Enzymes
UniProtKB help_outline | 2 proteins |
Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
L-tyrosyl-tRNATyr
Identifier
RHEA-COMP:9706
Reactive part
help_outline
- Name help_outline 3'-(L-tyrosyl)adenylyl group Identifier CHEBI:78536 Charge -1 Formula C19H21N6O8P SMILEShelp_outline N[C@@H](Cc1ccc(O)cc1)C(=O)O[C@@H]1[C@@H](COP([O-])(-*)=O)O[C@H]([C@@H]1O)n1cnc2c(N)ncnc12 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 cyclo(L-tyrosyl-L-tyrosyl) Identifier CHEBI:65063 (CAS: 10125-11-8) help_outline Charge 0 Formula C18H18N2O4 InChIKeyhelp_outline NGPCLOGFGKJCBP-HOTGVXAUSA-N SMILEShelp_outline Oc1ccc(C[C@@H]2NC(=O)[C@H](Cc3ccc(O)cc3)NC2=O)cc1 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
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Namehelp_outline
tRNATyr
Identifier
RHEA-COMP:9707
Reactive part
help_outline
- Name help_outline AMP 3'-end residue Identifier CHEBI:78442 Charge -1 Formula C10H12N5O6P SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(-*)=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 67 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:46448 | RHEA:46449 | RHEA:46450 | RHEA:46451 | |
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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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Cyclodipeptide synthases arec a family of tRNA-dependent peptide bond-forming enzymes.
Gondry M., Sauguet L., Belin P., Thai R., Amouroux R., Tellier C., Tuphile K., Jacquet M., Braud S., Courcon M., Masson C., Dubois S., Lautru S., Lecoq A., Hashimoto S., Genet R., Pernodet J.L.
Cyclodipeptides and their derivatives belong to the diketopiperazine (DKP) family, which is comprised of a broad array of natural products that exhibit useful biological properties. In the few known DKP biosynthetic pathways, nonribosomal peptide synthetases (NRPSs) are involved in the synthesis o ... >> More
Cyclodipeptides and their derivatives belong to the diketopiperazine (DKP) family, which is comprised of a broad array of natural products that exhibit useful biological properties. In the few known DKP biosynthetic pathways, nonribosomal peptide synthetases (NRPSs) are involved in the synthesis of cyclodipeptides that constitute the DKP scaffold, except in the albonoursin (1) pathway. Albonoursin, or cyclo(alpha,beta-dehydroPhe-alpha,beta-dehydroLeu), is an antibacterial DKP produced by Streptomyces noursei. In this pathway, the formation of the cyclo(Phe-Leu) (2) intermediate is catalyzed by AlbC, a small protein unrelated to NRPSs. We demonstrated that AlbC uses aminoacyl-tRNAs as substrates to catalyze the formation of the DKP peptide bonds. Moreover, several other bacterial proteins, presenting moderate similarity to AlbC, also use aminoacyl-tRNAs to synthesize various cyclodipeptides. Therefore, AlbC and these related proteins belong to a newly defined family of enzymes that we have named cyclodipeptide synthases (CDPSs). << Less
Nat. Chem. Biol. 5:414-420(2009) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase.
Vetting M.W., Hegde S.S., Blanchard J.S.
The Mycobacterium tuberculosis enzyme Rv2275 catalyzes the formation of cyclo(L-Tyr-L-Tyr) using two molecules of Tyr-tRNA(Tyr) as substrates. The three-dimensional (3D) structure of Rv2275 was determined to 2.0-Å resolution, revealing that Rv2275 is structurally related to the class Ic aminoacyl- ... >> More
The Mycobacterium tuberculosis enzyme Rv2275 catalyzes the formation of cyclo(L-Tyr-L-Tyr) using two molecules of Tyr-tRNA(Tyr) as substrates. The three-dimensional (3D) structure of Rv2275 was determined to 2.0-Å resolution, revealing that Rv2275 is structurally related to the class Ic aminoacyl-tRNA synthetase family of enzymes. Mutagenesis and radioactive labeling suggests a covalent intermediate in which L-tyrosine is transferred from Tyr-tRNA(Tyr) to an active site serine (Ser88) by transesterification with Glu233 serving as a critical base, catalyzing dipeptide bond formation. << Less