Information on EC 1.1.3.45 - aclacinomycin-N oxidase

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The expected taxonomic range for this enzyme is: Streptomyces galilaeus

EC NUMBER
COMMENTARY hide
1.1.3.45
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RECOMMENDED NAME
GeneOntology No.
aclacinomycin-N oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
aclacinomycin N + O2 = aclacinomycin A + H2O2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aclacinomycin biosynthesis
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Biosynthesis of type II polyketide products
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
aclacinomycin-N:oxygen oxidoreductase
A flavoprotein (FAD). This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. The enzyme utilizes the same active site to catalyse the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y (cf. EC 1.3.3.14, aclacinomycin A oxidase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the bifunctional enzyme catalyzes the last two steps in the biosynthesis of polyketide antibiotics of the aclacinomycin group, the oxidation of the terminal sugar moiety rhodinose to cinerulose A and the oxidation of cinerulose A to L-aculose
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 aclacinomycin N + O2
2 aclacinomycin A + H2O2
show the reaction diagram
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
2 aclacinomycin N + O2
2 aclacinomycin A + H2O2
show the reaction diagram
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the bifunctional enzyme catalyzes the last two steps in the biosynthesis of polyketide antibiotics of the aclacinomycin group, the oxidation of the terminal sugar moiety rhodinose to cinerulose A and the oxidation of cinerulose A to L-aculose
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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a flavoprotein. The cofactor is bicovalently attached to His70 and Cys130 as 8alpha-Ndelta1-histidyl, 6-S-cysteinyl FAD
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of AknOx with bound FAD and the product aclacinomycin Y, refined to 1.65 A resolution
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hanging-drop vapour-diffusion technique, crystals show this type of multidomain twinning
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E374A
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80-100% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
E374Q
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80-100% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
H271A
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activity is identical to wild-type activity, oxidation of aclacinomycin N
S376A
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80-100% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
Y144F
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5% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
Y378F
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activity is identical to wild-type activity, oxidation of aclacinomycin N
Y378F/Y144F
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inactive mutant enzyme, oxidation of aclacinomycin N
Y378F/Y450F
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4% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
Y378F/Y450F/Y144F
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inactive mutant enzyme, oxidation of aclacinomycin N
Y450F
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1-2% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
Y450F/Y144F
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inactive mutant enzyme, oxidation of aclacinomycin N