Information on EC 2.3.2.20 - cyclo(L-leucyl-L-phenylalanyl) synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.2.20
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RECOMMENDED NAME
GeneOntology No.
cyclo(L-leucyl-L-phenylalanyl) synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe = tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
L-leucyl-tRNALeu:L-phenylalanyl-tRNAPhe leucyltransferase (cyclizing)
The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the L-phenylalanine residue [2]. The protein, found in the bacterium Streptomyces noursei, also forms cyclo(L-phenylalanyl-L-phenylalanyl), cyclo(L-methionyl-L-phenylalanyl), cyclo(L-phenylalanyl-L-tyrosyl) and cyclo(L-methionyl-L-tyrosyl) [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bacillus sp. 171095 106
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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
L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe
tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
show the reaction diagram
L-phenylalanyl-tRNAPhe + L-methionyl-tRNAMet
tRNAPhe + tRNAMet + cyclo(L-phenylalanyl-L-methionyl)
show the reaction diagram
L-phenylalanyl-tRNAPhe + L-phenylalanyl-tRNAPhe
2 tRNAPhe + cyclo(L-phenylalanyl-L-phenylalanyl)
show the reaction diagram
L-phenylalanyl-tRNAPhe + L-tyrosinyl-tRNATyr
tRNAPhe + tRNATyr + cyclo(L-phenylalanyl-L-tyrosinyl)
show the reaction diagram
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-
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?
L-tryptophanyl-tRNATrp + L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
show the reaction diagram
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-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe
tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
show the reaction diagram
L-phenylalanyl-tRNAPhe + L-methionyl-tRNAMet
tRNAPhe + tRNAMet + cyclo(L-phenylalanyl-L-methionyl)
show the reaction diagram
L-phenylalanyl-tRNAPhe + L-phenylalanyl-tRNAPhe
2 tRNAPhe + cyclo(L-phenylalanyl-L-phenylalanyl)
show the reaction diagram
L-phenylalanyl-tRNAPhe + L-tyrosinyl-tRNATyr
tRNAPhe + tRNATyr + cyclo(L-phenylalanyl-L-tyrosinyl)
show the reaction diagram
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-
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?
L-tryptophanyl-tRNATrp + L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
show the reaction diagram
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-
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?
additional information
?
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the enzyme does not accept other aromatic aminoacyl-tRNA substrates than L-tryptophanyl-tRNA
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 10% (w/v) PEG8000, 50 mM KCl, 50 mM sodium cacodylate, pH 6.0
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to 1.9 A resolution, monomer that presents a compact alpha/beta structure. It is composed of a central beta-sheet with five parallel beta strands surrounded by ten alpha helices. AlbC contains a deep pocket, highly conserved among cyclodipeptide synthases. This pocket accommodates the aminoacyl moiety of the aa-tRNA substrate
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E182A
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mutation in putative catalytic pocket, inactive
E182D
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mutation in putative catalytic pocket, about 1% of wild-type activity
E182Q
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mutation in putative catalytic pocket, inactive
F59A
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about 10% of wild-type activity
G35A
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mutation in putative catalytic pocket, about 5% of wild-type activity
G79A
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about 70% of wild-type activity
H31A
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inactive
L200N
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mutation in putative catalytic pocket
L33Y/L185D
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mutation in putative catalytic pocket, inactive
P184A
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about 40% of wild-type activity
S37A
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mutation in putative catalytic pocket, inactive
S37C
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mutation in putative catalytic pocket, about 5% of wild-type activity
W54A
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inactive
Y128A
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inactive
Y178A
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mutation in putative catalytic pocket, inactive
Y178F
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mutation in putative catalytic pocket, about 10% of wild-type activity
Y202A
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mutation in putative catalytic pocket
Y202F
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mutation in putative catalytic pocket, about 15% of wild-type activity