EC |
1.14.19.70 |
Accepted name: |
mycocyclosin synthase |
Reaction: |
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
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For diagram of cyclic dipeptide biosynthesis, click here |
Glossary: |
mycocyclosin = (1S,14S)-6,9-dihydroxy-15,17-diazatetracyclo[12.2.2.13,7.18,12]icosa-3(20),4,6,8(19),9,11-hexaene-16,18-dione |
Other name(s): |
CYP121; rv2276 (locus name) |
Systematic name: |
cyclo(L-tyrosyl-L-tyrosyl),reduced ferredoxin:oxygen oxidoreductase (diarylbridge-forming) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein from the bacterium Mycobacterium tuberculosis catalysing an oxidative reaction that does not incorporate oxygen into the product. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Belin, P., Le Du, M.H., Fielding, A., Lequin, O., Jacquet, M., Charbonnier, J.B., Lecoq, A., Thai, R., Courcon, M., Masson, C., Dugave, C., Genet, R., Pernodet, J.L. and Gondry, M. Identification and structural basis of the reaction catalyzed by CYP121, an essential cytochrome P450 in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 106 (2009) 7426–7431. [DOI] [PMID: 19416919] |
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[EC 1.14.19.70 created 2013 as EC 1.14.21.9, transferred 2018 to EC 1.14.19.70] |
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EC
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1.14.21.9
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Transferred entry: | mycocyclosin synthase. Now EC 1.14.19.70, mycocyclosin synthase
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[EC 1.14.21.9 created 2013, deleted 2018] |
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EC |
2.3.2.21 |
Accepted name: |
cyclo(L-tyrosyl-L-tyrosyl) synthase |
Reaction: |
2 L-tyrosyl-tRNATyr = 2 tRNATyr + cyclo(L-tyrosyl-L-tyrosyl) |
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For diagram of cyclic dipeptide biosynthesis, click here |
Glossary: |
cyclo(L-tyrosyl-L-tyrosyl) = (3S,6S)-3,6-bis[(4-hydroxyphenyl)methyl]piperazine-2,5-dione |
Other name(s): |
Rv2275 (gene name); cYY synthase; cyclodityrosine synthase |
Systematic name: |
L-tyrosyl-tRNATyr:L-tyrosyl-tRNATyr tyrosyltransferase (cyclizing) |
Comments: |
The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the first L-tyrosine residue [2]. The protein, from the bacterium Mycobacterium tuberculosis, also forms small amounts of cyclo(L-tyrosyl-L-phenylalanyl) [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
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. and Pernodet, J.L. Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes. Nat. Chem. Biol. 5 (2009) 414–420. [DOI] [PMID: 19430487] |
2. |
Vetting, M.W., Hegde, S.S. and Blanchard, J.S. The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase. Nat. Chem. Biol. 6 (2010) 797–799. [DOI] [PMID: 20852636] |
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[EC 2.3.2.21 created 2013] |
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