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2.3.1.184: acyl-homoserine-lactone synthase

This is an abbreviated version!
For detailed information about acyl-homoserine-lactone synthase, go to the full flat file.

Word Map on EC 2.3.1.184

Reaction

an acyl-[acyl-carrier protein]
+
S-adenosyl-L-methionine
=
an [acyl-carrier protein]
+
S-methyl-5'-thioadenosine
+
an N-acyl-L-homoserine lactone

Synonyms

3-oxo-C12-HSL synthase, AbaI, ACII, acyl homoserine lactone synthase, acyl-homoserine lactone synthase, acyl-homoserine-lactone synthase, acyl-homoserinelactone synthase, acyl-HSL synthase, acylhomoserine lactone synthase, AHL synthase, AHS, AHSL synthase, AhyI, AinS, AinS protein, AurI, autoinducer synthase, autoinducer synthesis protein rhlI, C4-HSL synthase, C6-AHL synthase, CsaI, EsaI, ExpI, expIEcz, ExpISCC1, ExpISCC3065, hdtS, HHL synthase, LasI, LasI synthase, LasI/R, LasR, LuxI, LuxI protein, LuxM, More, MrlI1, MrlI2, MrtI, mtqI, N-acyl homoserine lactone synthase, N-acyl-homoserine lactone synthase, N-hexanoyl homoserine lactone synthase, NmuI, Nmul_A2390, PgaI, PhzI, PppuI, PsyI, RhlI, RhlI/R, signal synthase CviI, SmaI, SpnI, TofI, TraI, YenI, YpeRI, YspI, YspRI

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.184 acyl-homoserine-lactone synthase

Engineering

Engineering on EC 2.3.1.184 - acyl-homoserine-lactone synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
abaI_Km mutant
mutant failed to produce any detectable acyl-homoserine lactone signals
T140A
-
site-directed mutagenesis of EsaI, the mutant shows altered substrate acyl-chain length specificity compared to the wild-type enzyme
T142A
-
site-directed mutagenesis of LasI, the mutant shows slightly altered substrate acyl-chain length specificity compared to the wild-type enzyme
T142G
-
site-directed mutagenesis of LasI, the mutant shows reduced activity and altered substrate acyl-chain length specificity compared to the wild-type enzyme
T142S
-
site-directed mutagenesis of LasI, the mutant shows slightly altered substrate acyl-chain length specificity compared to the wild-type enzyme
T144V
-
site-directed mutagenesis of LasI, the mutant shows reduced activity and altered substrate acyl-chain length specificity compared to the wild-type enzyme
F69L
site-directed mutagenesis of ExpISCC1, the mutant shows altered substrate acyl-chain lemgth specificity compared to the wild-type enzyme
M127T
site-directed mutagenesis of ExpISCC1, the mutant shows altered substrate acyl-chain lemgth specificity compared to the wild-type enzyme
C126S
site-directed mutagenesis, the mutant shows 81.5% activity compared to the wild-type enzyme
C67S
site-directed mutagenesis, the mutant shows 1.9% activity compared to the wild-type enzyme
C67S/C69S
site-directed mutagenesis, the mutant shows 0.8% activity compared to the wild-type enzyme
C69S
site-directed mutagenesis, the mutant shows 30.4% activity compared to the wild-type enzyme
C89S
site-directed mutagenesis, the mutant shows 63% activity compared to the wild-type enzyme
D48N
site-directed mutagenesis, inactive mutant
D51N
site-directed mutagenesis, nearly inactive mutant
E101K
site-directed mutagenesis, inactive mutant
E144K
site-directed mutagenesis, the mutant shows 43.5% activity compared to the wild-type enzyme
E46K
site-directed mutagenesis, inactive mutant
E7K/F147L/P159E/E182G
-
strain R2: cells produce twicefold amount of butanoyl homoserine lactone compared to wild type and yield a hexanoyl homoserine lactone level comparable to the butanoyl homoserine lactone concentration
E7K/F147L/V201M
-
strain R1: cells produce twicefold amount of butanoyl homoserine lactone compared to wild type
F28L
site-directed mutagenesis, the mutant shows 0.18% activity compared to the wild-type enzyme
G159E
site-directed mutagenesis, the mutant shows 44.6% activity compared to the wild-type enzyme
G68D
site-directed mutagenesis, the mutant shows 0.075% activity compared to the wild-type enzyme
G68E
site-directed mutagenesis, inactive mutant
K150E/R154QE
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the fully active mutant LasIDELTAG
K150Q
-
site-directed mutagenesis, the mutant shows similar activity as the fully active mutant LasIDELTAG
K150Q/R154Q
-
site-directed mutagenesis, the mutant shows reduced activity compared to the fully active mutant LasIDELTAG
R104C
site-directed mutagenesis, nearly inactive mutant
R104H
site-directed mutagenesis, nearly inactive mutant
R154E
-
site-directed mutagenesis, the mutant shows reduced activity compared to the fully active mutant LasIDELTAG
R154Q
-
site-directed mutagenesis, the mutant shows similar activity as the fully active mutant LasIDELTAG
R172A
-
site-directed mutagenesis, the mutant shows increased activity compared to the fully active mutant LasIDELTAG
R24W
site-directed mutagenesis, inactive mutant
R71C
site-directed mutagenesis, the mutant shows 0.05% activity compared to the wild-type enzyme
R71H
site-directed mutagenesis, inactive mutant
S103E
site-directed mutagenesis, the mutant shows 5.4% activity compared to the wild-type enzyme
W34G
site-directed mutagenesis, the mutant shows 0.10% activity compared to the wild-type enzyme
W34Y
site-directed mutagenesis, the mutant shows 60% activity compared to the wild-type enzyme
additional information