Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
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- Name help_outline aclacinomycin N Identifier CHEBI:77991 Charge 0 Formula C42H55NO15 InChIKeyhelp_outline CPUWOKRFRYWIHK-BPPBZOKFSA-N SMILEShelp_outline CC[C@@]1(O)C[C@H](O[C@H]2C[C@@H]([C@H](O[C@H]3C[C@H](O)[C@H](O[C@H]4CC[C@H](O)[C@H](C)O4)[C@H](C)O3)[C@H](C)O2)[NH+](C)C)c2c([O-])c3C(=O)c4c(O)cccc4C(=O)c3cc2[C@H]1C(=O)OC 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline aclacinomycin A Identifier CHEBI:77980 Charge 0 Formula C42H53NO15 InChIKeyhelp_outline USZYSDMBJDPRIF-SVEJIMAYSA-N SMILEShelp_outline CC[C@@]1(O)C[C@H](O[C@H]2C[C@@H]([C@H](O[C@H]3C[C@H](O)[C@H](O[C@H]4CCC(=O)[C@H](C)O4)[C@H](C)O3)[C@H](C)O2)[NH+](C)C)c2c([O-])c3C(=O)c4c(O)cccc4C(=O)c3cc2[C@H]1C(=O)OC 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O2 Identifier CHEBI:16240 (Beilstein: 3587191; CAS: 7722-84-1) help_outline Charge 0 Formula H2O2 InChIKeyhelp_outline MHAJPDPJQMAIIY-UHFFFAOYSA-N SMILEShelp_outline [H]OO[H] 2D coordinates Mol file for the small molecule Search links Involved in 426 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:37423 | RHEA:37424 | RHEA:37425 | RHEA:37426 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning.
Sultana A., Alexeev I., Kursula I., Mantsala P., Niemi J., Schneider G.
The crystal structure of aclacinomycin oxidoreductase (AknOx), a tailoring enzyme involved in the biosynthesis of the polyketide antibiotic aclacinomycin, was determined to 1.65 A resolution by multiwavelength anomalous diffraction using data from selenomethionine-substituted crystals. The crystal ... >> More
The crystal structure of aclacinomycin oxidoreductase (AknOx), a tailoring enzyme involved in the biosynthesis of the polyketide antibiotic aclacinomycin, was determined to 1.65 A resolution by multiwavelength anomalous diffraction using data from selenomethionine-substituted crystals. The crystals belong to space group P2(1), with unit-cell parameters a = 68.2, b = 264.5, c = 68.2 A, beta = 119 degrees . Analysis of the intensity statistics clearly showed the presence of pseudomerohedral twinning. The data set could also be indexed and scaled with an R(sym) of 0.072 in the orthorhombic space group C222(1) (unit-cell parameters a = 69.7, b = 117.5, c = 264.4 A), indicating the possibility of pseudomerohedral twinning along the diagonal between the monoclinic a and c directions. Refinement using this twin operator resulted in an R(free) of 24.2%. A monoclinic lattice with a = c and beta close to 120 degrees can emulate a hexagonal metric, with the possibility of a threefold twin operator along the b axis and three twin domains. Refinement assuming three-domain twinning gave a final R(free) of 26.5%. The structure of AknOx can be thus refined with comparable R(free) values using either of the twin operators separately, suggesting the possibility that crystals of AknOx contain six twin domains generated by the twofold and threefold twin operators perpendicular to each other. Both twin operators coincide with noncrystallographic symmetry axes that may promote twinning. << Less
Acta Crystallogr D Biol Crystallogr 63:149-159(2007) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Aclacinomycin oxidoreductase (AknOx) from the biosynthetic pathway of the antibiotic aclacinomycin is an unusual flavoenzyme with a dual active site.
Alexeev I., Sultana A., Maentsaelae P., Niemi J., Schneider G.
Aclacinomycin (Acl) oxidoreductase (AknOx) catalyzes the last two steps in the biosynthesis of polyketide antibiotics of the Acl group, the oxidation of the terminal sugar moiety rhodinose to l-aculose. We present the crystal structure of AknOx with bound FAD and the product AclY, refined to 1.65- ... >> More
Aclacinomycin (Acl) oxidoreductase (AknOx) catalyzes the last two steps in the biosynthesis of polyketide antibiotics of the Acl group, the oxidation of the terminal sugar moiety rhodinose to l-aculose. We present the crystal structure of AknOx with bound FAD and the product AclY, refined to 1.65-A resolution. The overall fold of AknOx identifies the enzyme as a member of the p-cresol methylhydroxylase superfamily. The cofactor is bicovalently attached to His-70 and Cys-130 as 8alpha-Ndelta1-histidyl, 6-S-cysteinyl FAD. The polyketide ligand is bound in a deep cleft in the substrate-binding domain, with the tetracyclic ring system close to the enzyme surface and the three-sugar chain extending into the protein interior. The terminal sugar residue packs against the isoalloxazine ring of FAD and positions the carbon atoms that are oxidized close to the N5 atom of FAD. The structure and site-directed mutagenesis data presented here are consistent with a mechanism where the two different reactions of AknOx are catalyzed in the same active site but by different active site residues. Tyr-450 is responsible for proton removal from the C-4 hydroxyl group in the first reaction, the oxidation of rhodinose to cinerulose A. Tyr-378 acts as a catalytic base involved in proton abstraction from C3 of cinerulose A in the second reaction, for formation L-aculose. Replacement of this residue, however, does not impair the conversion of rhodinose to cinerulose A. << Less
Proc. Natl. Acad. Sci. U.S.A. 104:6170-6175(2007) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.