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EC Tree
IUBMB Comments 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).
The enzyme appears in viruses and cellular organisms
Synonyms
glase, alpha-1,4-glucan lyase, ag111,
more
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(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 isozyme 1
-
Dehydratase, alpha-1,4-glucan
-
-
-
-
exo-(1,4)-alpha-D-glucan lyase
-
-
-
-
Exo-alpha-1,4-glucan lyase
alpha-1,4-Glucan lyase
-
-
-
-
alpha-1,4-Glucan lyase
-
-
Exo-alpha-1,4-glucan lyase
-
-
-
-
Exo-alpha-1,4-glucan lyase
-
-
GLase
-
-
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[(1->4)-alpha-D-glucosyl]n+1 = 1,5-anhydro-D-fructose + [(1->4)-alpha-D-glucosyl]n
[(1->4)-alpha-D-glucosyl]n+1 = 1,5-anhydro-D-fructose + [(1->4)-alpha-D-glucosyl]n
-
-
-
-
[(1->4)-alpha-D-glucosyl]n+1 = 1,5-anhydro-D-fructose + [(1->4)-alpha-D-glucosyl]n
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
-
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C-O-bond cleavage
-
-
-
-
elimination
-
-
-
-
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(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).
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(1,4-alpha-D-glucosyl)n
1,5-anhydro-D-fructose + (1,4-alpha-D-glucosyl)n-1
-
degradation of glycogen and starch in eukaryotes
-
-
?
2,4,6-trichlorophenyl alpha-D-glucopyranoside
?
-
-
-
?
2,4-dinitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
2,5-dinitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
2-nitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
3,4-dinitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
3,5-dichlorophenyl alpha-D-glucopyranoside
?
-
-
-
?
3-nitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
4-chloro-2-nitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
4-chlorophenyl alpha-D-glucopyranoside
?
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
4-nitrophenyl alpha-D-glucoside
?
-
-
-
-
?
5-fluoro-alpha-D-glucopyranosyl fluoride
?
-
-
-
?
alpha-D-glucopyranosyl fluoride
?
amylopectin
?
-
barley amylopectin and potato amylopectin
-
?
amylopectin
D-glucose + 1,5-anhydro-D-fructose
-
-
-
-
?
Amylopectin
Glucose + 1,5-anhydro-D-fructose
maltosaccharide
?
-
-
-
-
?
Maltosaccharides
Glucose + 1,5-anhydro-D-fructose
maltose
D-glucose + 1,5-anhydro-D-fructose
Maltose
Glucose + 1,5-anhydro-D-fructose
p-nitrophenyl alpha-D-glucopyranoside
?
-
-
-
?
phenyl alpha-D-glucopyranoside
?
-
-
-
?
starch
1,5-anhydro-D-fructose + ?
-
-
-
-
?
additional information
?
-
alpha-D-glucopyranosyl fluoride
?
-
-
-
?
alpha-D-glucopyranosyl fluoride
?
-
-
-
?
Amylopectin
Glucose + 1,5-anhydro-D-fructose
-
-
-
-
?
Amylopectin
Glucose + 1,5-anhydro-D-fructose
-
-
-
-
?
Amylopectin
Glucose + 1,5-anhydro-D-fructose
-
-
-
-
?
Glycogen
?
-
-
-
?
Glycogen
?
-
the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
Glycogen
?
-
the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
Glycogen
?
-
rabbit liver glycogen
-
?
Glycogen
?
-
best substrate
-
-
?
Glycogen
?
-
best substrate
-
-
?
Maltoheptaose
?
-
-
-
?
Maltoheptaose
?
-
-
-
-
?
Maltosaccharides
Glucose + 1,5-anhydro-D-fructose
-
-
-
-
?
Maltosaccharides
Glucose + 1,5-anhydro-D-fructose
-
-
-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
-
-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
-
-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
-
-
-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
-
-
-
?
maltose
D-glucose + 1,5-anhydro-D-fructose
-
the enzyme degrades alpha-maltose and beta-maltose at different rates
-
?
Maltose
Glucose + 1,5-anhydro-D-fructose
-
-
-
-
?
Maltose
Glucose + 1,5-anhydro-D-fructose
-
-
-
-
?
Maltose
Glucose + 1,5-anhydro-D-fructose
-
-
-
-
?
Maltotetraose
?
-
-
-
?
Maltotetraose
?
-
-
-
-
?
starch
?
-
-
-
?
starch
?
-
the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
starch
?
-
the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
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
-
-
?
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
?
-
-
no activity towards glucans with alpha-1,1-linkages, alpha-1,3-linkages or alpha-1,6-linkages
-
-
?
additional information
?
-
-
no activity towards glucans with alpha-1,1-linkages, alpha-1,3-linkages or alpha-1,6-linkages
-
-
?
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(1,4-alpha-D-glucosyl)n
1,5-anhydro-D-fructose + (1,4-alpha-D-glucosyl)n-1
-
degradation of glycogen and starch in eukaryotes
-
-
?
Glycogen
?
-
the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
Glycogen
?
-
the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
starch
?
-
the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
starch
?
-
the enzyme catalyzes the first step of the anhydrofructose pathway
-
?
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Ca2+
-
1.3fold activation
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1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide hydrochloride
-
-
2,4,6-trinitrobenzene-sulfonyl acid
-
-
4-chloromercuribenzoic acid
-
-
5-fluoro-beta-L-idopyranosyl fluoride
-
-
Cu2+
-
10 mM, complete inactivation
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
PCMB
-
with amylopectin or glycogen as substrate
additional information
-
no effect with 1 mM Mg2+, Zn2+, Fe2+ or Co2+
-
acarbose
-
-
deoxynojirimycin
-
-
deoxynojirimycin
-
with amylopectin or glycogen as substrate
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Abscess
The use of radioactive silver for the detection of abscesses and tumors; the concentration of Ag111 in spontaneous and experimentally induced abscesses.
Hyperopia
Noncontact thermokeratoplasty to correct hyperopia induced by laser in situ keratomileusis.
Leukemia
Video-Rate Bioluminescence Imaging of Degranulation of Mast Cells Attached to the Extracellular Matrix.
Neoplasms
The use of radioactive silver for the detection of abscesses and tumors; the concentration of Ag111 in spontaneous and experimentally induced abscesses.
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0.77
2,4,6-trichlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
3.8
2,4-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
9.9
2,5-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
11
2-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
0.59
3,4-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
3.1
3,5-dichlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
2.2
3-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
2.7
4-chloro-2-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
2.1
4-chlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
2.1
4-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
10.7
5-fluoro-alpha-D-glucopyranosyl fluoride
-
pH 6.0, 30°C
27.9 - 28
alpha-D-glucopyranosyl fluoride
0.03
amylopectin
-
pH 5.0, 35°C, barley amylopectin or potato amylopectin
0.03
glycogen
-
pH 5.0, 35°C, rabbit liver glycogen
0.1
maltoheptaose
-
pH 5.0, 35°C
0.1
maltohexaose
-
pH 5.0, 35°C
0.1
maltopentaose
-
pH 5.0, 35°C
2.3
maltose
-
pH 5.0, 35°C
0.1
maltotetraose
-
pH 5.0, 35°C
0.4
maltotriose
-
pH 5.0, 35°C
2
p-nitrophenyl alpha-D-glucopyranoside
-
-
4.4
phenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
27.9
alpha-D-glucopyranosyl fluoride
-
pH 6.0, 30°C
28
alpha-D-glucopyranosyl fluoride
-
-
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1
2,4,6-trichlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
27
2,4-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
11
2,5-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
5.3
2-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
1.7
3,4-dinitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
1.5
3,5-dichlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
0.66 - 6.08
3-nitrophenyl alpha-D-glucopyranoside
6.3
4-chloro-2-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
0.44
4-chlorophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
0.4
4-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
0.131
5-fluoro-alpha-D-glucopyranosyl fluoride
-
pH 6.0, 30°C
505
alpha-D-glucopyranosyl fluoride
0.38
p-nitrophenyl alpha-D-glucopyranoside
-
-
0.11
phenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
0.66
3-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
6.08
3-nitrophenyl alpha-D-glucopyranoside
-
pH 6.0, 30°C
505
alpha-D-glucopyranosyl fluoride
-
-
505
alpha-D-glucopyranosyl fluoride
-
pH 6.0, 30°C
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28.3
5-fluoro-beta-L-idopyranosyl fluoride
-
-
0.00013
deoxynojirimycin
-
pH 6.0, 30°C
1.33
hydroximinogluconolactam
-
pH 6.0, 30°C
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2.5 - 7
-
maltose as substrate
3.5 - 7.5
-
amylopectin as substrate
6.5
-
-
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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
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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
-
optimal activity in presence of 1 mM calcium chloride
50
-
maltose or amylopectin as substrate
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25 - 55
-
25°C: about 60% of maximal activity, 55°C: about 55% of maximal activity, glycogen as substrate
25 - 60
-
25°C: about 40% of maximal activity, 60°C: about 40% of maximal activity, glycogen as substrate
33 - 65
-
about 50% of maximal activity at 33°C and 65°C
35 - 50
-
35°C: about 70% of maximal activity, 50°C: about 70% of maximal activity, activity without addition of any salt
35 - 55
-
35°C: about 50% of maximal activity, 55°C: about 80% of maximal activity, optimal activity in presence of 1 mM calcium chloride
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CBS 293.54
-
-
brenda
CBS 293.54
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
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-
-
brenda
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Q9STC2_GRALE
1092
0
123169
TrEMBL
Secretory Pathway (Reliability: 3 )
Q9STB9_GRALE
180
0
20427
TrEMBL
other Location (Reliability: 2 )
Q9STC0_GRALE
1091
0
123255
TrEMBL
Mitochondrion (Reliability: 3 )
Q9UVY7_9PEZI
163
0
18055
TrEMBL
other Location (Reliability: 2 )
Q9STB8_GRALE
571
0
65149
TrEMBL
other Location (Reliability: 2 )
Q9UVZ1_9PEZI
1070
0
121924
TrEMBL
other Location (Reliability: 1 )
Q9STC1_GRALE
1088
0
122338
TrEMBL
Mitochondrion (Reliability: 5 )
Q9UVZ2_9PEZI
1066
0
121536
TrEMBL
other Location (Reliability: 1 )
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100000
-
x * 100000, SDS-PAGE
111000
-
1 * 111000, SDS-PAGE
116700
-
martix-assisted laser desorption mass spectrometry
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monomer
-
1 * 111000, SDS-PAGE
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no glycoprotein
-
no detectable amount of carbohydrate
no glycoprotein
-
no detectable amount of carbohydrate
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quantum mechanics/molecular mechanics study on mechanism. Residue D665 acts as an acid to protonate the glycoside oxygen, which is concerted with the cleavage of the glycoside bond. Residue D553 functions as the nucleophile to attack the anomeric carbon to form the glycosyl-enzyme intermediate. The glycosylation process follows a stepwise mechanism. The deprotonated residue D553 further acts as a catalytic base to abstract the C2-proton of the glucosyl residue. The proton abstraction in the deglycosylation/elimination step is calculated to be the rate-limiting step of the whole catalytic reaction
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
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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
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1 mM NaCl or 10 mM calcium acetate stabilize against thermal inactivation at 50°C
-
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
-
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
-
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
-
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4C, bis-Tris propane-HCl buffer, pH 7.0, stable for several days
4C, bis-Tris propane-HCl buffer, pH 7.0, stable for several days
-
4C, bis-Tris propane-HCl buffer, pH 7.0, stable for several days
-
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-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Yu, S.; Pedersen, M.
alpha-1,4-Glucan lyase, a new class of starch/glycogen-degrading enzyme. II. Subcellular localization and partial amino-acid sequence
Planta
191
137-142
1993
Gracilariopsis lemaneiformis
brenda
Yu, S.; Christensen, T.M.I.E.; Kragh, K.M.; Bojsen, K.; Marcussen, J.
Efficient purification, characterization and partial amino acid sequencing of two alpha-1,4-glucan lyases from fungi
Biochim. Biophys. Acta
1339
311-320
1997
Morchella costata, Morchella vulgaris
brenda
Yu, S.; Kenne, L.; Pedersen, M.
alpha-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. I. Efficient purification and characterization from red seaweeds
Biochim. Biophys. Acta
1156
313-320
1993
Gracilaria gracilis, Gracilariopsis lemaneiformis
brenda
Yu, S.; Ahmad, T.; Kenne, L.; Pedersen, M.
alpha-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism
Biochim. Biophys. Acta
1244
1-9
1995
Gracilariopsis lemaneiformis
brenda
Lee, S.S.; Yu, S.; Withers, S.G.
Detailed dissection of a new mechanism for glycoside cleavage: alpha-1,4-glucan lyase
Biochemistry
42
13081-13090
2003
Gracilariopsis sp.
brenda
Yoshinaga, K.; Fujisue, M.; Abe, J.; Hanashiro, I.; Takeda, Y.; Muroya, K.; Hizukuri, S.
Characterization of exo-(1,4)-alpha glucan lyase from red alga Gracilaria chorda. Activation, inactivation and the kinetic properties of the enzyme
Biochim. Biophys. Acta
1472
447-454
1999
Gracilariopsis chorda
brenda
Yu, S.; Refdahl, C.; Lundt, I.
Enzymatic description of the anhydrofructose pathway of glycogen degradation; I. Identification and purification of anhydrofructose dehydratase, ascopyrone tautomerase and alpha-1,4-glucan lyase in the fungus Anthracobia melaloma
Biochim. Biophys. Acta
1672
120-129
2004
Anthracobia melaloma, Anthracobia melaloma CBS 293.54
brenda
Lee, S.S.; Yu, S.; Withers, S.G.
alpha-1,4-glucan lyase performs a trans-elimination via a nucleophilic displacement followed by a syn-elimination
J. Am. Chem. Soc.
124
4948-4949
2002
Gracilariopsis sp.
brenda
Nyvall, P.; Pedersen, M.; Kenne, L.; Gacesa, P.
Enzyme kinetics and chemical modification of alpha-1,4-glucan lyase from Gracilariopsis sp.
Phytochemistry
54
139-145
2000
Gracilariopsis sp.
brenda
Yip, V.L.Y.; Withers, S.G.
Nature's many mechanisms for the degradation of oligosaccharides
Org. Biomol. Chem.
2
2707-2713
2004
Gracilariopsis sp.
brenda
Lundt, I.; Yu, S.
1,5-Anhydro-D-fructose: biocatalytic and chemical synthetic methods for the preparation, transformation and derivatization
Carbohydr. Res.
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2010
Gracilaria gracilis
brenda
Rozeboom, H.J.; Yu, S.; Madrid, S.; Kalk, K.H.; Zhang, R.; Dijkstra, B.W.
Crystal structure of alpha-1,4-glucan lyase, a unique glycoside hydrolase family member with a novel catalytic mechanism
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288
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2013
Gracilariopsis lemaneiformis (Q9STC1), Gracilariopsis lemaneiformis
brenda
Su, H.; Dong, L.; Liu, Y.
A QM/MM study of the catalytic mechanism of alpha-1,4-glucan lyase from the red seaweed Gracilariopsis lemaneiformis
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Gracilariopsis lemaneiformis (Q9STC1)
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brenda
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