Information on EC 2.3.2.22 - cyclo(L-leucyl-L-leucyl) synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.2.22
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RECOMMENDED NAME
GeneOntology No.
cyclo(L-leucyl-L-leucyl) synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 L-leucyl-tRNALeu = 2 tRNALeu + cyclo(L-leucyl-L-leucyl)
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pulcherrimin biosynthesis
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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
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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PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in the apo form and complexed with substrate mimics, at 1.7-2.4 A resolutions. Data show the presence of an aminoacyl-enzyme reaction intermediate, but not a dipeptide tRNA intermediate. Reaction follows a sequential catalytic mechanism, with the successive attachment of two leucine residues on the enzyme via a conserved serine residue