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Information on EC 2.4.1.7 - sucrose phosphorylase and Organism(s) Bifidobacterium adolescentis and UniProt Accession Q84HQ2
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2.4.1.7 sucrose phosphorylaseIUBMB Comments
In the forward reaction, arsenate may replace phosphate. In the reverse reaction, various ketoses and L-arabinose may replace D-fructose.
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Word Map
- 2.4.1.7
- mesenteroides
- leuconostoc
-
bifidobacterium
- adolescentis
- phosphorylases
-
transglucosylation
- synthesis
- alpha-d-glucose
- laminaribiose
-
deglucosylation
- dextransucrase
-
pseudobutyrivibrio
- ruminis
- kojibiose
- medicine
- industry
The taxonomic range for the selected organisms is: Bifidobacterium adolescentis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
sucrose phosphorylase, unspase, lmspase, sucrose glucosyltransferase, 742spase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
disaccharide glucosyltransferase
-
-
-
-
sucrose glucosyltransferase
-
-
-
-
additional information
additional information
Q84HQ2
sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family
additional information
Q84HQ2
the enzyme belongs to the glycoside hydrolase family 13
additional information
Q84HQ2
the enzyme belongs to the glycoside hydrolase family 13
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
reaction mechanism, substrate access channel structure, catalytic active site residues are Asp192 and Glu232
Q84HQ2
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
a two-step catalytic mechanism: Asp192 is the catalytic nucleophile, Glu232 is the catalytic acid-base, and Asp290 functions as a transition state stabilizer. By forming a strong hydrogen bond with the hydroxyl groups at C2 and C3 of the glucosyl residue being transferred, the anionic side chain of Asp290 is suggested to provide selective stabilization to oxocarbenium ion-like transition states flanking the covalent alpha-glucosyl enzyme intermediate
Q84HQ2
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
sucrose:phosphate alpha-D-glucosyltransferase
In the forward reaction, arsenate may replace phosphate. In the reverse reaction, various ketoses and L-arabinose may replace D-fructose.
CAS REGISTRY NUMBER
COMMENTARY
9074-06-0
-
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
D-arabinose + alpha-D-glucose 1-phosphate
alpha-D-Glc(1-1)-beta-D-Ara + phosphate
Q84HQ2
-
-
-
?
D-arabitol + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
-
-
-
?
D-fructose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
D-fucose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
D-galactose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
D-glucose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
D-sorbitol + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
-
-
-
?
D-xylitol + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
high activity
-
-
?
D-xylose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
L-arabinose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
high activity
-
-
?
L-arabitol + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
high activity
-
-
?
L-fucose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
-
-
-
?
L-sorbose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
-
-
-
?
L-xylose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
resveratrol + alpha-D-glucose 1-phosphate
3-O-alpha-D-glucopyranosyl-(E)-resveratrol + phosphate
Q84HQ2
establishing of a resveratrol glycosylation method using the enzyme and IL AMMOENG 101 as the most effective cosolvent, solubility at pH 6.5 and 60°C, in the presence of 20% of different cosolvents and 1 M sucrose, overview
-
-
r
sucrose + (+)-catechin
D-fructose + (+)-catechin 3'-O-alpha-D-glucoside + (+)-catechin 3',5-O-alpha-D-diglucoside
Q84HQ2
activity of enzyme mutant Q345F
-
-
?
sucrose + (-)-epicatechin
D-fructose + (-)-epicatechin 3'-O-alpha-D-glucoside + (-)-epicatechin 5-O-alpha-D-glucoside + (-)-epicatechin 3',5-O-alpha-D-diglucoside
Q84HQ2
activity of enzyme mutant Q345F
-
-
?
sucrose + arsenate
D-fructose + alpha-D-glucose 1-arsenate
Q84HQ2
-
because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible
-
ir
sucrose + D-arabitol
pyridoxine + alpha-D-glucose 1-phosphate
Q84HQ2
-
-
-
r
sucrose + resveratrol
D-fructose + resveratrol 3-O-alpha-D-glucoside
Q84HQ2
activity of enzyme mutant Q345F
-
-
?
sucrose + D-glucose
D-fructose + 2-O-alpha-D-glucopyranosyl-alpha-D-glucopyranose
-
kojibiose i.e. 2-O-alpha-D-glucopyranosyl-alpha-D-glucopyranose
-
-
?
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
-
-
-
r
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
enzyme prefers the forward reaction
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
activity of wild-type enzyme and mutant Q345F
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
additional information
?
-
Q84HQ2
substrate specificity, di- and trisaccharides, including sucrose, are no acceptor substrate, overview
-
-
?
additional information
?
-
-
substrate specificity, di- and trisaccharides, including sucrose, are no acceptor substrate, overview
-
-
?
additional information
?
-
Q84HQ2
sucrose phosphorylase catalyzes three types of overall reaction: glucosyl transfer to and from phosphate, hydrolysis, and transglucosylation. Arsenate can replace phosphate as glucosyl acceptor substrate, other glucosyl acceptors are caffeic acid, benzoic acid, acetic acid, and formic acid
-
-
?
additional information
?
-
Q84HQ2
the wild-type enzyme shows poor activity with flavonoids or stilbenoids, e.g. resveratrol, (+)-catechin and (-)-epicatechin, while the compounds are substrates of the enzyme mutant Q345F
-
-
?
additional information
?
-
-
the wild-type enzyme shows poor activity with flavonoids or stilbenoids, e.g. resveratrol, (+)-catechin and (-)-epicatechin, while the compounds are substrates of the enzyme mutant Q345F
-
-
?
additional information
?
-
-
assay method with production of alpha-D-glucose-1-phosphate is coupled to the reduction of NAD+ in the presence of phosphoglucomutase and glucose-6-phosphate dehydrogenase
-
-
?
NATURAL SUBSTRATE
NATURAL 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
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
-
-
-
r
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Q84HQ2
enzyme activity is not dependent on cofactors or cosubstrates
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
Q84HQ2
sucrose phosphorylase is likely to serve a catabolic function in vivo, fueling the energy metabolism of the cell with Glc1P and D-fructose produced from sucrose
evolution
-
the enzyme belongs to glycoside hydrolase family GH 13 and follows the typical doubledisplacement mechanism of retaining glycosidases
additional information
Q84HQ2
mapping of the acceptor site of the enzyme by saturation mutagenesis and screening, overview. Residues Arg135, Leu343, and Tyr344 contribute to the specificity for phosphate, residues Tyr132 and Asp342 contribute to the specificity for D-fructose, and residues Pro134, Tyr196, His234, Gln345 contribute to the specificity for both. Alternative acceptors that are glycosylated rather efficiently (e.g. D-arabitol) interact with the same residues as fructose, whereas poor acceptors like pyridoxine do not seem to make any specific interactions with the enzyme
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
56189
Q84HQ2
2 * 58000, SDS-PAGE, 2 * 56189, sequence calculation
58000
58000
Q84HQ2
2 * 58000, SDS-PAGE, 2 * 56189, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
Q84HQ2
2 * 58000, SDS-PAGE, 2 * 56189, sequence calculation
additional information
Q84HQ2
an enzyme monomer consists of 4 domains: A, B, B', and C, domain A comprises the (beta/alpha)8-barrel including the active site, domain B' is involved in modulation of substrate acces via the substrate channel
additional information
-
an enzyme monomer consists of 4 domains: A, B, B', and C, domain A comprises the (beta/alpha)8-barrel including the active site, domain B' is involved in modulation of substrate acces via the substrate channel
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
inactive mutant E232Q and wild-type enzyme are cocrystallized with sucrose, 3.5 A resolution
Q84HQ2
recombinant enzyme mutant Q345F, in the presence of sucrose, and in complex with glucose, X-ray diffraction structure determination and analysis at 2.7 A resolution, PDB ID 5C8B
Q84HQ2
recombinant enzyme, hanging drop vapour diffusion method, 0.0025 ml protein solution, containing 0.5-1.0 mg/ml protein, 10 mM Tris-HCl, pH 7.1, is mixed with eual volume of precipitant solution containing 27% w/v PEG 4000, 0.1 M Tris-HCl, pH 8.5, and 0.1 sodium acetate, at 25°C, 3-14 days, X-ray diffraction structure determination and analysis at 1.77 A resolution
Q84HQ2
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D342A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
H234A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
L343A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
P134A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Q345A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Q345F
Q84HQ2
site-directed mutagenesis, the mutation allows efficient glucosylation of resveratrol, (+)-catechin and (-)-epicatechin in yields of up to 97% whereas the wild-type enzyme favours sucrose hydrolysis. The crystal structure of the variant reveals a widened access channel with a hydrophobic aromatic surface that is likely to contribute to the improved activity towards aromatic acceptors. The generation of this channel can be explained in terms of a cascade of structural changes arising from the Q345F exchange, structural changes in the active site of BaSP Q345F, modeling, overview
R135A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Y132A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Y196A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Y344A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
A498H
-
site-directed mutagenesis, the mutant shows reduced activity and thermostability compared to the wild-type enzyme
D445P
-
site-directed mutagenesis, the mutant shows slightly decreased activity and increased thermostability compared to the wild-type enzyme
D445P/D446G
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
D445P/D446P
-
site-directed mutagenesis, the mutant shows reduced activity and unaltered thermostability compared to the wild-type enzyme
D445P/D446T
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
D446G
-
site-directed mutagenesis, the mutant shows similar activity and thermostability as the wild-type enzyme
D446P
-
site-directed mutagenesis, the mutant shows slightly increased activity and the same thermostability compared to the wild-type enzyme
D446T
-
site-directed mutagenesis, the mutant shows reduced activity and slightly reduced thermostability compared to the wild-type enzyme
L306H
-
site-directed mutagenesis, the mutant shows similar activity and thermostability as the wild-type enzyme
N325D/V473H
-
site-directed mutagenesis, the mutant shows reduced activity and thermostability compared to the wild-type enzyme
N414D
-
site-directed mutagenesis, the mutant shows reduced activity and thermostability compared to the wild-type enzyme
Q331E
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
Q460E/E485H
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
R393N
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
additional information
additional information
Q84HQ2
construction of s stabilized enzyme mutant LNFI through 6 point mutations
additional information
Q84HQ2
redesign of the active site of sucrose phosphorylase through a clash-induced cascade of loop shifts
additional information
-
redesign of the active site of sucrose phosphorylase through a clash-induced cascade of loop shifts
additional information
-
formation of a glutaraldehyde cross-linked enzyme aggregate for high improvement of the enzyme's stability at 60°C, molecular imprinting of the cross-linked enzyme aggregate with a suitable substrate, i.e. glycerol, involving enzyme precipitation by tert-butyl alcohol can 2fold increase the transglucosylation activity, stability and specificity of the modified enzyme, method, overview. The modified enzyme is more useful as industrial biocatalyst than the native enzyme
additional information
-
immobilization of the enzyme by cross-linking leads to a 17 degree higher temperature tolerance compared to the soluble enzyme from Bifidobacterium adolescentis, overview
additional information
-
increasing the thermostability of sucrose phosphorylase by a combination of sequence- and structure-based mutagenesis, substitution of the most flexible residues with amino acids that occur more frequently at the corresponding positions in related sequences, and substitutions to promote electrostatic interactions
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
60
-
purified wild-type enzyme, pH 7.0, 24 h, 30% activity remaining, purified mutants show 15.3-42.9% remaining activity, overview
60
-
the immobilized enzyme is stable for one week without loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
half-lives of the enzyme at pH 6.5 and 60°C, in the presence of 20% of different cosolvents and 1 M sucrose, overview
Q84HQ2
the immobilized enzyme is stable for over 10 reaction cycles in glycosylation of molecules
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme partially from Escherichia coli via heat treatment removing the contaminating phosphatase activity
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene sucP, cloning from genomic library, DNA and amino acid sequence determination and analysis, determination of promotor region, expression in Escherichia coli
Q84HQ2
expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
heterologous expression in a food-grade Bacillus subtilis strain. Efficiently secreted into the extracellular medium in the absence of a signal peptide. After culturing the recombinant strain in a 3-l bioreactor, crude enzyme yield and activity reach 7.5 g/l and 5.3 U/ml, respectively
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
synthesis
Q84HQ2
the enzyme is useful as transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals, overview. The enzyme is also used in the industrial process for production of 2-O-(alpha-D-glucopyranosyl)-sn-glycerol as active ingredient of cosmetic formulations
synthesis
Q84HQ2
sucrose phosphorylase is a promising biocatalyst for the production of special sugars and glycoconjugates, but its transglycosylation activity rarely exceeds the competing hydrolytic reaction
synthesis
-
sucrose phosphorylase can glycosylate a variety of small molecules using sucrose as cheap ut efficient donor substrate. The immobilized enzyme is optimized due to a higher temperature tolerance compared to the soluble enzyme from Bifidobacterium adolescentis, overview
synthesis
-
effective kojibiose synthesis i as performed using the crude enzyme solution from the supernatant of fermentation broth of Bacillus subtilis expressing the enzyme from Bifidobacterium adolescentis, providing a basis for potential industrial-scale preparation of kojibiose. Kojibiose is prebiotic element, a low-calorie sweetener and exhibits antitoxic activity, thereby promoting the emergence of new drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
van den Broek, L.A.; van Boxtel, E.L.; Kievit, R.P.; Verhoef, R.; Beldman, G.; Voragen, A.G.
Physico-chemical and transglucosylation properties of recombinant sucrose phosphorylase from Bifidobacterium adolescentis DSM20083
Appl. Microbiol. Biotechnol.
65
219-227
2004
Bifidobacterium adolescentis (Q84HQ2), Bifidobacterium adolescentis
Sprogoe, D.; van den Broek, L.A.; Mirza, O.; Kastrup, J.S.; Voragen, A.G.; Gajhede, M.; Skov, L.K.
Crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis
Biochemistry
43
1156-1162
2004
Bifidobacterium adolescentis (Q84HQ2), Bifidobacterium adolescentis
Mirza, O.; Skov, L.K.; Sprogoe, D.; van den Broek, L.A.; Beldman, G.; Kastrup, J.S.; Gajhede, M.
Structural rearrangements of sucrose phosphorylase from Bifidobacterium adolescentis during sucrose conversion
J. Biol. Chem.
281
35576-35584
2006
Bifidobacterium adolescentis (Q84HQ2), Bifidobacterium adolescentis
Goedl, C.; Sawangwan, T.; Wildberger, P.; Nidetzky, B.
Sucrose phosphorylase: A powerful transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals
Biocatal. Biotransform.
28
10-21
2010
Leuconostoc mesenteroides, Pelomonas saccharophila, Streptococcus mutans, Bifidobacterium adolescentis (Q84HQ2), Leuconostoc mesenteroides B-1149
-
Cerdobbel, A.; De Winter, K.; Desmet, T.; Soetaert, W.
Sucrose phosphorylase as cross-linked enzyme aggregate: improved thermal stability for industrial applications
Biotechnol. J.
5
1192-1197
2010
Bifidobacterium adolescentis
De Winter, K.; Soetaert, W.; Desmet, T.
An imprinted cross-linked enzyme aggregate (iCLEA) of sucrose phosphorylase: combining improved stability with altered specificity
Int. J. Mol. Sci.
13
11333-11342
2012
Bifidobacterium adolescentis
Cerdobbel, A.; De Winter, K.; Aerts, D.; Kuipers, R.; Joosten, H.; Soetaert, W.; Desmet, T.
Increasing the thermostability of sucrose phosphorylase by a combination of sequence- and structure-based mutagenesis
Protein Eng. Des. Sel.
24
829-834
2011
Bifidobacterium adolescentis
Kraus, M.; Grimm, C.; Seibel, J.
Redesign of the active site of sucrose phosphorylase through a clash-induced cascade of loop shifts
ChemBioChem
17
33-36
2016
Bifidobacterium adolescentis (Q84HQ2), Bifidobacterium adolescentis
De Winter, K.; Verlinden, K.; Kren, V.; Weignerova, L.; Soetaert, W.; Desmet, T.
Ionic liquids as cosolvents for glycosylation by sucrose phosphorylase: balancing acceptor solubility and enzyme stability
Green Chem.
15
1949-1955
2013
Bifidobacterium adolescentis (Q84HQ2)
-
Verhaeghe, T.; Diricks, M.; Aerts, D.; Soetaert, W.; Desmet, T.
Mapping the acceptor site of sucrose phosphorylase from Bifidobacterium adolescentis by alanine scanning
J. Mol. Catal. B
96
81-88
2013
Bifidobacterium adolescentis (Q84HQ2)
-
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