KEGG   ENZYME: 1.1.3.45Help
Entry
EC 1.1.3.45                 Enzyme                                 

Name
aclacinomycin-N oxidase;
AknOx (ambiguous);
aclacinomycin oxidoreductase (ambiguous)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
aclacinomycin-N:oxygen oxidoreductase
Reaction(IUBMB)
aclacinomycin N + O2 = aclacinomycin A + H2O2 [RN:R09334]
Reaction(KEGG)
Substrate
aclacinomycin N [CPD:C18637];
O2 [CPD:C00007]
Product
aclacinomycin A [CPD:C18638];
H2O2 [CPD:C00027]
Comment
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).
History
EC 1.1.3.45 created 2013
Pathway
Biosynthesis of type II polyketide products
Biosynthesis of antibiotics
Orthology
K15949  
aclacinomycin-N/aclacinomycin-A oxidase
Reference
1  [PMID:17395717]
  Authors
Alexeev I, Sultana A, Mantsala P, Niemi J, Schneider G.
  Title
Aclacinomycin oxidoreductase (AknOx) from the biosynthetic pathway of the antibiotic aclacinomycin is an unusual flavoenzyme with a dual active site.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 6170-5.
  Sequence
Reference
2  [PMID:17242508]
  Authors
Sultana A, Alexeev I, Kursula I, Mantsala P, Niemi J, Schneider G
  Title
Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning.
  Journal
Acta. Crystallogr. D. Biol. Crystallogr. 63 (2007) 149-59.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

DBGET integrated database retrieval system