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Information on EC 1.14.99.55 - lytic starch monooxygenase
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EC Tree
1.14.99.55 lytic starch monooxygenaseIUBMB Comments
The enzyme cleaves starch in an oxidative manner. It releases fragments of starch with a D-glucono-1,5-lactone at the reducing end. The initially formed alpha-D-glucono-1,5-lactone at the reducing end of the shortend amylose chain quickly hydrolyses spontaneously to the aldonic acid. In vitro ascorbate has been found to be able to serve as reducing agent. The enzyme contains copper at the active site.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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D-glucono-1,5-lactone-terminated malto-oligosaccharides
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short-chain malto-oligosaccharides
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Synonyms
AA13, ANIA_05463, ANIA_06103, AO090701000246, ATEG_07286, LPMO, LPMO13A, LPMO13B, MGCH7_ch7g978, More, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AA13
ANIA_05463
ANIA_06103
AO090701000246
ATEG_07286
LPMO
LPMO13A
LPMO13B
MGCH7_ch7g978
additional information
additional information
in CAZY database classified as auxiliary activity family 13, AA13
additional information
in CAZY database classified as auxiliary activity family 13, AA13
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additional information
in CAZY database classified as auxiliary activity family 13, AA13
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
starch + reduced acceptor + O2 = D-glucono-1,5-lactone-terminated malto-oligosaccharides + short-chain malto-oligosaccharides + acceptor + H2O
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SYSTEMATIC NAME
IUBMB Comments
starch, hydrogen-donor:oxygen oxidoreductase (D-glucosyl C1-hydroxylating)
The enzyme cleaves starch in an oxidative manner. It releases fragments of starch with a D-glucono-1,5-lactone at the reducing end. The initially formed alpha-D-glucono-1,5-lactone at the reducing end of the shortend amylose chain quickly hydrolyses spontaneously to the aldonic acid. In vitro ascorbate has been found to be able to serve as reducing agent. The enzyme contains copper at the active site.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylopectin + ascorbic acid + O2
malto-aldonic acids + dehydroascorbate
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-
?
starch + AH2 + O2
aldonic acid-terminated malto-oligosaccharides + A + H2O
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?
starch + cysteine + O2
malto-oligosaccharide aldonic acid + cystine + H2O
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C1-oxidized maltooligosaccharides with a degree of polymerization from DP5 to DP13, unmodified oligosaccharide species are not observed
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additional information
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no oxidative activity with phosphoric acid-swollen cellulose, chitin, polygalacturonan or esterified pectin
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?
additional information
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towards starch, the enzyme shows a binding pattern typical of CBM20-containing amylolytic hydrolases
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?
additional information
?
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towards starch, the enzyme shows a binding pattern typical of CBM20-containing amylolytic hydrolases
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?
additional information
?
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towards starch, the enzyme shows a binding pattern typical of CBM20-containing amylolytic hydrolases
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?
additional information
?
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Pyricularia oryzae ATCC MYA-4617
towards starch, the enzyme shows a binding pattern typical of CBM20-containing amylolytic hydrolases
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylopectin + ascorbic acid + O2
malto-aldonic acids + dehydroascorbate
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-
?
starch + AH2 + O2
aldonic acid-terminated malto-oligosaccharides + A + H2O
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
cellobiose dehydrogenase may serve as the physiologic electron donor. In the presence of cellobiose dehydrogenase and cellobiose the enzyme activity is comparable to that with excess ascorbate.
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
Cu2+
-
Kd value 26 nM, protein shows a mononuclear copper-based EPR signal
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cellobiose dehydrogenase
cellobiose dehydrogenase may serve as the physiologic electron donor. In the presence of cellobiose dehydrogenase and cellobiose the enzyme activity is comparable to that with excess ascorbate.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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enzyme acts in synergy with glycoside hydrolase, beta-amylase, largely enhancing maltose release from retrograded starch by beta-amylase. The largest enhancements are obtained under specific conditions using the reducing cofactor cysteine, the presence of LPMO enhances the release of maltose by beta-amylase by 100fold
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A8J8W0G0_9EURO
401
0
42901
TrEMBL
Secretory Pathway (Reliability: 1)
Q0CGA6_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
400
0
42734
TrEMBL
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Q2KEQ8_MAGO7
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
353
0
37220
TrEMBL
other Location (Reliability: 1)
Q2U8Y3_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
279
0
30859
TrEMBL
-
Q5B027_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
328
0
36354
TrEMBL
other Location (Reliability: 3)
Q5B1W7_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
385
0
40790
TrEMBL
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Q7SCE9_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
385
0
41004
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals grown in areservoir containing 0.14 M calcium chloride, 0.07 M sodium acetate, pH 4.6, 14% v/v isopropanol and 30% v/v glycerol
structure with an ordered zinc-bound active site, at 1.65 A resolution, and three structures from crystals soaked with maltooligosaccharides in solutions devoid of zinc ions, at resolutions of up to 1.10 A
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concomitant with secretion of several redoxactive enzymes
LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concommitant with secretion of several redoxactive enzymes
LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concomitant with secretion of several redoxactive enzymes
LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concomitant with secretion of several redoxactive enzymes
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LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concommitant with secretion of several redoxactive enzymes
LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concommitant with secretion of several redoxactive enzymes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lo Leggio, L.; Simmons, T.J.; Poulsen, J.C.; Frandsen, K.E.; Hemsworth, G.R.; Stringer, M.A.; von Freiesleben, P.; Tovborg, M.; Johansen, K.S.; De Maria, L.; Harris, P.V.; Soong, C.L.; Dupree, P.; Tryfona, T.; Lenfant, N.; Henrissat, B.; Davies, G.J.; Walton, P.H.
Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase
Nat. Commun.
6
5961-5961
2015
Aspergillus oryzae (Q2U8Y3), Aspergillus oryzae RIB 40 (Q2U8Y3)
brenda
Vu, V.V.; Beeson, W.T.; Span, E.A.; Farquhar, E.R.; Marletta, M,A,
A family of starch-active polysaccharide monooxygenases
Proc. Natl. Acad. Sci. USA
111
13822-13827
2014
Neurospora crassa (Q7SCE9)
brenda
Nekiunaite, L.; Arntzen, M.; Svensson, B.; Vaaje-Kolstad, G.; Hachem, M.
Lytic polysaccharide monooxygenases and other oxidative enzymes are abundantly secreted by Aspergillus nidulans grown on different starches
Biotechnol. Biofuels
9
187
2016
Aspergillus nidulans (Q5B027), Aspergillus nidulans (Q5B1W7), Aspergillus nidulans ATCC 38163 (Q5B027), Aspergillus nidulans ATCC 38163 (Q5B1W7)
brenda
Nekiunaite, L.; Isaksen, T.; Vaaje-Kolstad, G.; Abou Hachem, M.
Fungal lytic polysaccharide monooxygenases bind starch and beta-cyclodextrin similarly to amylolytic hydrolases
FEBS Lett.
590
2737-2747
2016
Aspergillus terreus (Q0CGA6), Pyricularia oryzae (Q2KEQ8), Aspergillus terreus NIH 2624 (Q0CGA6), Pyricularia oryzae ATCC MYA-4617 (Q2KEQ8)
brenda
Lo Leggio, L.; Simmons, T.J.; Poulsen, J.C.; Frandsen, K.E.; Hemsworth, G.R.; Stringer, M.A.; von Freiesleben, P.; Tovborg, M.; Johansen, K.S.; De Maria, L.; Harris, P.V.; Soong, C.L.; Dupree, P.; Tryfona, T.; Lenfant, N.; Henrissat, B.; Davies, G.J.; Walton, P.H.
Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase
Nat. Commun.
6
5961
2015
Aspergillus nidulans
brenda
Frandsen, K.; Poulsen, J.; Tovborg, M.; Johansen, K.; Lo Leggio, L.
Learning from oligosaccharide soaks of crystals of an AA13 lytic polysaccharide monooxygenase Crystal packing, ligand binding and active-site disorder
Acta Crystallogr. Sect. D
73
64-76
2017
Aspergillus oryzae (Q2U8Y3), Aspergillus oryzae ATCC 42149 (Q2U8Y3)
brenda
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Release 2023.1 (January 2023)
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