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Information on EC 1.1.3.45 - aclacinomycin-N oxidase and Organism(s) Streptomyces galilaeus and UniProt Accession Q0PCD7

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.45 aclacinomycin-N oxidase
IUBMB Comments
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).
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Streptomyces galilaeus
UNIPROT: Q0PCD7
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Word Map
  • 1.1.3.45
  • sirtuins
  • deacetylation
  • nad+-dependent
  • nicotinamide
  • hyperacetylation
  • mnsod
  • caloric
  • sirt3-dependent
  • longevity
  • sirt3-mediated
  • sirts
  • sirt1-7
  • foxo3a
  • acetylome
  • honokiol
The taxonomic range for the selected organisms is: Streptomyces galilaeus
The enzyme appears in selected viruses and cellular organisms
Synonyms
aknox, aclacinomycin oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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).
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 SUBSTRATE
NATURAL 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
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
a flavoprotein. The cofactor is bicovalently attached to His70 and Cys130 as 8alpha-Ndelta1-histidyl, 6-S-cysteinyl FAD
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AKNOX_STRGJ
545
0
59014
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion technique, crystals show this type of multidomain twinning
crystal structure of AknOx with bound FAD and the product aclacinomycin Y, refined to 1.65 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E374A
-
80-100% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
E374Q
-
80-100% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
H271A
-
activity is identical to wild-type activity, oxidation of aclacinomycin N
S376A
-
80-100% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
Y144F
-
5% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
Y378F
-
activity is identical to wild-type activity, oxidation of aclacinomycin N
Y378F/Y144F
-
inactive mutant enzyme, oxidation of aclacinomycin N
Y378F/Y450F
-
4% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
Y378F/Y450F/Y144F
-
inactive mutant enzyme, oxidation of aclacinomycin N
Y450F
-
1-2% of activity compared to wild-type enzyme, oxidation of aclacinomycin N
Y450F/Y144F
-
inactive mutant enzyme, oxidation of aclacinomycin N
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sultana, A.; Alexeev, I.; Kursula, I.; Mntsl, P.; Niemi, J.; Schneider, G.
Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning
Acta Crystallogr. Sect. D
63
149-159
2007
Streptomyces galilaeus (Q0PCD7)
Manually annotated by BRENDA team
Alexeev, I.; Sultana, A.; Mntsl, P.; Niemi, J.; Schneider, G.
Aclacinomycin oxidoreductase (AknOx) from the biosynthetic pathway of the antibiotic aclacinomycin is an unusual flavoenzyme with a dual active site
Proc. Natl. Acad. Sci. USA
104
6170-6175
2007
Streptomyces galilaeus
Manually annotated by BRENDA team