Information on EC 3.2.1.48 - sucrose alpha-glucosidase

New: Word Map on EC 3.2.1.48
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
3.2.1.48
-
RECOMMENDED NAME
GeneOntology No.
sucrose alpha-glucosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
metabolism of disaccharids
-
-
Starch and sucrose metabolism
-
-
sucrose degradation III (sucrose invertase)
-
-
sucrose degradation V (sucrose alpha-glucosidase)
-
-
SYSTEMATIC NAME
IUBMB Comments
sucrose-alpha-D-glucohydrolase
This enzyme is isolated from intestinal mucosa as a single polypeptide chain that also displays activity towards isomaltose (EC 3.2.1.10 oligo-1,6-glucosidase).
CAS REGISTRY NUMBER
COMMENTARY hide
37288-39-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
snail
-
-
Manually annotated by BRENDA team
T14V
-
-
Manually annotated by BRENDA team
T14V
-
-
Manually annotated by BRENDA team
pea aphid; pea aphid, strain UY2, collected from Pisum sativum plants and maintained on Vicia faba plants, located in the honeydew
-
-
Manually annotated by BRENDA team
goose
-
-
Manually annotated by BRENDA team
slug
-
-
Manually annotated by BRENDA team
maltose-inducible alpha-glucosidase MalL, sucrase-isomaltase-maltase
-
-
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
Leishmania donovani MHOM/IN/1978/UR6
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
green mussel Perna viridis L.
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,6-di-O-alpha-D-glucopyranosyl-D-fructofuranose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
99% cleavage compared to 1,6-di-O-alpha-D-glucopyranosyl-D-fructofuranose
-
-
?
1-O-alpha-D-glucopyranosyl-D-glucitol + H2O
alpha-D-glucose + D-glucitol
show the reaction diagram
-
68% cleavage compared to 1-O-alpha-D-glucopyranosyl-D-glucitol
-
-
?
1-O-alpha-D-glucopyranosyl-D-mannitol + H2O
alpha-D-glucose + D-mannitol
show the reaction diagram
-
25% cleavage compared to 1-O-alpha-D-glucopyranosyl-D-mannitol
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-D-glucoside + H2O
4-nitrophenol + alpha-D-glucose
show the reaction diagram
-
-
-
?
6-bromo-2-naphthyl-alpha-D-glucoside + H2O
6-bromonaphthol + alpha-D-glucose
show the reaction diagram
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-glucitol + H2O
alpha-D-glucose + D-glucitol
show the reaction diagram
-
35% cleavage compared to 6-O-alpha-D-glucopyranosyl-D-glucitol
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructofuranose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
97% cleavage compared to alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructofuranose
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructopyranose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
92% cleavage compared to alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructopyranose
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucopyranose + H2O
alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucopyranosyl-(1-6)-D-fructofuranose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
100% cleavage compared to alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucopyranosyl-(1-6)-D-fructofuranose
-
-
?
alpha-D-glucopyranosyl-(1-6)-beta-fructofuranosyl-alpha-D-glucopyranoside + H2O
alpha-D-glucose + beta-D-fructose
show the reaction diagram
-
29% cleavage compared to alpha-D-glucopyranosyl-(1-6)-beta-fructofuranosyl-alpha-D-glucopyranoside
-
-
?
dextran + H2O
D-glucose
show the reaction diagram
-
-
-
?
inulin + H2O
?
show the reaction diagram
isomaltose + H2O
2 alpha-D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
?
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
isomaltose + H2O
glucose
show the reaction diagram
L-ascorbic acid alpha-glucoside + H2O
?
show the reaction diagram
-
-
-
-
?
levan + H2O
?
show the reaction diagram
maltopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltose + H2O
?
show the reaction diagram
comparable catalytic efficiencies for panose and maltose
-
-
?
maltose + H2O
alpha-D-glucose
show the reaction diagram
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
maltose + H2O
glucose
show the reaction diagram
maltose + L-ascorbic acid
L-ascorbic acid alpha-D-glucoside
show the reaction diagram
-
-
enzyme form L-ascorbic acid alpha-glucoside by splitting maltose among the disaccharides
r
maltotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
maltotriose + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-glucoside + H2O
p-nitrophenol + D-glucose
show the reaction diagram
panose + H2O
?
show the reaction diagram
comparable catalytic efficiencies for panose and maltose
-
-
?
raffinose + H2O
?
show the reaction diagram
sucrose + glucan
?
show the reaction diagram
SUH active site structure analysis, overview
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
isomaltose + H2O
glucose
show the reaction diagram
maltose + H2O
glucose
show the reaction diagram
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Li+
-
low concentration: activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,6-tribromophenol
-
purified from the red alga Grateloupia elliptica
2,4-Dibromophenol
-
purified from the red alga Grateloupia elliptica
2-Amino-2-ethyl-1,3-propanediol
-
-
2-amino-2-methyl-1,3-propanediol
-
-
2-amino-2-methyl-1-propanol
-
-
6-Bromo-2-naphthyl-alpha-glucoside
-
-
acarbose
Bis-Tris
-
-
castanospermine
-
no effect on the biosynthesis of sucrase
CdCl2
-
0.0056 mM 50% inactivation
CuSO4
-
0.0028 mM 50% inactivation
deoxygalactonojirimycin
-
IC50: 71.1 mM
deoxynojirimycin
diethanolamine
-
-
gallic acid
-
inhibition of brush border sucrase by polyphenols in mouse intestine. Inhibition by gallic acid is a pure V effect at pH 5.0, which changes to mixed type at pH 7.2, and pure K effect at pH 8.5
H+
-
competitive inhibitor in the interaction of sucrase with sucrose and sodium
HgCl2
-
0.0022 mM 50% inactivation
isomaltose
-
competitive inhibition
kotalanol
binding structure, strong structural conservation of -1 subsite residues, overview
Li+
-
high concentration, 300 mM Li+, pH dependent inhibition, complete at pH 8
maltose
-
-
Monoethanolamine
-
-
Nojirimycin
-
-
p-Nitrophenyl-alpha-glucoside
-
competitive inhibitor, inhibits both sucrase and isomaltase
PbCl2
-
0.0079 mM 50% inactivation
PCMB
-
-
ranitidine
-
noncompetitive. Ranitidine can bind to both free enzyme and enzyme-substrate complex, which is accompanied by reduction of emission intensity and red shift of fluorescence spectra
Scopolamine
Sucrose
-
high concentration
Tannic acid
-
inhibition of brush border sucrase by polyphenols in mouse intestine. Sucrase inhibition by tannic acid is a pure K effect at acidic pH and uncompetitive type in the alkaline pH range
triethanolamine
-
-
valienamine
-
an aminocyclitol, isolated from the enzymolysis broth of validamycins, configuration is similar to alpha-D-glucose, IC50 in vitro is 1.17 mM, the inhibition is pH-dependent and competitive, 80% inhibition at 2.5 mM and pH 6.6
voglibose
-
-
ZnCl2
-
0.0133 mM 50% inactivation
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-amino-2-methyl-1-propanol
-
causes activation at pH 5.2
D-glucose
-
2 mM
glucagons-like peptide 2
-
enhances the activity
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.051
4-nitrophenyl alpha-D-glucopyranoside
90C, pH not specified in the publication
1.3
4-nitrophenyl-alpha-D-glucoside
pH 6.5, 37C
0.12
6-bromo-2-naphthyl-alpha-D-glucoside
-
-
0.455 - 11.5
isomaltose
13.3
maltopentaose
-
-
0.135 - 13.5
maltose
11.1
maltotetraose
-
-
3.8
maltotriose
-
-
0.21 - 3.1
p-nitrophenyl-alpha-D-glucoside
3.2
panose
90C, pH not specified in the publication
0.0607 - 138
Sucrose
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.9
4-nitrophenyl alpha-D-glucopyranoside
Pyrococcus furiosus
Q8U4F6
90C, pH not specified in the publication
17
4-nitrophenyl-alpha-D-glucoside
Homo sapiens
P14410
pH 6.5, 37C
58.8 - 97
isomaltose
137 - 1600
maltose
278
panose
Pyrococcus furiosus
Q8U4F6
90C, pH not specified in the publication
12.34 - 107
Sucrose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
429
4-nitrophenyl alpha-D-glucopyranoside
Pyrococcus furiosus
Q8U4F6
90C, pH not specified in the publication
1313
11.8
isomaltose
Pyrococcus furiosus
Q8U4F6
90C, pH not specified in the publication
449
225
maltose
Pyrococcus furiosus
Q8U4F6
90C, pH not specified in the publication
86
85.6
panose
Pyrococcus furiosus
Q8U4F6
90C, pH not specified in the publication
1065
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
acarbose
pH 6.5, 37C
0.0006
kotalanol
pH 6.5, 37C
2.3
ranitidine
-
pH 7.0, temperature not specified in the publication
0.6
Scopolamine
-
pH 8.0, 37C
0.77
valienamine
-
pH 6.6, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0042
2,4,6-tribromophenol
Rattus norvegicus
-
-
0.0036
2,4-Dibromophenol
Rattus norvegicus
-
-
0.00002 - 0.000059
acarbose
71.1
deoxygalactonojirimycin
Acyrthosiphon pisum
-
IC50: 71.1 mM
0.034
deoxynojirimycin
Acyrthosiphon pisum
-
IC50: 0.034 mM
2.2
ranitidine
Saccharomyces cerevisiae
-
pH 7.0, temperature not specified in the publication
1.17
valienamine
Sus scrofa
-
an aminocyclitol, isolated from the enzymolysis broth of validamycins, configuration is similar to alpha-D-glucose, IC50 in vitro is 1.17 mM, the inhibition is pH-dependent and competitive, 80% inhibition at 2.5 mM and pH 6.6
0.00006
voglibose
Rattus norvegicus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
-
-
0.14
-
rhesus monkey rotavirus-infected Caco-2 cells
0.3
-
uninfected Caco-2 cells
1.46
-
adult rats
1.47
-
maltose
2.02
-
isomaltose
2.32
-
-
2.95
-
-
4.47
-
sucrose
9.5
-
maltose to L-ascorbic acid alpha-glucoside forming activity
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 5
-
L-ascorbic acid alpha-glucoside formation
6 - 6.5
-
-
6.6
-
-
7.2
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7.8
-
pH 4, 35% of maximal activity, pH 7.8, 50% of maximal activity
4.1 - 8.8
-
activity almost neglegible at pH 4.1 and pH 8.8
4.8 - 9.2
-
activating effect of sodium in the pH-range 4.8-7.2
7 - 8
-
assay at, 20% less activity at pH 8.0 compared to pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
maximal activity of L-ascorbic acid alpha-glucoside formation and maltose hydrolysis
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 65
-
from 20C to 40C linear increase of sucrase activity, at 65C, 78% activity retained
30
85% of maximal activity at 40C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
evelopmental changes in morphometry of the jejunal enzyme activity during the first nine weeks of postnatal growth, overview
Manually annotated by BRENDA team
-
production of enzyme in secreting and non-secreting medium
Manually annotated by BRENDA team
additional information
-
aphids are cultivated on diets with different sucrose levels, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
0.5-1.5% of total activity
-
Manually annotated by BRENDA team
additional information
-
congenital enzyme deficiency results in a transport block and retention of the enzyme of the brush border enzyme in the endoplasmic reticulum/cis-Golgi intermediate compartment and the cis-Golgi, probably the quality control system is involved in retention induced by a retention signal or folding determinant, i.e. the extracellular folding motif F1093-X-F1095-X-X-X-F1099, of the temperature-sensitive Q1098P mutant enzyme
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
99320
-
gene coding sucrase cloned in pPNG102 contains a ORF which defines a polypeptide of 99319 Da, the sequence shows similarity to previously sequenced sucrose-hydrolyzing enzymes
130000
-
gel filtration, density gradient, equilibrium centrifugation, sucrase subunit
140000
150000
-
SDS-PAGE, intact pancreatic duct, subunit II
220000
245000
-
fully glycosylated enzyme in the Golgi apparatus
260000
270000
-
SDS-PAGE
280000
290000
-
gel filtration, sucrase-isomaltase complex, intestinal mucosa
380000
-
380000 sucrase + 543000 isomaltase, enzyme complex after solubilisation by emulphogen and papain
additional information
-
The enzyme complex is a pseudo-dimeric assembly of a correctly folded and an enzymatically active pro-SI. The sucrase subunit functions as an intramolecular chaperone implicated in the folding of isomaltase subunit. After acquisition of a correct folding in the sucrase subunit this mature form binds tightly to the isomaltase, disrupting its interaction with calnexin. The consequence is that the isomaltase subunit acquires correct folding and sucrase subunit is no longer secreted into the external milieu.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 210000, about
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
free enzyme and enzyme in complex with the inhibitor kotalanol, hanging drop vapor diffusion method, 0.001 ml of reservoir solution containing 0.5 M NaCl, 0.1 M bis tris propane, pH 7.0, and 18% PEG 4000, is equilibrated over 0.0015 ml of protein solution and 0.003 ml of reservoir solution, containing 0.1 M MgCl2, 0.1 M bis tris propane, pH 7.0, 15% PEG 4000, X-ray diffraction structure determination and analysis at 3.2 and 2.15 A resolution, respectively, molecular replacement
purified mutant E322Q in complex with Tris or sucrose, E322Q SUH is crystallized by hanging-drop vapor-diffusion method at 22C in a crystallization buffer consisting of 0.1 M HEPES, pH 6.5, 0.2 M calcium acetate, 16% PEG 3000, and 5 mM DTT, with 0.1 M caesium chloride, and crystallization of SeMet SUH sitting-drop method at 22C in a crystallization buffer consisting of 0.1 M HEPES, pH 6.5, 0.2 M calcium acetate, 16% PEG 3000, and 5 mM DTT, with 0.1 M guanidine chloride, X-ray diffraction structure determination and analysis at 1.8 A resolution
purified enzyme in the resting state with an empty active site, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
half-life 3.5 h
65
-
thermostable, 78% activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C or -20C, 0.02% sodium azide, Triton X-100, several weeks, sucrase-isomaltase
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from brush border 155fold by isolation from the microvillus membranes by papain, gel filtration and anion exchange chromatography
-
partially from intestinal mucosa by ammonium sulfate precipitation
-
partially from jejunal brush border membrane by diffeential centrifugation and Mg2+ precipitation
-
produced and purified in Escherichia coli RB791/pMalL
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Chinese hamster ovary cells and in Xenopus laevis oocytes
-
expression in Escherichia coli
-
expression in Escherichia coli, IPTG induction does not increase sucrase activity in Escherichia coli, the cloned gene may be transcribed from itst own promoter, the first sucrase cloned from Leuconostoc mesenteroides with invertase activity
-
expression in Escherichia coli, the gene coding the enzyme has been identified in the ORF yvdL/malL
-
expression of fluorescence-labeled wild-type and mutant enzymes in COS-1 cells
-
expression of the cDNA constructs encoding the sucrase and isomaltase domains in transfected cells
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene levJ from a library of T14V DNA constructed in plasmid pUC18, pPNG102 contains the ORF for the sucrase polypeptide
-
glucagons-like peptide 2 enhances enzyme gene expression
-
mouse SI mRNA synthesized from mouse SI cDNA, pMSI-A1 cloned into pBluescript KS, cDNA cloned from mouse intestinal RNA with anchored polymerase chain reaction method
-
transfection in COS-1 cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C1229Y
-
heterozygous mutation within the sucrose domain, found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is transported only to the Golgi apparatus. Isomaltase activity is not affected by the mutation
F1093A/F1095A/F1099A
-
site-directed mutagenesis, mutation of the extracellular folding signal motif, CSID-phenotype II-like temperature-sensitive mutant enzyme which undergoes transport arrest in the endoplasmic reticulum/cis-Golgi intermediate and cis-Golgi compartments and acquires correct folding and function at reduced temperatures as a consequence of anterograde and retrograde transport between endoplasmic reticulum and cis-Golgi, overview
F1745C
-
heterozygous mutation within the sucrose domain, found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is misfolded and can not exit the endoplasmic reticulum. Isomaltase activity is not affected by the mutation
G1073D
-
heterozygous mutation found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is misfolded and can not exit the endoplasmic reticulum
Q1098P
V577G
-
heterozygous mutation found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is misfolded and can not exit the endoplasmic reticulum
E322Q
site-directed mutagenesis, a catalytically inactive Xag SUH mutant
G219R
site-directed mutagenesis, the mutant shows increased catalytic activity compared to the wild-type enzyme
G219R/G444R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G219R/L414R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G444R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
L414R
site-directed mutagenesis, the mutant shows slightly reduced catalytic activity compared to the wild-type enzyme
L414R/G444R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
sucrose-metabolizing enzymes are tools in plant science, genes enconding various sucrose-metabolizing enzymes are valuable in genetic engineering of higher plants
medicine