Information on EC 2.3.2.21 - cyclo(L-tyrosyl-L-tyrosyl) synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Mycobacterium tuberculosis

EC NUMBER
COMMENTARY hide
2.3.2.21
-
RECOMMENDED NAME
GeneOntology No.
cyclo(L-tyrosyl-L-tyrosyl) synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 L-tyrosyl-tRNATyr = 2 tRNATyr + cyclo(L-tyrosyl-L-tyrosyl)
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mycocyclosin biosynthesis
-
-
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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-tRNALeu
2 tRNATyr + cyclo(L-tyrosyl-L-tyrosyl)
show the reaction diagram
-
-
-
-
?
2 L-tyrosyl-tRNATyr
2 tRNATyr + cyclo(L-tyrosyl-L-tyrosyl)
show the reaction diagram
additional information
?
-
-
cyclodipeptides synthesized by gene product Rv2275 always contain L-tyrosine
-
-
-
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