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Information on EC 2.3.2.22 - cyclo(L-leucyl-L-leucyl) synthase and Organism(s) Streptomyces noursei and UniProt Accession Q8GED7

for references in articles please use BRENDA:EC2.3.2.22
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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.22 cyclo(L-leucyl-L-leucyl) synthase
IUBMB Comments
The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the first L-leucine residue . The proteins from bacteria of the genus Bacillus also form small amounts of cyclo(L-phenylalanyl-L-leucyl) and cyclo(L-leucyl-L-methionyl) .
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This record set is specific for:
Streptomyces noursei
UNIPROT: Q8GED7
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The taxonomic range for the selected organisms is: Streptomyces noursei
The enzyme appears in selected viruses and cellular organisms
Synonyms
CDPS, cLL synthase, cyclo(L-leucyl-L-leucyl) synthase, cyclodileucine synthase, cyclodipeptide synthase, pSHaeC06, Shae-CDPS, YvmC, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cLL synthase
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cyclodileucine synthase
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YvmC
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-leucyl-tRNALeu:L-leucyl-tRNALeu leucyltransferase (cyclizing)
The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the first L-leucine residue [2]. The proteins from bacteria of the genus Bacillus also form small amounts of cyclo(L-phenylalanyl-L-leucyl) and cyclo(L-leucyl-L-methionyl) [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-leucyl-tRNALeu
2 tRNALeu + cyclo(L-leucyl-L-leucyl)
show the reaction diagram
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?
additional information
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enzyme AlbC uses aminoacyl-tRNAs to synthesize various cyclodipeptides, including the reactions of cyclo(L-tyrosyl-L-tyrosyl) synthase, EC 2.3.2.21, and cyclo(L-phenylalanyl-L-leucyl) synthase, EC 2.3.2.20
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CLPS_STRNR
239
0
26774
Swiss-Prot
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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
Bacillus subtilis, Streptomyces noursei (Q8GED7)
Manually annotated by BRENDA team