Information on EC 1.14.99.B8 - lytic starch monooxygenase

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The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
1.14.99.B8
preliminary BENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
lytic starch monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
starch + AH2 + O2 = aldonic acid-terminated malto-oligosaccharides + A + H2O
show the reaction diagram
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
starch, hydrogen-donor:oxygen oxidoreductase (D-glucosyl C1-hydroxylating)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
amylopectin + ascorbic acid + O2
malto-aldonic acids + dehydroascorbate
show the reaction diagram
-
-
-
?
starch + AH2 + O2
aldonic acid-terminated malto-oligosaccharides + A + H2O
show the reaction diagram
-
-
-
?
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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
amylopectin + ascorbic acid + O2
malto-aldonic acids + dehydroascorbate
show the reaction diagram
Q7SCE9
-
-
-
?
starch + AH2 + O2
aldonic acid-terminated malto-oligosaccharides + A + H2O
show the reaction diagram
Q7SCE9
-
-
-
?
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
top print hide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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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top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30860
calculated from amino acid sequence
41000
calculated from amino acid sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methylation
the enzyme contains a methylated N-terminal histidine
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amylose resin column, followed by a size exclusion column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.99.B8)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)