ID: | 2.3.2.21 |
---|---|
Description: | Cyclo(L-tyrosyl-L-tyrosyl) synthase. |
Alternative Name: |
Cyclodityrosine synthase. |
Cath: | 3.40.50.11710; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.3.2.21 |
BRENDA Enzyme Link: | BRENDA 2.3.2.21 |
KEGG Enzyme Link: | KEGG2.3.2.21 |
BioCyc Enzyme Link: | BioCyc 2.3.2.21 |
ExPASy Enzyme Link: | ExPASy2.3.2.21 |
EC2PDB Enzyme Link: | EC2PDB 2.3.2.21 |
ExplorEnz Enzyme Link: | ExplorEnz 2.3.2.21 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.3.2.21 |
IntEnz Enzyme Link: | IntEnz 2.3.2.21 |
MEDLINE Enzyme Link: | MEDLINE 2.3.2.21 |
RHEA:46448 | 2 L-tyrosyl-tRNA(Tyr) = cyclo(L-tyrosyl-L-tyrosyl) + 2 tRNA(Tyr) |
RULE(radius=1) | [*:1]-[O;H0;+0:2]-[C;H0;+0:3](=[*:4])-[*:5]-[NH2;+0:6].[*:7]-[O;H0;+0:8]-[C;H0;+0:9](=[*:10])-[*:11]-[NH2;+0:12]>>[*:1]-[OH;+0:2].[*:7]-[OH;+0:8].[*:4]=[C;H0;+0:3]1-[*:5]-[NH;+0:6]-[C;H0;+0:9](=[*:10])-[*:11]-[NH;+0:12]-1 |
Reaction | ![]() |
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Core-to-Core |
Title | Authors | Date | PubMed ID |
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The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase. | Vetting MW, Hegde SS, Blanchard JS | 2010 Nov | 20852636 |
Cyclodipeptide synthases are 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, Courçon M, Masson C, Dubois S, Lautru S, Lecoq A, Hashimoto S, Genet R, Pernodet JL | 2009 Jun | 19430487 |