates an additional binding site for glucose, the mutant shows a much lower activity compared to wild-type enzyme mSBEIIa
Y352F
site-directed mutagenesis, , the mutant shows a much lower activity compared to wild-type enzyme mSBEIIa
additional information
DELTA1-112
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truncated enzyme transferrs a greater amount of longer chains than the wild-type enzyme
DELTA1-112
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the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, the mutant enzyme DELTA1-112 transfers a greater propertion of chains with higher degree of polymerization, 15-20
additional information
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be1-1 be2-1, T-DNA insertion double mutant in enzyme BE1 and BE2. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.; be1-1 be3-2, T-DNA insertion double mutant in enzyme BE1 and BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.; be1-1 (DYK140), T-DNA insertion mutant line for BE1. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.; be1-2 (N637880), T-DNA insertion mutant line for BE1. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.; be2-1 be3-2, T-DNA insertion double mutant in enzyme BE2 and BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type. The be2-1 be3-2 double mutant is free of starch, coupled with an accumulation of very high levels of water-soluble glucans, that are not observable in other lines. Moreover, this double mutant displays a lower growth rate, a pale color and a general wilting of the inflorescence.; be2-1 (EFH20), T-DNA insertion mutant line for BE2. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.; be2-2 (DSA16), T-DNA insertion mutant line for BE2. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.; be3-1 (N548089), T-DNA insertion mutant line for BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.; be3-2 (EQJ13), T-DNA insertion mutant line for BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.
additional information
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production of highly branched amylopectin and amylose from rice starch in a multistep procedure using several different enzymes, for braching of amylose, the Bacillus subtilis 168 branching enzyme is used, analysis of the resulting structural changes, overview
additional information
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production of highly branched amylopectin and amylose from rice starch in a multistep procedure using several different enzymes, for braching of amylose, the Bacillus subtilis 168 branching enzyme is used, analysis of the resulting structural changes, overview
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additional information
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enzyme overexpression results in decrease cell proliferation when treated by deltamethrin
additional information
enzyme overexpression results in decrease cell proliferation when treated by deltamethrin
additional information
enzyme overexpression results in decrease cell proliferation when treated by deltamethrin
additional information
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CT Dg, truncated at 3' end; GGR, construction of chimeric genes, with C-domain of GBE of Deinococcus radiodurans; GRR, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus radiodurans; NT Dg, tuncated at 5' end; RGG, construction of chimeric genes, with N-domain of GBE of Deinococcus radiodurans; RRG, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus radiodurans
additional information
CT Dg, truncated at 3' end; GGR, construction of chimeric genes, with C-domain of GBE of Deinococcus radiodurans; GRR, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus radiodurans; NT Dg, tuncated at 5' end; RGG, construction of chimeric genes, with N-domain of GBE of Deinococcus radiodurans; RRG, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus radiodurans
additional information
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CTT Dr, tuncated at 3' end; GGR, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus geothermalis; GRR, construction of chimeric genes, with N-domain of GBE of Deinococcus geothermalis; RGG, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus geothermalis; RRG, construction of chimeric genes, with C-domain of GBE of Deinococcus geothermalis
additional information
CTT Dr, tuncated at 3' end; GGR, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus geothermalis; GRR, construction of chimeric genes, with N-domain of GBE of Deinococcus geothermalis; RGG, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus geothermalis; RRG, construction of chimeric genes, with C-domain of GBE of Deinococcus geothermalis
additional information
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CTT Dr, tuncated at 3' end; GGR, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus geothermalis; GRR, construction of chimeric genes, with N-domain of GBE of Deinococcus geothermalis; RGG, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus geothermalis; RRG, construction of chimeric genes, with C-domain of GBE of Deinococcus geothermalis
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additional information
concominant reduction in SBE IIb with suppression of SBE IIa; SBE IIa-/SBE IIb-, transgenic line with suppressed SBE IIb and suppressed SBE IIa; SBE IIa-/SBE IIb-, transgenic line with suppressed SBE IIb and suppressed SBE IIa; SBE IIa-, transgenic line with suppressed SBE IIa; SBE IIb-, transgenic line with suppressed SBE IIb; suppression of SBE IIa with concominant reduction in SBE IIb
additional information
concominant reduction in SBE IIb with suppression of SBE IIa; SBE IIa-/SBE IIb-, transgenic line with suppressed SBE IIb and suppressed SBE IIa; SBE IIa-/SBE IIb-, transgenic line with suppressed SBE IIb and suppressed SBE IIa; SBE IIa-, transgenic line with suppressed SBE IIa; SBE IIb-, transgenic line with suppressed SBE IIb; suppression of SBE IIa with concominant reduction in SBE IIb
additional information
a mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, shows about 30% decrease in specific activity
additional information
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a mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, shows about 30% decrease in specific activity
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additional information
construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2; construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2
additional information
construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2; construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2
additional information
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chimeric enzymes of PvSBE2: only one chimeric recombinat protein ((I Na/2Nb)-II) has enzyme actvity. It shows 6.1% of the specific activity of the wild type enzyme.; N-termial truncated enzyme of PvSBE2. Delta46-PvSBE2 has no branching enzyme activity.
additional information
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starch from tubers of enzyme overexpressing plants posses an increased degree of amylopectin branching, with more short chains of degree of polymerisation (DP) 6-12 and particularly of DP6. Construction of transgenic lines expressing a GRANULE-BOUND STARCH SYNTHASE (GBSS) RNAi, which exhibit post-transcriptional gene silencing of GBSS and reduced amylose content in the starch. Both transgenic modifications do not affect granule morphology but reduce starch peak viscosity. In starch from SBEII-overexpressing lines, the increased ratio of short to long amylopectin branches facilitates gelatinisation, which occurs at a reduced temperature (by up to 3°C) or lower urea concentration. In contrast, silencing of GBSS increases the gelatinisation temperature by 4°C, and starch requires a higher urea concentration for gelatinisation. In lines with a range of SBEII overexpression, the magnitude of the increase in SBEII activity, reduction in onset of gelatinisation temperature and increase in starch swollen pellet volume are highly correlated, consistent with reports that starch swelling is greatly dependent upon the amylopectin branching pattern. Amylose content in starch and thermal properties of tuber starch granules from potato tubers of a range of lines exhibiting silencing of GBSS or overexpressing SBEII, overview
additional information
recombinant TK1436 protein (amino acids [aa] 1 to 675) and a deletion derivative devoid of the C-terminal two-copy helix-hairpin-helix (HhH)2 motif (TK1436deltaH, aa 1 to 562)
additional information
construction of domain-truncated (N1 and N) and N1-domain-swapped (with VvGBE N1 replacing the counter part of Escherichia coli GBE) mutants. The truncation mutants synthesize branched products with a greatly reduced proportion of short chains compared to the wild-type. The swapping mutant exhibit a branching pattern of the short chain region similar to that of the ewild-type enzyme
additional information
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construction of domain-truncated (N1 and N) and N1-domain-swapped (with VvGBE N1 replacing the counter part of Escherichia coli GBE) mutants. The truncation mutants synthesize branched products with a greatly reduced proportion of short chains compared to the wild-type. The swapping mutant exhibit a branching pattern of the short chain region similar to that of the ewild-type enzyme
additional information
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construction of domain-truncated (N1 and N) and N1-domain-swapped (with VvGBE N1 replacing the counter part of Escherichia coli GBE) mutants. The truncation mutants synthesize branched products with a greatly reduced proportion of short chains compared to the wild-type. The swapping mutant exhibit a branching pattern of the short chain region similar to that of the ewild-type enzyme
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additional information
generation of N- and C-terminally truncated enzyme mutants. Activities of kinases on wild-type and enzyme mutants, overview
additional information
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application of RNAi technology for improving amylose content in maize endosperm through the suppression of the ZmSBEIIa and ZmSBEIIb genes by hairpin SBEIIRNAi constructs. These SBEIIRNAi transgenes lead to the downregulation of ZmSBEII expression and SBE activity to various degrees and altered the morphology of starch granule; application of RNAi technology for improving amylose content in maize endosperm through the suppression of the ZmSBEIIa and ZmSBEIIb genes by hairpin SBEIIRNAi constructs. These SBEIIRNAi transgenes lead to the downregulation of ZmSBEII expression and SBE activity to various degrees and altered the morphology of starch granule
additional information
construction of enzyme point mutants by site-directed mutagenesis to change the chain-length distribution CLD by changing activity of enzyme SBE. The enzyme mutants show no or only a slight change in degree of polymerization of branched glucans
additional information
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generation of N- and C-terminally truncated enzyme mutants. Activities of kinases on wild-type and enzyme mutants, overview
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
unfolding equilibrium is a two-state process with no intermediates
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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RNAi technology is applied to suppress the expression of starch branching enzyme IIa and IIb and to increase amylose content in maize endosperm, and stably inherit high-amylose maize lines; RNAi technology is applied to suppress the expression of starch branching enzyme IIa and IIb and to increase amylose content in maize endosperm, and stably inherit high-amylose maize lines. Transgenic maize lines with amylose content of up to 55.89% are produced, which avoid the significant decreases in starch content and grain yield that occur in high-amylose starch branching enzyme IIb gene mutant
drug development
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small molecules with diverse scaffolds but similar three-dimensional structures show a similar biological effect. Deriving scaffolds from docking and similarity search is a successful design strategy for difficult targets
food industry
medicine
defining the molecular basis of equine glycogen storage disease IV will allow for accurate DNA testing and the ability to prevent occurence of this disease affecting American Quarter Horses and related breeds. A C to A substitution at base 102 results in a tyrosine (Y) to stop (X) mutation in codon 34 of exon of exon 1. All 11 affected foals are homozygous for the X34 allele, all 16 control horses are homozygous for the Y34 allele
nutrition
food industry
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analyzation and characterization of reaction products of branching enzymes from different sources for starch processing to synthesize the food ingredient, highly branched cyclic dextrin. The amount of short chains with a degree of polymerization of 6-8 is signifi cantly increased in the product of Bacillus cereus
food industry
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analyzation and characterization of reaction products of branching enzymes from different sources for starch processing to synthesize the food ingredient, highly branched cyclic dextrin; starch processiong to synthesize a food ingredient, highly branched cyclic dextrin
food industry
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analyzation and characterization of reaction products of branching enzymes from different sources for starch processing to synthesize the food ingredient, highly branched cyclic dextrin. The amount of short chains with a degree of polymerization of 6-8 is significantly increased in the product of Phaseolus vulgaris
food industry
involved in the synthesis of highly-branched cyclic dextrin, a dextrin food ingredient
food industry
addition of RmGBE to wheat bread results in a 26% increase in specific volume and a 38% decrease in crumb firmness in comparison with the control. Besides, the retrogradation of bread is significantly retarded along with the enzyme reaction. These properties make RmGBE highly useful in the food and starch industries
food industry
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addition of RmGBE to wheat bread results in a 26% increase in specific volume and a 38% decrease in crumb firmness in comparison with the control. Besides, the retrogradation of bread is significantly retarded along with the enzyme reaction. These properties make RmGBE highly useful in the food and starch industries
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nutrition
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production of very-high-amylose potato starch by simultaneous inhibition of SBE A and SBE B to a level of less than 1% using an antisense construct
nutrition
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cooking and textural characteristics of rice depend not only on the ratio of amylose, but also on the degree of amylopectin branching. Short chains of glucose with a degree of polymerization (DP)of 69 inhibit retrogradation. In vivo modification of starches using genetic engineering holds potential for both enhancing nutritional qualities and for obviating post-harvest modifications often necessary for utilization of this complex carbohydrate
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