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Information on EC 1.3.3.14 - aclacinomycin-A oxidase and Organism(s) Streptomyces galilaeus and UniProt Accession Q0PCD7

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EC Tree
     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.3 With oxygen as acceptor
                1.3.3.14 aclacinomycin-A 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 (cf. EC 1.1.3.45) and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y.
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Streptomyces galilaeus
UNIPROT: Q0PCD7
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The taxonomic range for the selected organisms is: Streptomyces galilaeus
The enzyme appears in selected viruses and cellular organisms
Synonyms
AknOx, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
aclacinomycin-A: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 (cf. EC 1.1.3.45) and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
aclacinomycin A + O2
aclacinomycin Y + 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
aclacinomycin A + O2
aclacinomycin Y + H2O2
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
-
5 mM, 44% inhibition
Fe2+
-
0.5 mM, 26% inhibition. 1 mM, 73% inhibition
NaN3
-
1 mM, 15% inhibition. 5 mM, 53% inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
952
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8 - 7
-
pH 3.8: about 40% of maximal activity, pH 7.0: about 65% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72000
-
gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion technique, crystals show this type of multidomain twinning
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
37°C, 3 h, stable
722462
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
pH 7, 30 min, stable
60
-
pH 7, 30 min, 20% loss of activity
80
-
pH 7, 30 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no loss of activity is observed on freezing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 10% glycerol, 0.05 M Tris-HCl, pH 7.2, stable for at least 2 months
-
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
Yoshimoto, A.; Ogasawara, T.; Kitamura, I.; Oki, T.; Inui, T.; Takeuchi, T.; Umezawa, H.
Enzymatic conversion of aclacinomycin A to Y by a specific oxidoreductase in Streptomyces
J. Antibiot.
32
472-481
1979
Streptomyces galilaeus, Streptomyces galilaeus MA144-M1 6U-21
Manually annotated by BRENDA team