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 | 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 | 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 | UniProt | Comment | Textmining |
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Streptomyces galilaeus | - |
- |
- |
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 | - |
? | |
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 | Comment | Organism |
---|---|---|
AknOx | - |
Streptomyces galilaeus |
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 | 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 |