The Enzyme Database

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EC 1.1.3.45     
Accepted name: aclacinomycin-N oxidase
Reaction: aclacinomycin N + O2 = aclacinomycin A + H2O2
For diagram of aclacinomycin A and Y biosynthesis, click here
Glossary: aclacinomycin N = 2-ethyl-2,5,7-trihydroxy-6,11-dioxo-4-[[2,3,6-trideoxy-4-O-[2,6-dideoxy-4-O-[(2S,5S,6S)-5-hydroxy-6-methyltetrahydro-2H-pyran-2-yl]-α-L-lyxo-hexopyranosyl]-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy]-1,2,3,4,6,11-hexahydronaphthacene-1-carboxylic acid methyl ester
aclacinomycin A = 2-ethyl-2,5,7-trihydroxy-6,11-dioxo-4-[[2,3,6-trideoxy-4-O-[2,6-dideoxy-4-O-[(2R,6S)-6-methyl-5-oxotetrahydro-2H-pyran-2-yl]-α-L-lyxo-hexopyranosyl]-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy]-1,2,3,4,6,11-hexahydronaphthacene-1-carboxylic acid methyl ester
Other name(s): AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous)
Systematic name: aclacinomycin-N:oxygen oxidoreductase
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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Alexeev, I., Sultana, A., Mantsala, P., Niemi, J. and 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 (2007) 6170–6175. [DOI] [PMID: 17395717]
2.  Sultana, A., Alexeev, I., Kursula, I., Mantsala, P., Niemi, J. and Schneider, G. Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning. Acta Crystallogr. D Biol. Crystallogr. 63 (2007) 149–159. [DOI] [PMID: 17242508]
[EC 1.1.3.45 created 2013]
 
 
EC 1.3.3.14     
Accepted name: aclacinomycin-A oxidase
Reaction: aclacinomycin A + O2 = aclacinomycin Y + H2O2
For diagram of aclacinomycin A and Y biosynthesis, click here
Glossary: aclacinomycin A = 2-ethyl-1,2,3,4,6,11-hexahydro-2,5,7-trihydroxy-6,11-dioxo-4-[[2,3,6-trideoxy-4-O-[2,6-dideoxy-4-O-[(2R,6S)-tetrahydro-6-methyl-5-oxo-2H-pyran-2-yl]-α-L-lyxo-hexopyranosyl]-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy]naphthacene-1-carboxylic acid methyl ester
aclacinomycin Y = 2-ethyl-1,2,3,4,6,11-hexahydro-2,5,7-trihydroxy-6,11-dioxo-4-[[2,3,6-trideoxy-4-O-[2,6-dideoxy-4-O-[(2R,6S)-5,6-dihydro-6-methyl-5-oxo-2H-pyran-2-yl]-α-L-lyxo-hexopyranosyl]-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy]naphthacene-1-carboxylic acid methyl ester
Other name(s): AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous)
Systematic name: aclacinomycin-A:oxygen oxidoreductase
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Yoshimoto, A., Ogasawara, T., Kitamura, I., Oki, T., Inui, T., Takeuchi, T. and Umezawa, H. Enzymatic conversion of aclacinomycin A to Y by a specific oxidoreductase in Streptomyces. J. Antibiot. (Tokyo) 32 (1979) 472–481. [PMID: 528393]
2.  Alexeev, I., Sultana, A., Mantsala, P., Niemi, J. and 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 (2007) 6170–6175. [DOI] [PMID: 17395717]
3.  Sultana, A., Alexeev, I., Kursula, I., Mantsala, P., Niemi, J. and Schneider, G. Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning. Acta Crystallogr. D Biol. Crystallogr. 63 (2007) 149–159. [DOI] [PMID: 17242508]
[EC 1.3.3.14 created 2013]
 
 


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