EC Number   |
General Information |
Reference |
|---|
  2.3.2.22 | evolution |
CDPSs fall into two subfamilies, NYH and XYP, characterized by the presence of specific sequence signatures. Comparison of the XYP and NYH enzymes shows that the two subfamilies mainly differ in the first half of their Rossmann fold. The XYP and NYH motifs correspond to two structural solutions to facilitate the reactivity of the catalytic serine residue. The CDPS from Bacillus licheniformis belongs to the NYH subfamily |
-, 759679 |
| 2.3.2.22 | evolution |
CDPSs fall into two subfamilies, NYH and XYP, characterized by the presence of specific sequence signatures. Comparison of the XYP and NYH enzymes shows that the two subfamilies mainly differ in the first half of their Rossmann fold. The XYP and NYH motifs correspond to two structural solutions to facilitate the reactivity of the catalytic serine residue. The CDPS from Staphylococcus haemolyticus belongs to the TYH subfamily |
-, 759679 |
| 2.3.2.22 | metabolism |
comparison of different CDPS-containing biosynthetic pathways, enzyme YvmC is involved in the pulcherrimin biosynthetic pathway, overview. In Bacillus subtilis, the CDPS YvmC catalyzes formation of major product cyclo(L-leucyl-L-leucyl) as well as minor cyclic dipeptide products containing one leucine residue. The yvmC gene is part of a two gene operon with cypX |
-, 759890 |
| 2.3.2.22 | metabolism |
in Bacillus subtilis, the enzymes YvmC and CypX are involved in pulcherriminic acid biosynthesis. The cyclodipeptide synthase YvmC utilizes charged leucyl-tRNAs as substrate to catalyze the formation of cyclo-L-leucyl-L-leucyl (cLL). The cytochrome P450 CypX is implicated in the transformation of cLL into pulcherriminic acid. Pulcherriminic acid derived from cyclo-L-leucyl-L-leucyl is excreted and chelates free ferric ions to form the pulcherrimin. Analysis of mechanisms controlling the transcription of the yvmC-cypX operon, overview. The Bacillus subtilis YvmB MarR-like regulator is the major transcription factor controlling yvmC-cypX expression, involvement of YvmB as repressor in the control of yvm-CcypX expression. Expression of yvmB depends on iron availability. Genes yvmBA, yvmC-cypX and yvnB are identified for negative regulation and yisI for positive regulation. A 14-bp palindromic motif constitutes the YvmB binding site. YvmB might not control expression of yisI, whose encoding protein plays a negative role in the regulation of the sporulation initiation pathway. YvmB appears as an additional regulatory element into the cell's decision to grow or sporulate |
-, 758970 |
| 2.3.2.22 | more |
CDPSs structure comparisons, comparison of the XYP and NYH enzymes shows that the two subfamilies mainly differ in the first half of their Rossmann fold, overview. The CDPS adopts a common architecture with a monomer built around a Rossmann fold domain that displays structural similarity to the catalytic domain of the two class Ic aminoacyl-tRNA synthetases (aaRSs), TyrRS and TrpRS. It contains a deep surface-accessible pocket P1, the location of which corresponds to that of the aminoacyl-binding pocket of the two aaRSs. The XYP and the NYH architectures appear as two solutions to stabilize Y202 and facilitate the reactivity of the catalytic S37. The XYP and the NYH architectures appear as two solutions to stabilize Y202 and facilitate the reactivity of the catalytic S37. The XYP and the NYH architectures appear as two solutions to stabilize Y202 and facilitate the reactivity of the catalytic S37. Despite these differences, the key catalytic residues (S37, Y202, Y178 and E182, AlbC numbering) are conserved in all CDPSs and have a same location in the catalytic centre of the enzymes. Residues belonging to the signature sequences play parallel roles in the two subfamilies, contributing to the positioning of the catalytic serine and of the crucial Y202 residue. The mode of action of the signature residues however differs, with a more complex network of hydrogen bonds in NYH enzymes. Notably, the signature residues are located in the two catalytic loops at the switch point between the two halves of the Rossmann fold |
-, 759679 |
| 2.3.2.22 | more |
CDPSs structure comparisons, comparison of the XYP and NYH enzymes shows that the two subfamilies mainly differ in the first half of their Rossmann fold, overview. The XYP and the NYH architectures appear as two solutions to stabilize Y202 and facilitate the reactivity of the catalytic S37. The XYP and the NYH architectures appear as two solutions to stabilize Y202 and facilitate the reactivity of the catalytic S37. The XYP and the NYH architectures appear as two solutions to stabilize Y202 and facilitate the reactivity of the catalytic S37. Despite these differences, the key catalytic residues (S37, Y202, Y178 and E182, AlbC numbering) are conserved in all CDPSs and have a same location in the catalytic centre of the enzymes. Residues belonging to the signature sequences play parallel roles in the two subfamilies, contributing to the positioning of the catalytic serine and of the crucial Y202 residue. The mode of action of the signature residues however differs, with a more complex network of hydrogen bonds in NYH enzymes. Notably, the signature residues are located in the two catalytic loops at the switch point between the two halves of the Rossmann fold |
-, 759679 |
| 2.3.2.22 | more |
the CDPS catalytic mechanism entails initial covalent tethering of the aminoacyl moiety from the first aa-tRNA substrate onto a conserved active site serine (Ser) residue. Nucleophilic attack of the amino nitrogen on the carbonyl carbon from the second aa-tRNA substrate yields the first peptide bond. The resulting enzyme-linked dipeptidyl intermediate then undergoes intramolecular peptide bond formation to yield the DKP group with concomitant release from the active site. The two aa-tRNA substrates bind at different sites of the CDPS |
-, 759890 |
| 2.3.2.22 | physiological function |
cyclodipeptide synthases (CDPSs) are recognized catalysts of 2,5-diketopiperazine (DKP) assembly, employing two aminoacyl-tRNAs (aa-tRNAs) as substrates. Representative 2,5-diketopiperazine (DKP) natural products and bioactivities, overview |
-, 759890 |
