Information on EC 4.2.2.13 - exo-(1->4)-alpha-D-glucan lyase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
4.2.2.13
-
RECOMMENDED NAME
GeneOntology No.
exo-(1->4)-alpha-D-glucan lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
linear alpha-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose
show the reaction diagram
-
-
-
-
linear alpha-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose
show the reaction diagram
reaction mechanism occurred by an acid-catalysed formation of a covalent glycosyl-enzyme intermediate via the nucleophilic aspartic acid residue Asp 553 followed by the E1-like E2 elimination of the enzyme carboxylate to generate 1,5-anhydrofructose
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C-O bond cleavage
-
-
C-O-bond cleavage
-
-
-
-
elimination
-
-
-
-
elimination
-
-
SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming)
The enzyme catalyses the sequential degradation of (1->4)-alpha-D-glucans from the non-reducing end with the release of 1,5-anhydro-D-fructose. Thus, for an alpha-glucan containing n (1->4)-linked glucose units, the final products are 1 glucose plus (n-1) 1,5-anhydro-D-fructose. Maltose, maltosaccharides and amylose are all completely degraded. It does not degrade (1->6)-alpha-glucosidic bonds and thus the degradation of a branched glucan, such as amylopectin or glycogen, will result in the formation of 1,5-anhydro-D-fructose plus a limit dextrin. Other enzymes involved in the anhydrofructose pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase) and EC 5.3.2.7 (ascopyrone tautomerase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(1,4)-alpha-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming)
-
-
-
-
alpha-(1,4)-Glucan 1,5-anhydro-D-fructose eliminase
-
-
-
-
alpha-1,4-Glucan exo-lyase
-
-
-
-
alpha-1,4-Glucan lyase
-
-
-
-
alpha-1,4-Glucan lyase
-
-
Dehydratase, alpha-1,4-glucan
-
-
-
-
exo-(1,4)-alpha-D-glucan lyase
-
-
-
-
Exo-alpha-1,4-glucan lyase
-
-
-
-
Exo-alpha-1,4-glucan lyase
-
-
CAS REGISTRY NUMBER
COMMENTARY
148710-18-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Anthracobia melaloma
CBS 293.54
-
-
Manually annotated by BRENDA team
Anthracobia melaloma CBS 293.54
CBS 293.54
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1,4-alpha-D-glucosyl)n
1,5-anhydro-D-fructose + (1,4-alpha-D-glucosyl)n-1
show the reaction diagram
-
degradation of glycogen and starch in eukaryotes
-
-
?
2,4,6-trichlorophenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
2,5-dinitrophenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
2-nitrophenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
3,4-dinitrophenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
3,5-dichlorophenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
3-nitrophenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
4-chloro-2-nitrophenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
4-chlorophenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
4-nitrophenyl alpha-D-glucoside
?
show the reaction diagram
-
-
-
-
?
5-fluoro-alpha-D-glucopyranosyl fluoride
?
show the reaction diagram
-
-
-
?
alpha-D-glucopyranosyl fluoride
?
show the reaction diagram
-
-
-
?
alpha-D-glucopyranosyl fluoride
?
show the reaction diagram
-
-
-
?
Amylopectin
Glucose + 1,5-anhydro-D-fructose
show the reaction diagram
-
-
-
-
-
Amylopectin
Glucose + 1,5-anhydro-D-fructose
show the reaction diagram
-
-
-
-
-
amylopectin
?
show the reaction diagram
-
barley amylopectin and potato amylopectin
-
?
amylopectin
D-glucose + 1,5-anhydro-D-fructose
show the reaction diagram
-
-
-
-
?
Glycogen
?
show the reaction diagram
-
-
-
-
?
Glycogen
?
show the reaction diagram
-
-
-
-
-
Glycogen
?
show the reaction diagram
Anthracobia melaloma
-
-
-
?
Glycogen
?
show the reaction diagram
-
best substrate
-
-
-
Glycogen
?
show the reaction diagram
-
rabbit liver glycogen
-
?
Glycogen
?
show the reaction diagram
Anthracobia melaloma
-
the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
Glycogen
?
show the reaction diagram
Anthracobia melaloma CBS 293.54
-
-, the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
Maltoheptaose
?
show the reaction diagram
-
-
-
-
-
Maltoheptaose
?
show the reaction diagram
-
-
-
?
Maltohexaose
?
show the reaction diagram
-
-
-
?
maltopentaose
?
show the reaction diagram
-
-
-
?
maltosaccharide
?
show the reaction diagram
-
-
-
-
?
Maltosaccharides
Glucose + 1,5-anhydro-D-fructose
show the reaction diagram
-
-
-
-
-
Maltose
Glucose + 1,5-anhydro-D-fructose
show the reaction diagram
-
-
-
-
-
Maltose
Glucose + 1,5-anhydro-D-fructose
show the reaction diagram
-
-
-
-
-
maltose
D-glucose + 1,5-anhydro-D-fructose
show the reaction diagram
-
-
-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
show the reaction diagram
Anthracobia melaloma
-
-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
show the reaction diagram
-
-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
show the reaction diagram
-
the enzyme degrades alpha-maltose and beta-maltose at different rates
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
show the reaction diagram
Anthracobia melaloma CBS 293.54
-
-
-
?
Maltotetraose
?
show the reaction diagram
-
-
-
-
-
Maltotetraose
?
show the reaction diagram
-
-
-
?
p-nitrophenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
phenyl alpha-D-glucopyranoside
?
show the reaction diagram
-
-
-
?
Pullulan
?
show the reaction diagram
-
-
-
-
-
starch
?
show the reaction diagram
Anthracobia melaloma
-
-, the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
starch
?
show the reaction diagram
Anthracobia melaloma CBS 293.54
-
-, the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
starch
1,5-anhydro-D-fructose + ?
show the reaction diagram
-
-
-
-
?
maltotriose
?
show the reaction diagram
-
-
-
?
additional information
?
-
-
no activity towards glucans with alpha-1,1-linkages, alpha-1,3-linkages or alpha-1,6-linkages
-
-
-
additional information
?
-
-
the enzyme catalyzes the breakdown of alpha-1,4-glucans via a mechanism involving the formation of a covalent glycosyl-enzyme intermediate which then undergoes a syn-elimination
-
?
additional information
?
-
-
the enzyme is highly specific for alpha-1,4-glucosidic bonds found in starch-type substrates and shows low or no activity towards other types of glucosidic bonds and other types of polysaccharides
-
-
-
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
(1,4-alpha-D-glucosyl)n
1,5-anhydro-D-fructose + (1,4-alpha-D-glucosyl)n-1
show the reaction diagram
-
degradation of glycogen and starch in eukaryotes
-
-
?
Glycogen
?
show the reaction diagram
Anthracobia melaloma, Anthracobia melaloma CBS 293.54
-
the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
starch
?
show the reaction diagram
Anthracobia melaloma, Anthracobia melaloma CBS 293.54
-
the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
1.3fold activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-deoxynojirimycin
-
-
1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide hydrochloride
-
-
1-ethyl-3-(3.dimethylaminopropyl)carbodiimide
-
inhibits in a time dependent manner when an external nucleophile is added. No protection by amylopectin, maltitol or 1-deoxinojirimycin
2,4,6-trinitrobenzene-sulfonyl acid
-
-
4-chloromercuribenzoic acid
-
-
5-fluoro-beta-L-idopyranosyl fluoride
-
-
acarbose
-
competitive
bromoconduritol
-
-
Cu2+
-
10 mM, complete inactivation
deoxynojirimycin
-
with amylopectin or glycogen as substrate
deoxynojirimycin
-
-
glucose
-
with amylopectin as substrate. No effect with glycogen as substrate
Hg2+
-
1 mM, complete inactivation
hydroximinogluconolactam
-
poor
maltitol
-
with amylopectin or glycogen as substrate
N-bromosuccinimide
-
-
PCMB
-
with amylopectin or glycogen as substrate
methyl alpha-glucoside
-
with glycogen as substrate
additional information
-
no effect with 1 mM Mg2+, Zn2+, Fe2+ or Co2+
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.77
-
2,4,6-trichlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
3.8
-
2,4-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
9.9
-
2,5-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
11
-
2-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
0.59
-
3,4-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
3.1
-
3,5-dichlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
2.2
-
3-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
2.7
-
4-chloro-2-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
2.1
-
4-chlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
2.1
-
4-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
10.7
-
5-fluoro-alpha-D-glucopyranosyl fluoride
-
pH 6.0, 30C
27.9
-
alpha-D-glucopyranosyl fluoride
-
pH 6.0, 30C
28
-
alpha-D-glucopyranosyl fluoride
-
-
0.03
-
Amylopectin
-
pH 5.0, 35C, barley amylopectin or potato amylopectin
0.03
-
glycogen
-
pH 5.0, 35C, rabbit liver glycogen
0.1
-
maltoheptaose
-
pH 5.0, 35C
0.1
-
maltohexaose
-
pH 5.0, 35C
0.1
-
maltopentaose
-
pH 5.0, 35C
2.3
-
maltose
-
pH 5.0, 35C
0.1
-
maltotetraose
-
pH 5.0, 35C
0.4
-
maltotriose
-
pH 5.0, 35C
2
-
p-nitrophenyl alpha-D-glucopyranoside
-
-
4.4
-
phenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1
-
2,4,6-trichlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
27
-
2,4-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
11
-
2,5-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
5.3
-
2-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
1.7
-
3,4-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
1.5
-
3,5-dichlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
0.66
-
3-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
6.08
-
3-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
6.3
-
4-chloro-2-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
0.44
-
4-chlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
0.4
-
4-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
0.131
-
5-fluoro-alpha-D-glucopyranosyl fluoride
-
pH 6.0, 30C
505
-
alpha-D-glucopyranosyl fluoride
-
pH 6.0, 30C
505
-
alpha-D-glucopyranosyl fluoride
-
-
0.38
-
p-nitrophenyl alpha-D-glucopyranoside
-
-
0.11
-
phenyl alpha-D-glucopyranoside
-
pH 6.0, 30C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
28.3
-
5-fluoro-beta-L-idopyranosyl fluoride
-
-
0.00002
-
acarbose
-
-
0.00013
-
deoxynojirimycin
-
pH 6.0, 30C
1.33
-
hydroximinogluconolactam
-
pH 6.0, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
7
-
maltose as substrate
3.5
7.5
-
amylopectin as substrate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
6.5
-
pH 3: about 50% of maximal activity, pH 6.5: about 60% of maximal activity
4.5
8
-
pH 4.5: about 40% of maximal activity, pH 8.0: about 55% of maximal activity
5
8
-
pH 5.0: about 60% of maximal activity, pH 8.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
amylopectin as substrate
40
-
-
glycogen as substrate
43
-
-
amylopectin as substrate
45
-
-
optimal activity without addition of any salt
48
-
-
glycogen as substrate
50
-
-
maltose or amylopectin as substrate
50
-
-
optimal activity in presence of 1 mM calcium chloride
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
55
-
25C: about 60% of maximal activity, 55C: about 55% of maximal activity, glycogen as substrate
25
60
-
25C: about 40% of maximal activity, 60C: about 40% of maximal activity, glycogen as substrate
33
65
-
about 50% of maximal activity at 33C and 65C
35
50
-
35C: about 70% of maximal activity, 50C: about 70% of maximal activity, activity without addition of any salt
35
55
-
35C: about 50% of maximal activity, 55C: about 80% of maximal activity, optimal activity in presence of 1 mM calcium chloride
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
98000
-
-
gel filtration
116700
-
-
martix-assisted laser desorption mass spectrometry
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 100000, SDS-PAGE
monomer
-
1 * 111000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no glycoprotein
-
no detectable amount of carbohydrate
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
pH 5.0, 20 min, 77% loss of activity without addition of any salt, 49% loss of activity in presence of 1 mM NaCl, 41% loss of activity in presence of 10 mM calcium acetate
70
-
-
in absence of substrate, complete loss of activity after 5 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1 mM NaCl or 10 mM calcium acetate stabilize against thermal inactivation at 50C
-
glycogen stabilizes at higher temperatures
-
less than 10% loss of activity by freezing at -20C overnight and thawing, at a protein concentration of 0.07 mg/ml in 15 mM NaCl
-
glycogen stabilizes at higher temperatures
-
less than 10% loss of activity by freezing at -20C overnight and thawing, at a protein concentration of 0.07 mg/ml in 15 mM NaCl
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, bis-Tris propane-HCl buffer, pH 7.0, stable for several days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Anthracobia melaloma
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Anthracobia melaloma
-