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

New: Word Map on EC 4.2.2.13
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

EC NUMBER
COMMENTARY hide
4.2.2.13
-
RECOMMENDED NAME
GeneOntology No.
exo-(1->4)-alpha-D-glucan lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
linear alpha-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-O bond cleavage
-
-
C-O-bond cleavage
-
-
-
-
elimination
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycogen degradation III (via anhydrofructose)
-
-
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).
CAS REGISTRY NUMBER
COMMENTARY hide
148710-18-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
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
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
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
(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
amylopectin
?
show the reaction diagram
-
barley amylopectin and potato amylopectin
-
?
amylopectin
D-glucose + 1,5-anhydro-D-fructose
show the reaction diagram
-
-
-
-
?
Amylopectin
Glucose + 1,5-anhydro-D-fructose
show the reaction diagram
Glycogen
?
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
D-glucose + 1,5-anhydro-D-fructose
show the reaction diagram
Maltose
Glucose + 1,5-anhydro-D-fructose
show the reaction diagram
Maltotetraose
?
show the reaction diagram
maltotriose
?
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
1,5-anhydro-D-fructose + ?
show the reaction diagram
-
-
-
-
?
starch
?
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
(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
starch
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
1.3fold activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxynojirimycin
-
-
1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide hydrochloride
-
-
2,4,6-trinitrobenzene-sulfonyl acid
-
-
4-chloromercuribenzoic acid
-
-
5-fluoro-beta-L-idopyranosyl fluoride
-
-
acarbose
bromoconduritol
-
-
Cu2+
-
10 mM, complete inactivation
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
methyl alpha-glucoside
-
with glycogen as substrate
N-bromosuccinimide
-
-
PCMB
-
with amylopectin or glycogen as substrate
additional information
-
no effect with 1 mM Mg2+, Zn2+, Fe2+ or Co2+
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
10.7
5-fluoro-alpha-D-glucopyranosyl fluoride
-
pH 6.0, 30C
27.9 - 28
alpha-D-glucopyranosyl fluoride
0.03
amylopectin
0.1
maltoheptaose
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
2,4,6-trichlorophenyl alpha-D-glucopyranoside
Gracilariopsis sp.
-
pH 6.0, 30C
27
2,4-dinitrophenyl alpha-D-glucopyranoside
Gracilariopsis sp.
-
pH 6.0, 30C
11
2,5-dinitrophenyl alpha-D-glucopyranoside
Gracilariopsis sp.
-
pH 6.0, 30C
5.3
2-nitrophenyl alpha-D-glucopyranoside
Gracilariopsis sp.
-
pH 6.0, 30C
1.7
3,4-dinitrophenyl alpha-D-glucopyranoside
Gracilariopsis sp.
-
pH 6.0, 30C
1.5
3,5-dichlorophenyl alpha-D-glucopyranoside
Gracilariopsis sp.
-
pH 6.0, 30C
0.66 - 6.08
3-nitrophenyl alpha-D-glucopyranoside
6.3
4-chloro-2-nitrophenyl alpha-D-glucopyranoside
Gracilariopsis sp.
-
pH 6.0, 30C
0.44
4-chlorophenyl alpha-D-glucopyranoside
Gracilariopsis sp.
-
pH 6.0, 30C
0.4
4-nitrophenyl alpha-D-glucopyranoside
Gracilariopsis sp.
-
pH 6.0, 30C
0.131
5-fluoro-alpha-D-glucopyranosyl fluoride
Gracilariopsis sp.
-
pH 6.0, 30C
505
alpha-D-glucopyranosyl fluoride
0.38
p-nitrophenyl alpha-D-glucopyranoside
Gracilariopsis sp.
-
-
0.11
phenyl alpha-D-glucopyranoside
Gracilariopsis sp.
-
pH 6.0, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 7
-
maltose as substrate
3.5 - 7.5
-
amylopectin as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
98000
-
gel filtration
116700
-
martix-assisted laser desorption mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 100000, SDS-PAGE
monomer
-
1 * 111000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure contains a (beta/alpha)8-barrel catalytic domain with B and B' subdomains, an N-terminal domain N, and the C-terminal domains C and D. The N-terminal domain binds a trisaccharide. Complexes of the enzyme with acarbose and 1-dexoynojirimycin and two different covalent glycosyl-enzyme intermediates show that the aspartic acid residues Asp553 and Asp665 are the catalytic nucleophile and acid, respectively. The catalytic nucleophile is in a position to act also as a base that abstracts a proton from the C2 carbon atom of the covalently bound subsite -1 glucosyl residue
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, bis-Tris propane-HCl buffer, pH 7.0, stable for several days
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Anthracobia melaloma
-