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Literature summary for 1.1.3.45 extracted from

  • Alexeev, I.; Sultana, A.; Mäntsälä, 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 (2007), Proc. Natl. Acad. Sci. USA, 104, 6170-6175.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of AknOx with bound FAD and the product aclacinomycin Y, refined to 1.65 A resolution Streptomyces galilaeus

Protein Variants

Protein Variants Comment Organism
E374A 80-100% of activity compared to wild-type enzyme, oxidation of aclacinomycin N Streptomyces galilaeus
E374Q 80-100% of activity compared to wild-type enzyme, oxidation of aclacinomycin N Streptomyces galilaeus
H271A activity is identical to wild-type activity, oxidation of aclacinomycin N Streptomyces galilaeus
S376A 80-100% of activity compared to wild-type enzyme, oxidation of aclacinomycin N Streptomyces galilaeus
Y144F 5% of activity compared to wild-type enzyme, oxidation of aclacinomycin N Streptomyces galilaeus
Y378F activity is identical to wild-type activity, oxidation of aclacinomycin N Streptomyces galilaeus
Y378F/Y144F inactive mutant enzyme, oxidation of aclacinomycin N Streptomyces galilaeus
Y378F/Y450F 4% of activity compared to wild-type enzyme, oxidation of aclacinomycin N Streptomyces galilaeus
Y378F/Y450F/Y144F inactive mutant enzyme, oxidation of aclacinomycin N Streptomyces galilaeus
Y450F 1-2% of activity compared to wild-type enzyme, oxidation of aclacinomycin N Streptomyces galilaeus
Y450F/Y144F inactive mutant enzyme, oxidation of aclacinomycin N Streptomyces galilaeus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 aclacinomycin N + O2 Streptomyces galilaeus 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 2 aclacinomycin A + H2O2
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Organism

Organism UniProt Comment Textmining
Streptomyces galilaeus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 aclacinomycin N + O2 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 Streptomyces galilaeus 2 aclacinomycin A + H2O2
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2 aclacinomycin N + O2 bifunctional enzyme. The two different reactions of AknOx are catalyzed in the same active site but by different active site residues. Tyr450 is responsible for proton removal from the C4 hydroxyl group in the first reaction, the oxidation of rhodinose to cinerulose A. Tyr378 acts as a catalytic base involved in proton abstraction from C3 of cinerulose A in the second reaction, for formation L-aculose Streptomyces galilaeus 2 aclacinomycin A + H2O2
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Synonyms

Synonyms Comment Organism
AknOx
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Streptomyces galilaeus

Cofactor

Cofactor Comment Organism Structure
FAD a flavoprotein. The cofactor is bicovalently attached to His70 and Cys130 as 8alpha-Ndelta1-histidyl, 6-S-cysteinyl FAD Streptomyces galilaeus

General Information

General Information Comment Organism
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 Streptomyces galilaeus