Information on EC 3.2.1.60 - glucan 1,4-alpha-maltotetraohydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.1.60
-
RECOMMENDED NAME
GeneOntology No.
glucan 1,4-alpha-maltotetraohydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan maltotetraohydrolase
Compare EC 3.2.1.2 beta-amylase, which removes successive maltose residues, and EC 3.2.1.98 (glucan 1,4-alpha-maltohexaosidase) and EC 3.2.1.116 (glucan 1,4-alpha-maltotriohydrolase).
CAS REGISTRY NUMBER
COMMENTARY hide
37288-44-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MG-4
-
-
Manually annotated by BRENDA team
GM8901
-
-
Manually annotated by BRENDA team
Bacillus sp. GM8901
GM8901
-
-
Manually annotated by BRENDA team
IMD 353
-
-
Manually annotated by BRENDA team
MS300
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl-maltopentaoside + H2O
4-nitrophenol + maltopentaose
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
maltotetraose + ?
show the reaction diagram
amylose + H2O
maltotetraose
show the reaction diagram
amylose + H2O
maltotetraose + ?
show the reaction diagram
-
enzyme hydrolysates of amylose contains a considerably lower concentration of reducing sugars
-
-
?
azurine cross-linked amylose + H2O
maltotetraose + ?
show the reaction diagram
-
-
-
-
?
glycogen + H2O
maltotetraose
show the reaction diagram
maize starch + H2O
maltotetraose + ?
show the reaction diagram
-
the enzyme decreases the end viscosity of the maize starch suspension
-
-
?
maltoheptaose + H2O
maltotetraose + maltotriose
show the reaction diagram
maltohexaose + H2O
maltotetraose + maltose
show the reaction diagram
maltopentaose + H2O
?
show the reaction diagram
starch + H2O
maltotetraose
show the reaction diagram
starch + H2O
maltotetraose + ?
show the reaction diagram
-
the enzyme is capable of producing more than 45% maltotetraose from liquefied starch under optimal conditions
-
-
?
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
starch + H2O
maltotetraose + ?
show the reaction diagram
-
the enzyme is capable of producing more than 45% maltotetraose from liquefied starch under optimal conditions
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
-
1 mM AgNO3 activates
Ca2+
-
1 mM CaCl2 activates
Co2+
-
1 mM CoCl2 activates
Cu2+
-
1 mM CuCl2 activates
Mg2+
-
1 mM MgCl2 activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
AgNO3, recombinant and native enzyme
Al3+
-
F1 and F2 form 30% inhibition
Co2+
-
F1 and F2 form 47% inhibition
EDTA
-
1 mM, 82% inhibition
Fe2+
-
F1 form, 96% F2 form, 98% inhibition
N-bromosuccinimide
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F1 form, pH 6.5 complete inhibition, pH 8.0, 93% inhibition, F2 form, pH 6.5, 95% inhibition, pH 8.0, 28% inhibition
Ni2+
-
F1 form 62%, F2 form 67% inhibition
Pb2+
-
Pb(OAc)2, recombinant and native enzyme
phenylmethylsulfonyl fluoride
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1 mM, 4°C, 10 h incubation, 76% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.32
amylose
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F1 and F2 form
6.7 - 7.1
oyster glycogen
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5.7 - 5.9
starch
additional information
additional information
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-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
313
-
G4-1 form
364
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G4-2 form
1544
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amylase A
1775
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amylase B
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
amylase A, 40°C
6.5
-
recombinant and native enzyme
7
-
G4-1 and G4-2 form
7.8
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amylase B, 40°C
7.8 - 8.2
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F1 and F2 form
10.5 - 12
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
-
recombinant and native enzyme, pH 4.0, 30%, pH 9.0, 50% of maximal activity
4.5 - 10.5
-
95% of maximum activity at pH 7 and pH 9.5, pH 4.5, 40% of maximal activity, pH 10.5, 82% of maximal activity
6 - 13
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pH 6.0, 30%, pH 13.0, 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
immobilized enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 60
-
15°C, 20% of maximal activity, 60°C, 30% of maximal activity
25 - 65
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F1 and F2 form 25°C, 60% of maximal activity, 65°C, 20% of maximal activity
30 - 80
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30°C, 40% of maximal activity, 80°C, 20% of maximal activity
40 - 55
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40°C and 55°C, 80% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
-
gel filtration
12500
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x * 12500, dimers, tetramers, hexamers, octamers or decamers, concentration dependent
47000
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x * 47000, SDS-PAGE
47200
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calculation from sequence of amino acid
55000
-
F1 and F2 form, SDS-PAGE
56000
-
recombinant and native enzyme, SDS-PAGE
97000
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SDS-PAGE
125000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
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x * 12500, dimers, tetramers, hexamers, octamers or decamers, concentration dependent
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
57 kDa G4-1, X-ray analysis
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mutant E219Q
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X-ray structure analysis
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 11
-
30°C, 60 min, presence of CaCl2, stable between
136729
6 - 13
-
stable between, 85-100% of maximal activity
136738
6.5 - 8.5
-
absence of Ca2+, 30°C, 60 min stable between
136729
6.5 - 9.5
-
G4-1 and G4-2 form, stable between
136733
7 - 9
-
stable between
136734
7 - 8
-
amylase A, 40°C, 30 min, stable between
136739
7 - 9
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amylase B, 40°C, 30 min, stable between
136739
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
G4-1-form heat-sensitive than G4-2 form
55
-
F1 and F2 form, complete loss of activity in the absence of Ca2+
70
-
pH 6.0, 30 min, 80% activity remaining
80
-
pH 6.0, 30 min, 30% activity remaining
90
-
pH 6.0, 30 min, inactivation
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes
-
Ca2+ stabilizes immobilized enzyme
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dialysis, 4°C, prolonged periods, complete loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amylase A and B
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two active forms, F1 and F2
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two active forms, G4-1 and G4-2
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
food industry
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utilization of a maltotetraose-producing amylase as a whole wheat bread improver of the baking performance of whole-grain wheat flour, overview. Whole-grain bread dough prepared with the enzyme shows reduced water absorption and increased development time, while the dough stability is not affected. Also, the enzyme-treated samples exhibit lower Mixolab torque values than the control upon heating and cooling. The viscous characteristics of whole-grain bread dough become dominant with increasing levels of the enzyme. The enzyme delays the crumb firming of whole-grain wheat bread during a 7-d storage period and can function as an antiretrogradation agent to enhance the quality attributes of whole-grain wheat bread