Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.2.21 extracted from

  • Bourgeois, G.; Seguin, J.; Babin, M.; Belin, P.; Moutiez, M.; Mechulam, Y.; Gondry, M.; Schmitt, E.
    Structural basis for partition of the cyclodipeptide synthases into two subfamilies (2018), J. Struct. Biol., 203, 17-26 .
    View publication on PubMed
Search for more literature for 2.3.2.21

Application

Application Comment Organism
synthesis cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides that can be further used for the synthesis of diketopiperazines Mycobacterium tuberculosis

Cloned(Commentary)

Cloned (Comment) Organism
gene Rv2275, recombinant expression in Escherichia coli strain BL21AI, subcloning in Escherichia coli strain DH5alpha Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WPF9
-
-
Mycobacterium tuberculosis ATCC 25618 P9WPF9
-
-
Mycobacterium tuberculosis H37Rv P9WPF9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21AI Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides. Catalytic mechanism, overview Mycobacterium tuberculosis ?
-
-
additional information cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides. Catalytic mechanism, overview Mycobacterium tuberculosis H37Rv ?
-
-
additional information cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides. Catalytic mechanism, overview Mycobacterium tuberculosis ATCC 25618 ?
-
-

Synonyms

Synonyms Comment Organism
CDPS
-
 Mycobacterium tuberculosis
cyclo(L-tyrosyl-L-tyrosyl) synthase
-
 Mycobacterium tuberculosis
cyclodipeptide synthase
-
 Mycobacterium tuberculosis
Rv2275
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
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 Mycobacterium tuberculosis belongs to the NYH subfamily Mycobacterium tuberculosis
additional information 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. 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 Mycobacterium tuberculosis