Information on EC 3.2.1.48 - sucrose alpha-glucosidase

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

EC NUMBER
COMMENTARY
3.2.1.48
-
RECOMMENDED NAME
GeneOntology No.
sucrose alpha-glucosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action
show the reaction diagram
-
-
-
-
hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action
show the reaction diagram
The enzyme complex consists of two noncovalently linked subunits. The active site of the sucrase subunit cleaves alpha,beta-(1-2)glycosidic bonds and contains only two subsites and, thus can bind only two monomeric parts of a substrate with positive affinity. The isomaltase cleaves alpha-(1-6) and alpha-(1-1) glycoside bonds
-
hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action
show the reaction diagram
the protein with strong homology to a rabbit sucrase-isomaltase is a cAMP-dependent epithelial chloride channel
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Starch and sucrose metabolism
-
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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alpha-glucosidase
-
-
glucosidase, sucrose alpha-
-
-
-
-
intestinal sucrase
-
-
-
-
intestinal sucrase
-
-
PF0132
Q8U4F6
gene name
sucrase
-
-
-
-
sucrase
-
-
sucrase isomaltase
-
-
sucrase-invertase
-
-
-
-
sucrase-isomaltase
-
-
-
-
sucrase-isomaltase
P14410
-
sucrase-isomaltase
-
-
sucrase-isomaltase
-
-
sucrase-isomaltase
-
-
sucrase-isomaltase enzyme complex
-
-
sucrase/isomaltase
-
-
sucrose alpha-glucohydrolase
-
-
-
-
sucrose hydrolase
Q6UVM5
-
isomaltase
Q8U4F6
-
additional information
-
the enzyme belongs to the subfamily 4 of the glycoside hydrolase family 13, GH-13
CAS REGISTRY NUMBER
COMMENTARY
37288-39-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Actinomyces naeslundii T14V
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
bifunctional sucrase-isomaltase from patients with congenital sucrase-isomaltase deficiency
-
-
Manually annotated by BRENDA team
cf. EC 3.2.1.10
UniProt
Manually annotated by BRENDA team
human, sucrase/isomaltase molecule is an hybrid consisting of 2 distinct alpha-glucosidases
-
-
Manually annotated by BRENDA team
sucrase-isomaltase in adult human colon and colonic polyps
-
-
Manually annotated by BRENDA team
Leishmania donovani MHOM/IN/1978/UR6
-
-
-
Manually annotated by BRENDA team
mouse, inbred strains CBA/J, CBA/Ca, CBA/CaH, CBA/CaHN, C57B1/6
-
-
Manually annotated by BRENDA team
green mussel Perna viridis L.
-
-
Manually annotated by BRENDA team
rat, single protein with sucrase and isomaltase activity
-
-
Manually annotated by BRENDA team
sucrase-isomaltase
-
-
Manually annotated by BRENDA team
sucrase-isomaltase synthesized as a one-chain polypeptide, precursor that is split into the subunits after its transfer to the microvillus membrane
-
-
Manually annotated by BRENDA team
parenterally fed premature neonatal piglets
-
-
Manually annotated by BRENDA team
pig
-
-
Manually annotated by BRENDA team
sucrose hydrolase; pv. glycines
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
promastigotes take up sucrose via a H+-sucrose symport system and, on entering the cell, the sucrose is hydrolysed to its component monosaccharides by intracellular sucrase
physiological function
-
core2 1,6-N-acetylglucosaminyltransferase-2 knockdown significantly reduces cell surface expression of sucrase isomaltase and dipeptidyl peptidase-IV in Caco-2 cells. Overexpression of the core3 structure in HT-29 cells attenuates cell surface expression of both enzymes
physiological function
-
the fully glycosylated mature form of sucrase isomaltase is decreased in core2 1,6-N-acetylglucosaminyltransferase-2 knock-out mice but not in core2 N-acetylglucosaminyltransferase-3 nulls. Expression of sucrase isomaltase and dipeptidyl peptidase-IV is dramatically reduced in core2 1,6-N-acetylglucosaminyltransferase-1-3 triple knock-out mice. Goblet cells in the upper part of the crypt show impaired maturation in the core2 O-glycan-deficient mice
physiological function
-, Q8U4F6
involved in processing alpha-1,6-glucans. Pullulan is likely degraded extracellularly by an amylopullulanase and further hydrolyzed by the PF0132 protein after intracellular transport
physiological function
Leishmania donovani MHOM/IN/1978/UR6
-
promastigotes take up sucrose via a H+-sucrose symport system and, on entering the cell, the sucrose is hydrolysed to its component monosaccharides by intracellular sucrase
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-, Q8U4F6
-
-
-
?
4-nitrophenyl-alpha-D-glucoside + H2O
4-nitrophenol + alpha-D-glucose
show the reaction diagram
P14410
-
-
-
?
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
glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
glucose
show the reaction diagram
-
-
-
-
?
isomaltose + H2O
glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
P14410
-
-
-
?
isomaltose + H2O
?
show the reaction diagram
-, Q8U4F6
-
-
-
?
isomaltose + H2O
2 alpha-D-glucose
show the reaction diagram
P14410
-
-
-
?
L-ascorbic acid alpha-glucoside + H2O
?
show the reaction diagram
-
-
-
-
?
levan + H2O
?
show the reaction diagram
Actinomyces naeslundii, Actinomyces naeslundii T14V
-
-
-
-
?
maltopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
Actinomyces naeslundii T14V
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
maltose + H2O
?
show the reaction diagram
-, Q8U4F6
comparable catalytic efficiencies for panose and maltose
-
-
?
maltose + H2O
alpha-D-glucose
show the reaction diagram
P14410
-
-
-
?
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
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
Q6UVM5, -
-
-
-
?
p-nitrophenyl-alpha-glucoside + H2O
p-nitrophenol + D-glucose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-glucoside + H2O
p-nitrophenol + D-glucose
show the reaction diagram
-
-
-
?
panose + H2O
?
show the reaction diagram
-, Q8U4F6
comparable catalytic efficiencies for panose and maltose
-
-
?
raffinose + H2O
?
show the reaction diagram
Actinomyces naeslundii, Actinomyces naeslundii T14V
-
-
-
-
?
sucrose + glucan
?
show the reaction diagram
Q6UVM5, -
SUH active site structure analysis, overview
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
-
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
Q6UVM5, -
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
Actinomyces naeslundii T14V
-
-
-
?
sucrose + H2O
glucose + fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
glucose + fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
glucose + fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
glucose + fructose
show the reaction diagram
Actinomyces naeslundii, Actinomyces naeslundii T14V
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
P14410
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
the enzyme is involved in osmoregulation in the gut and hemolymph of pea aphids in response to the diet, analysis of honeydew sugar composition
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
substrate binding site and structure, overview
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
the absolute enzyme exhibits a flat negative trough, indicating the presence of alpha-helices and beta-sheet structures in the enzyme
-
-
?
maltotriose + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme is involved in regulating the secretion of cellobiase through co-aggregation
-
-
-
additional information
?
-
-
Additional substrates are mixtures of isomers containing mannitol and glucitol, e.g. alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-mannitol and alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-glucitol in a ratio 2:3, alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-gluco-pyranosyl-(1-1)-D-mannitol and alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-gluco-pyranosyl-(1-1)-D-glucitol in a ratio 2:3, 1,6-di-O-alpha-D-glucopyranosyl-D-mannitol and 1,6-di-O-alpha-D-glucopyranosyl-D-glucitol, alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-mannitol and alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-glucitol. The end products are glucose, mannose and glucitol in accordance with the composition of the initial substrate.
-
-
-
additional information
?
-
Q6UVM5, -
not: alpha-D-glucopyranosyl-(1-4)-D-glucopyranose, alpha-D-glucopyranosyl-(1-6)-D-glucopyranose, alpha-D-glucopyranosyl alpha-D-glucopyranoside, alpha-D-galactopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-2)-beta-D-fructofuranoside, alpha-D-galactopyranosyl-(1-6)-alpha-D-galactopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-2)-beta-D-fructofuranoside
-
-
-
additional information
?
-
-
enzyme mutation can cause the congenital sucrase-isomaltase deficiency phenotype II, overview
-
-
-
additional information
?
-
-
rhesus monkey rotavirus impairs expression and activity of the brush border-associated enzyme in Caco-2 cells, the inhibition is not due to virus-induced, Ca2+-dependent disassembly of the F-actin cytoskeleton, but to a mechanism involving cAMP protein kinase A, PKA, EC 2.7.11.11, signalling and hyperphosphorylation of cytokeratin 18, the effect is antagonized by PKA blockers, e.g. H-89
-
-
-
additional information
?
-
-
the enzyme activity influences the development of size and digestive capacity of the jejunum and small intestine
-
-
-
additional information
?
-
-
the enzyme expression is transactivated by transcription factors hepatocyte nuclear factors 1alpha and 1beta, HNF-1alpha and HNF-1beta, molecular mechanism and responsible amino acids of HNFs, overview
-
-
-
additional information
?
-
Q6UVM5, -
the enzyme is identified as NpAS, i.e. Neisseria polysaccharea amylosucrase, homolog, involved in regulation of the utilization of plant sucrose in phytopathogenic bacteria. But the enzyme is exclusively a hydrolase and not a glucosyltransferase and is termed sucrose hydrolase, SUH, overview
-
-
-
additional information
?
-
P14410
hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products, human maltase-glucoamylase and sucrase-isomaltase are composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities. The N-terminal catalytic domain of human MGAM has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides
-
-
-
additional information
?
-
-, Q8U4F6
pullulan is likely degraded extracellularly by an amylopullulanase and further hydrolyzed by the PF0132 protein after intracellular transport
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
isomaltose + H2O
glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
glucose
show the reaction diagram
-
-
-
-
?
isomaltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
-
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
P14410
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
the enzyme is involved in osmoregulation in the gut and hemolymph of pea aphids in response to the diet, analysis of honeydew sugar composition
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
Actinomyces naeslundii T14V
-
-
-
?
maltose + H2O
glucose
show the reaction diagram
Actinomyces naeslundii T14V
-
-
-
?
additional information
?
-
-
the enzyme is involved in regulating the secretion of cellobiase through co-aggregation
-
-
-
additional information
?
-
-
enzyme mutation can cause the congenital sucrase-isomaltase deficiency phenotype II, overview
-
-
-
additional information
?
-
-
rhesus monkey rotavirus impairs expression and activity of the brush border-associated enzyme in Caco-2 cells, the inhibition is not due to virus-induced, Ca2+-dependent disassembly of the F-actin cytoskeleton, but to a mechanism involving cAMP protein kinase A, PKA, EC 2.7.11.11, signalling and hyperphosphorylation of cytokeratin 18, the effect is antagonized by PKA blockers, e.g. H-89
-
-
-
additional information
?
-
-
the enzyme activity influences the development of size and digestive capacity of the jejunum and small intestine
-
-
-
additional information
?
-
-
the enzyme expression is transactivated by transcription factors hepatocyte nuclear factors 1alpha and 1beta, HNF-1alpha and HNF-1beta, molecular mechanism and responsible amino acids of HNFs, overview
-
-
-
additional information
?
-
Q6UVM5, -
the enzyme is identified as NpAS, i.e. Neisseria polysaccharea amylosucrase, homolog, involved in regulation of the utilization of plant sucrose in phytopathogenic bacteria. But the enzyme is exclusively a hydrolase and not a glucosyltransferase and is termed sucrose hydrolase, SUH, overview
-
-
-
additional information
?
-
P14410
hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products
-
-
-
additional information
?
-
-, Q8U4F6
pullulan is likely degraded extracellularly by an amylopullulanase and further hydrolyzed by the PF0132 protein after intracellular transport
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Li+
-
low concentration: activation
Na+
-
low concentration: activation
Na+
-
low concentration: activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
BAY g 5421
acarbose
-
IC50: 0.000059 mM; in vitro and in vivo
acarbose
P14410
binding structure,overview
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
-
-
deoxynojirimycin
-
IC50: 0.034 mM
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
P14410
binding structure, strong structural conservation of -1 subsite residues, overview
Li+
-
high concentration, 300 mM Li+, pH dependent inhibition, complete at pH 8
Na+
-
high concentration
Na+
-
high concentration
p-Nitrophenyl-alpha-glucoside
-
competitive inhibitor, inhibits both sucrase and isomaltase
PbCl2
-
0.0079 mM 50% inactivation
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
-
i.e. hyoscine, is commonly used as an anticholinergic drug to relieve nausea, vomiting and dizziness of amotion sickness as well as recovery from anesthesia and surgery. It shows non-competitive inhibition at different concentrations of 0.6-3.6 mM
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
-
-
Tris
-
concentration-dependent biphasic effect, first causing activation, fully competitive inhibition above pH 6.8, inhibition is stronger at alkaline pH values
Tris
-
concentration-dependent biphasic effect, first causing activation, fully competitive inhibition above pH 6.8, inhibition is stronger at alkaline pH values
Tris
-
concentration-dependent biphasic effect, first causing activation, fully competitive inhibition above pH 6.8, inhibition is stronger at alkaline pH values
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
ZnCl2
-
0.0133 mM 50% inactivation
Monoethanolamine
-
-
additional information
-
rhesus monkey rotavirus impairs expression and activity of the brush border-associated enzyme in Caco-2 cells, the inhibition is not due to virus-induced, Ca2+-dependent disassembly of the F-actin cytoskeleton, but to a mechanism involving cAMP protein kinase A, PKA, EC 2.7.11.11, signalling and hyperphosphorylation of cytokeratin 18, the effect is antagonized by PKA blockers, e.g. H-89
-
additional information
-
compounds with alpha-glucosidase inhibitory activity are preliminarily screened and purified from ten different seaweeds (two green, four brown, and four red). The alpha-glucosidase inhibitory activity of the MeOH H2O (4:1, v/v) extract of Polyopes lancifolia at 5 mg/ml is highest at 52.2%, followed by Grateloupia elliptica (42.0%), Sargassum thunbergii (24.3%), and Grateloupia. lanceolata (22.0%) in decreasing order
-
additional information
-
inhibition of mice sucrase by polyphenols is pH-dependent, and is associated with conformational modifications of the enzyme. At pH 4.8, the polyphenols inhibit sucrase activity by 85-96%, which is reduced to 51 and 64%, respectively, at pH 7.2. However, at pH 8.5, 60 and 76% inhibition of enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
transcription factors HNF-1alpha and HNF-1beta transactivate enzyme expression in the small intestine, reduced activation activity of 13 HNF mutants, overview
-
additional information
-
transcription factors HNF-1alpha and HNF-1beta induce constitutive enzyme expression by direct binding to sites SIF2 and SIF3 of the SI gene promoter
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.051
-
4-nitrophenyl alpha-D-glucopyranoside
-, Q8U4F6
90C, pH not specified in the publication
1.3
-
4-nitrophenyl-alpha-D-glucoside
P14410
pH 6.5, 37C
0.12
-
6-bromo-2-naphthyl-alpha-D-glucoside
-
-
0.455
-
isomaltose
-
-
3.2
-
isomaltose
-
-
5
-
isomaltose
-, Q8U4F6
90C, pH not specified in the publication
11.1
-
isomaltose
P14410
pH 6.5, 37C
11.5
-
isomaltose
-
-
13.3
-
maltopentaose
-
-
0.135
-
maltose
-
-
1
-
maltose
-
-
7.1
-
maltose
P14410
pH 6.5, 37C
7.1
-
maltose
-, Q8U4F6
90C, pH not specified in the publication
7.2
-
maltose
-
-
13.5
-
maltose
-
the existence of 2 Km values supports the notion of substrate hydrolysis at 2 active sites on the sucrase-isomaltase complex
11.1
-
maltotetraose
-
-
0.21
-
p-nitrophenyl-alpha-D-glucoside
-
-
1.5
-
p-nitrophenyl-alpha-D-glucoside
-
-
3.1
-
p-nitrophenyl-alpha-D-glucoside
-
-
3.2
-
panose
-, Q8U4F6
90C, pH not specified in the publication
0.184
-
Sucrose
-
-
1.3
-
Sucrose
Q6UVM5, -
recombinant mutant L414R/G444R
1.34
-
Sucrose
Q6UVM5, -
recombinant mutant G444R
1.73
-
Sucrose
Q6UVM5, -
recombinant mutant G219R/G444R
2.24
-
Sucrose
Q6UVM5, -
recombinant wild-type enzyme
2.4
-
Sucrose
Q6UVM5, -
pH 7.5, 30C
2.48
-
Sucrose
Q6UVM5, -
recombinant mutant G219R
2.97
-
Sucrose
Q6UVM5, -
recombinant mutant L414R
3.6
-
Sucrose
Q6UVM5, -
recombinant mutant G219R/L4141R
9
-
Sucrose
-
-
10.2
-
Sucrose
-
-
10.5
-
Sucrose
-
-
11.5
-
Sucrose
-
pH 7.0, temperature not specified in the publication
15.9
-
Sucrose
-
pH 7.6
16
-
Sucrose
-
-
19.7
-
Sucrose
-
-
20
-
Sucrose
-
-
20
-
Sucrose
-
-
20
-
Sucrose
-
-
20.2
21.2
Sucrose
-
inbred strains of mice with genetic and posttranslational variations in SI complex structure, incubation at 37C
22
-
Sucrose
-
value remains constant at Li+ concentration from 20-120 mM
30.8
-
Sucrose
-
-
96.7
-
Sucrose
-
pH 8.5
130
-
Sucrose
-
pH 5.0
138
-
Sucrose
-
pH 7.2
3.8
-
maltotriose
-
-
additional information
-
additional information
-
Km values in presence of inhibitors, at pH 7.2, both gallic acid and tannic acid show mixed-type enzyme inhibition, Km is enhanced by 77-114% and Vmax by 55-60%, overview
-
additional information
-
additional information
-
Michaelis-Menten kinetics, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
21.9
-
4-nitrophenyl alpha-D-glucopyranoside
-, Q8U4F6
90C, pH not specified in the publication
17
-
4-nitrophenyl-alpha-D-glucoside
P14410
pH 6.5, 37C
58.8
-
isomaltose
-, Q8U4F6
90C, pH not specified in the publication
97
-
isomaltose
P14410
pH 6.5, 37C
137
-
maltose
P14410
pH 6.5, 37C
1600
-
maltose
-, Q8U4F6
90C, pH not specified in the publication
278
-
panose
-, Q8U4F6
90C, pH not specified in the publication
12.34
-
Sucrose
Q6UVM5, -
recombinant mutant G444R
12.49
-
Sucrose
Q6UVM5, -
recombinant mutant L414R/G444R
12.77
-
Sucrose
Q6UVM5, -
recombinant mutant G219R/G444R
60.64
-
Sucrose
Q6UVM5, -
recombinant mutant G219R/L4141R
66.45
-
Sucrose
Q6UVM5, -
recombinant wild-type enzyme
78.01
-
Sucrose
Q6UVM5, -
recombinant mutant L414R
107
-
Sucrose
Q6UVM5, -
recombinant mutant G219R
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
429
-
4-nitrophenyl alpha-D-glucopyranoside
-, Q8U4F6
90C, pH not specified in the publication
206452
11.8
-
isomaltose
-, Q8U4F6
90C, pH not specified in the publication
11801
225
-
maltose
-, Q8U4F6
90C, pH not specified in the publication
12854
85.6
-
panose
-, Q8U4F6
90C, pH not specified in the publication
15203
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.014
-
acarbose
P14410
pH 6.5, 37C
0.0006
-
kotalanol
P14410
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]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0042
-
2,4,6-tribromophenol
-
-
0.0036
-
2,4-Dibromophenol
-
-
0.00002
-
acarbose
-
-
0.000059
-
acarbose
-
IC50: 0.000059 mM
71.1
-
deoxygalactonojirimycin
-
IC50: 71.1 mM
0.034
-
deoxynojirimycin
-
IC50: 0.034 mM
2.2
-
ranitidine
-
pH 7.0, temperature not specified in the publication
1.17
-
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
0.00006
-
voglibose
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.05
-
-
-
0.14
-
-
rhesus monkey rotavirus-infected Caco-2 cells
0.3
-
-
uninfected Caco-2 cells
0.51
-
-
-
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
17.5
-
-
-
47
-
-
-
additional information
-
-
-
additional information
-
-
comparison of activity from washed mycelia in secreting and non-secreting media from extracellular, intracellular fractions in dependence on grown time
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
5
-
L-ascorbic acid alpha-glucoside formation
5.8
-
-
-
5.9
-
-
in the presence of 50 mM Na+
6
6.5
-
-
6.2
-
-
-
6.5
-
-
-
6.5
-
P14410
assay at
6.6
-
-
-
6.7
-
-
-
7
-
-
with PNPG as substrate, at pH 5.75 and 8.0 activity reduced to 50%
7.2
-
-
assay at
7.5
-
Q6UVM5, -
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
6.5
8.5
Q6UVM5, -
-
7
8
-
assay at, 20% less activity at pH 8.0 compared to pH 7.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
; assay at
37
-
-
assay at
37
-
P14410
assay at
37
-
-
assay at
40
-
Q6UVM5, -
-
60
-
-
maximal activity of L-ascorbic acid alpha-glucoside formation and maltose hydrolysis
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
65
-
from 20C to 40C linear increase of sucrase activity, at 65C, 78% activity retained
30
-
Q6UVM5, -
85% of maximal activity at 40C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
production of enzyme in secreting and non-secreting medium
Manually annotated by BRENDA team
-
presence of a stable intracellular pool of the sucrose splitting enzyme, sucrase, in promastigote stage parasites
Manually annotated by BRENDA team
Leishmania donovani MHOM/IN/1978/UR6
-
presence of a stable intracellular pool of the sucrose splitting enzyme, sucrase, in promastigote stage parasites
-
Manually annotated by BRENDA team
-
developmental changes in morphometry of the small intestine enzyme activity during the first nine weeks of postnatal growth, overview
Manually annotated by BRENDA team
-
evelopmental changes in morphometry of the jejunal enzyme activity during the first nine weeks of postnatal growth, overview
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 ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is sorted with high fidelity to the apical membrane via O-linked glycans that mediate its association with lipid rafts or detergent-resistant membranes
Manually annotated by BRENDA team
-
0.5-1.5% of total activity
-
Manually annotated by BRENDA team
-
Intracellular sucrase activity, remaining more or less constant around 75 nmoles/200000000cells for up to 3 h
Manually annotated by BRENDA team
Leishmania donovani MHOM/IN/1978/UR6
-
Intracellular sucrase activity, remaining more or less constant around 75 nmoles/200000000cells for up to 3 h
-
Manually annotated by BRENDA team
-
the isomaltase subunit is membrane associated and the sucrase subunit is hydrophilic
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
-
gel filtration, luminal
140000
-
-
SDS-PAGE, sucrase-isomaltase
140000
-
-
SDS-PAGE, intact pancreatic duct, subunit I
150000
-
-
SDS-PAGE, intact pancreatic duct, subunit II
200000
-
-
-
220000
-
-
ultracentrifugation analysis, mature complex precursor
220000
-
-
-
245000
-
-
fully glycosylated enzyme in the Golgi apparatus
260000
-
-
SDS-PAGE, disconnected pancreatic duct
260000
-
-
gel filtration
270000
-
-
SDS-PAGE
280000
-
-
gel filtration, density gradient equilibrium centrifugation, human, sucrase-isomaltase complex
280000
-
-
gel filtration, density gradient equilibrium centrifugation, human, sucrase-isomaltase complex
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 ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 210000, about
dimer
-
1 * 140000 - 160000 + 1 * 140000 -160000 2 large subunits, EC 3.2.1.48 and EC 3.2.1.10, functional dimer, SDS-PAGE
dimer
-
1 * 140000 + 1 * 150000, intact pancreatic duct, SDS -PAGE
dimer
-
-
dimer
-
1 * 112000 + 1* 100000, hetero-dimer, 2 catalytically active sites for maltase and sucrase
dimer
-
1 * 145000, sucrase + 1* 151000, isomaltase
dimer
-
-
monomer
-
disconnected pancreatic duct, SDS-PAGE
monomer
Q6UVM5, -
1 * 64000, SDS-PAGE
additional information
-
-
additional information
P14410
human maltase-glucoamylase and sucrase-isomaltase are composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities
additional information
-
residues Arg516 and Asp138 are not engaged in salt-bridge formation in the resting enzyme from Xanthomonas campestris pv. campestris in contrast to the enzyme from Xanthomonas axonopodis pv. glycines. In the absence of the salt bridge an opening is created which gives access to subsite 1 from the nonreducing end
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
the individual expression of isomaltase subunit in COS-1 cells results in a malfolded and transport-incompetent glycoprotein, during the sucrase subunit a transport-competent protein
glycoprotein
-
the enzyme is highly glycosylated, glycosylation is inhibited by benzyl-GalNAc. Modulation of the glycosylation pattern of the enzyme with benzyl-2-acetamido-2-deoxy-alpha-D-galactopyranoside and deoxymannojirimycin, overview. N- and O-glycosylation and detergent-resistant membranes are implicated in the regulation of the function of the enzyme in intestinal Caco-2 cells
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
P14410
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
Q6UVM5, -
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
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
Q6UVM5, -
half-life 14 h
40
-
Q6UVM5, -
half-life 3.5 h
50
-
-
pH 5.9, inactivation, soluble enzyme activity is stable to heat treatment, membrane associated enzyme was heat-labile under these conditions
50
-
-
pH 5.9, inactivation, soluble enzyme activity is stable to heat treatment, membrane associated enzyme was heat-labile under these conditions
60
-
-
soluble enzyme is stable at 60C for 30 min in cortisone and thyroxine treated animals, heat-labile in control and insulin given animals, 3% activity less, incubation for 40 min
60
-
-
soluble enzyme is stable at 60C for 30 min in cortisone and thyroxine treated animals, heat-labile in control and insulin given animals, 3% activity less, incubation for 40 min
65
-
-
thermostable, 78% activity
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C or -20C, 0.02% sodium azide, Triton X-100, several weeks, sucrase-isomaltase
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
produced and purified in Escherichia coli RB791/pMalL
-
native enzyme from brush border 155fold by isolation from the microvillus membranes by papain, gel filtration and anion exchange chromatography
-
native enzyme
-, Q8U4F6
partially from intestinal mucosa by ammonium sulfate precipitation
-
partially from jejunal brush border membrane by diffeential centrifugation and Mg2+ precipitation
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene levJ from a library of T14V DNA constructed in plasmid pUC18, pPNG102 contains the ORF for the sucrase polypeptide
-
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
-
transfection in COS-1 cells
-
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
-
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
-
expression in Chinese hamster ovary cells and in Xenopus laevis oocytes
-
expression in Escherichia coli
-
glucagons-like peptide 2 enhances enzyme gene expression
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Q6UVM5, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
Q1098P
-
the mutation causes a temperature-sensitive arrest of enzyme in the endoplasmic reticulum and cis-Golgi, at 20C the mutant shows 93% activity in comparison to 100% activity of wild-type enzyme. At 37C the mutant shows 10% activity in comparison to 100% activity of wild-type enzyme
Q1098P
-
naturally occurring mutation, phenotype II of the congenital sucrase-isomaltase deficiency, CSID, the mutation generates a temperature-sensitive and activity-impaired mutant enzyme, 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
V577G
-
heterozygous mutation found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is misfolded and can not exit the endoplasmic reticulum
E322Q
Q6UVM5, -
site-directed mutagenesis, a catalytically inactive Xag SUH mutant
G219R
Q6UVM5, -
site-directed mutagenesis, the mutant shows increased catalytic activity compared to the wild-type enzyme
G219R/G444R
Q6UVM5, -
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G219R/L414R
Q6UVM5, -
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G444R
Q6UVM5, -
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
L414R
Q6UVM5, -
site-directed mutagenesis, the mutant shows slightly reduced catalytic activity compared to the wild-type enzyme
G1073D
-
heterozygous mutation found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is misfolded and can not exit the endoplasmic reticulum
additional information
-
overexpression of transcription factors HNF-1alpha and HNF-1beta mutants HNF-1lphaT539fsdelC and HNF-1betaR177X in Caco-2 cells reduces the sucrase-isomaltase activity
L414R/G444R
Q6UVM5, -
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
additional information
Q6UVM5, -
conformational changes in the SUH active site du to mutational alterations, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
sucrase-isomaltase SI is a marker enzyme of the absorptive villose cells in adult small intestine, human intestinal sucrase-isomaltase help develop a specific inhibitor of sucrase, to retard the absorption of sucrose in the intestinal tract of diabetic patients
medicine
-
one therapeutic approach for decreasing postprandial hyperglycemia is to retard absorption of glucose by inhibition of alpha-glucosidase. Bromophenols of Grateloupia elliptica have potential as natural nutraceuticals to prevent diabetes mellitus because of their high a-glucosidase inhibitory activity
agriculture
-
sucrose-metabolizing enzymes are tools in plant science, genes enconding various sucrose-metabolizing enzymes are valuable in genetic engineering of higher plants