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Information on EC 2.3.2.21 - cyclo(L-tyrosyl-L-tyrosyl) synthase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WPF9

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.21 cyclo(L-tyrosyl-L-tyrosyl) synthase
IUBMB Comments
The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the first L-tyrosine residue . The protein, from the bacterium Mycobacterium tuberculosis, also forms small amounts of cyclo(L-tyrosyl-L-phenylalanyl) .
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WPF9
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
rv2275, cyclodityrosine synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclo(L-tyrosyl-L-tyrosyl) synthase
-
cyclodipeptide synthase
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cyclodityrosine synthetase
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cYY synthase
Rv2275
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 L-tyrosyl-tRNATyr = 2 tRNATyr + cyclo(L-tyrosyl-L-tyrosyl)
show the reaction diagram
reaction proceeds via a covalent intermediate in which L-tyrosine is transferred from Tyr-tRNATyr to an active site serine, S88, by transesterification and with residue E233 serving as a critical base catalyzing dipeptide bond formation
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-tyrosyl-tRNATyr:L-tyrosyl-tRNATyr tyrosyltransferase (cyclizing)
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 L-tyrosyl-tRNATyr
2 tRNATyr + cyclo(L-tyrosyl-L-tyrosyl)
show the reaction diagram
-
-
-
?
2 L-tyrosyl-tRNALeu
2 tRNATyr + cyclo(L-tyrosyl-L-tyrosyl)
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 L-tyrosyl-tRNATyr
2 tRNATyr + cyclo(L-tyrosyl-L-tyrosyl)
show the reaction diagram
-
-
-
?
additional information
?
-
Rv2275 is established as a CDPS that catalyzes formation of cyclo(L-tyrosyl-L-tyrosyl) as its major product, along with a handful of minor products containing tyrosine
-
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
metabolism
comparison of different CDPS-containing biosynthetic pathways, enzyme Rv2275 is involved in the mycocyclosin biosynthetic pathway, overview. Rv2275 is established as a CDPS that catalyzes formation of cyclo(L-tyrosyl-L-tyrosyl) as its major product, along with a handful of minor products containing tyrosine
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
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.0 A resolution. Gene product Rv2275 is structurally related to the class Ic aminoacyl-tRNA-synthetase family of enzymes. Reaction proceeds via a covalent intermediate in which L-tyrosine is transferred from Tyr-tRNATyr to an active site serine, S88, by transesterification and with residue E233 serving as a critical base catalyzing dipeptide bond formation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21AI
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Rv2275, recombinant expression in Escherichia coli strain BL21AI, subcloning in Escherichia coli strain DH5alpha
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes
Nat. Chem. Biol.
5
414-420
2009
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Vetting, M.W.; Hegde, S.S.; Blanchard, J.S.
The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase
Nat. Chem. Biol.
6
797-799
2010
Mycobacterium tuberculosis (P9WPF9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPF9)
Manually annotated by BRENDA team
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
J. Struct. Biol.
203
17-26
2018
Mycobacterium tuberculosis (P9WPF9), Mycobacterium tuberculosis ATCC 25618 (P9WPF9), Mycobacterium tuberculosis H37Rv (P9WPF9)
Manually annotated by BRENDA team
Borgman, P.; Lopez, R.; Lane, A.
The expanding spectrum of diketopiperazine natural product biosynthetic pathways containing cyclodipeptide synthases
Org. Biomol. Chem.
17
2305-2314
2019
Mycobacterium tuberculosis (P9WPF9)
Manually annotated by BRENDA team