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ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ATP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
ATP + 2,3-bis[3-(tetradecanoyl)tetradecanoyl]-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,3,2',3'-tetrakis[3-(tetradecanoyl)tetradecanoyl]-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
-
-
-
?
ATP + 2-(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,2',3'-tris(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
-
-
-
?
ATP + 2-(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2-(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,2'-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
-
-
-
?
ATP + 3-aza-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 3-aza-2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
-
-
-
?
CTP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
CDP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
-
approx. 50% of activity with ATP
-
?
GTP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
GDP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
-
approx. 50% of activity with ATP
-
?
UTP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
UDP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
-
approx. 50% of activity with ATP
-
?
additional information
?
-
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
-
-
-
?
ATP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
-
no activity with lipid X
-
?
ATP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
-
involved with EC 2.3.1.129 and 2.4.1.182 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane
-
?
additional information
?
-
lipid IVA is bound in the putative lipid-binding pocket on the underside of the N-terminal enzyme domain. The L4 loop, which includes the Walker B motif, appears to contain important residues for binding the lipid substrate, lipid IVA binding structures of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
the interaction of residue D99 with H261 acts to increase the pKa of the imidazole moiety, which in turn serves as the catalytic base to deprotonate the 4'-hydroxyl of the DSMP substrate. The LpxK enzyme activity in vitro requires the presence of a detergent micelle and formation of a ternary LpxK-ATP/Mg2+-DSMP complex
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ATP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
-
involved with EC 2.3.1.129 and 2.4.1.182 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
ATP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
ADP + (2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.007 - 0.128
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
additional information
additional information
bi-substrate kinetics, steady-state kinetics
-
0.007
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant wild-type enzyme
0.007
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant D138A
0.007
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant D138N
0.009
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant N43A
0.0097
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant R119A
0.014
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant D139N
0.015
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant H261A
0.0174
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant E100A
0.018
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant E172A
0.028
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant Q142A
0.028
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant R72A
0.046
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant D139A
0.048
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant Y74A
0.05
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant H143A
0.128
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant R171A
0.0011
ATP
pH 8.5, 30°C, recombinant mutant D99N
0.0012
ATP
pH 8.5, 30°C, recombinant wild-type enzyme
0.0013
ATP
pH 8.5, 30°C, recombinant mutant H261A
0.0014
ATP
pH 8.5, 30°C, recombinant mutant D139N
0.0015
ATP
pH 8.5, 30°C, recombinant mutant K51A
0.0016
ATP
pH 8.5, 30°C, recombinant mutant D260A
0.0017
ATP
pH 8.5, 30°C, recombinant mutant Y74A
0.0019
ATP
pH 8.5, 30°C, recombinant mutant E100A
0.002
ATP
pH 8.5, 30°C, recombinant mutant E100D
0.0022
ATP
pH 8.5, 30°C, recombinant mutant T52A
0.0023
ATP
pH 8.5, 30°C, recombinant mutant D99E
0.0027
ATP
pH 8.5, 30°C, recombinant mutant S49A
0.0028
ATP
pH 8.5, 30°C, recombinant mutant D99A
0.0029
ATP
pH 8.5, 30°C, recombinant mutant E100Q
0.0032
ATP
pH 8.5, 30°C, recombinant mutant D138N
0.004
ATP
pH 8.5, 30°C, recombinant mutant D138A
0.005
ATP
pH 8.5, 30°C, recombinant mutant D139A
0.006
ATP
pH 8.5, 30°C, recombinant mutant S53A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00051 - 2.4
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
0.00051
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant D139A
0.0011
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant D138A
0.00123
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant E100A
0.0031
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant H261A
0.0063
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant D139N
0.0138
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant R171A
0.028
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant D138N
0.031
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant Y74A
0.036
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant R119A
0.16
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant H143A
0.35
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant Q142A
0.36
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant N43A
0.39
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant R72A
0.7
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant mutant E172A
2.4
(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate)
pH 8.5, 30°C, recombinant wild-type enzyme
0.00035
ATP
pH 8.5, 30°C, recombinant mutant D99N
0.00048
ATP
pH 8.5, 30°C, recombinant mutant D139A
0.00048
ATP
pH 8.5, 30°C, recombinant mutant E100Q
0.00083
ATP
pH 8.5, 30°C, recombinant mutant D138A
0.0013
ATP
pH 8.5, 30°C, recombinant mutant K51A
0.0013
ATP
pH 8.5, 30°C, recombinant mutant T52A
0.0015
ATP
pH 8.5, 30°C, recombinant mutant D99A
0.0027
ATP
pH 8.5, 30°C, recombinant mutant E100D
0.0029
ATP
pH 8.5, 30°C, recombinant mutant E100A
0.0046
ATP
pH 8.5, 30°C, recombinant mutant H261A
0.0076
ATP
pH 8.5, 30°C, recombinant mutant D139N
0.022
ATP
pH 8.5, 30°C, recombinant mutant Y74A
0.05
ATP
pH 8.5, 30°C, recombinant mutant D99E
0.057
ATP
pH 8.5, 30°C, recombinant mutant D138N
0.073
ATP
pH 8.5, 30°C, recombinant mutant D260A
0.47
ATP
pH 8.5, 30°C, recombinant mutant S53A
3.9
ATP
pH 8.5, 30°C, recombinant wild-type enzyme
3.9
ATP
pH 8.5, 30°C, recombinant mutant S49A
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evolution
kinase LpxK is a member of the P-loop containing nucleoside triphosphate hydrolase superfamily. The active site Walker A (P-loop) and Walker B (Mg2+-binding) motifs are common to all P-loop kinase family members
metabolism
the sixth step in the lipid A biosynthetic pathway involves phosphorylation of the tetraacyldisaccharide-1-phosphate (DSMP) intermediate by the cytosol-facing inner membrane kinase LpxK
metabolism
a model for the biosynthesis of the outer membrane in Escherichia coli is presented. The catalytic activity is dependent on the concentration of unsaturated fatty acids. LpxC is additionally regulated by an unidentified protease whose activity is independent of lipid A disaccharide concentration (the feedback source for FtsH-mediated LpxC regulation) but can be induced in vitro by palmitic acid
metabolism
tetraacyldisaccharide 4'-kinase (LpxK) of Pseudomonas aeruginosa is an important tparticipant in the biosynthesis of lipopolysaccharide
metabolism
-
tetraacyldisaccharide 4'-kinase (LpxK) of Pseudomonas aeruginosa is an important tparticipant in the biosynthesis of lipopolysaccharide
-
metabolism
-
tetraacyldisaccharide 4'-kinase (LpxK) of Pseudomonas aeruginosa is an important tparticipant in the biosynthesis of lipopolysaccharide
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metabolism
-
tetraacyldisaccharide 4'-kinase (LpxK) of Pseudomonas aeruginosa is an important tparticipant in the biosynthesis of lipopolysaccharide
-
metabolism
-
tetraacyldisaccharide 4'-kinase (LpxK) of Pseudomonas aeruginosa is an important tparticipant in the biosynthesis of lipopolysaccharide
-
metabolism
-
tetraacyldisaccharide 4'-kinase (LpxK) of Pseudomonas aeruginosa is an important tparticipant in the biosynthesis of lipopolysaccharide
-
metabolism
-
tetraacyldisaccharide 4'-kinase (LpxK) of Pseudomonas aeruginosa is an important tparticipant in the biosynthesis of lipopolysaccharide
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metabolism
-
a model for the biosynthesis of the outer membrane in Escherichia coli is presented. The catalytic activity is dependent on the concentration of unsaturated fatty acids. LpxC is additionally regulated by an unidentified protease whose activity is independent of lipid A disaccharide concentration (the feedback source for FtsH-mediated LpxC regulation) but can be induced in vitro by palmitic acid
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metabolism
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tetraacyldisaccharide 4'-kinase (LpxK) of Pseudomonas aeruginosa is an important tparticipant in the biosynthesis of lipopolysaccharide
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physiological function
enzyme LpxK is an essential membrane-bound kinase in the lipid A biosynthetic pathway. In Gram-negative bacteria, lipidA is the hydrophobic anchor of lipopolysaccharide, which makes up the outer leaflet of the asymmetric outer membrane of these organisms. This acylated disaccharide of glucosamine plays an important role in eliciting an immunogenic response to bacterial pathogens and is essential to the survival of the vast majority of these microbes
physiological function
in the reaction catalyzed by LpxK in Kdo2-lipid A biosynthesis, enzyme LpxK is responsible for the phosphorylation of the 4'-hydroxyl of tetraacyldisaccharide-1-phosphate (DSMP)
additional information
apparent steady-state kinetic parameters for LpxK activity support the formation of a ternary LpxK-ATP/Mg2+-DSMP complex. In its closed catalytically competent form, the C-terminal domain of LpxK undergoes a hinge motion to close around the nucleotide substrate upon binding. Active sites of ATP-bound enzyme LpxK are in the open form, modeling, overview
additional information
structural and kinetic studies reveal the molecular basis of lipid binding, overview. The LpxK active site recognizes the lipid's glucosamine/phosphate headgroups and only accommodates disaccharides. Steady-state kinetic analysis of multiple point mutants of the lipid-binding pocket pinpoints critical residues involved in substrate binding, and characterization of N-terminal helix truncation mutants uncovers the role of this substructure as a hydrophobic membrane anchor
additional information
the enzyme's active site is modeled with residues Tyr28, Val31, Arg35, Asn58, Val61, Gly62, Thr64, Lys66, Ser88, Arg89, Gly90, Tyr91, Glu114, Pro115, Arg72, Arg132, Asp151, Asp152, Gln155, His156, Leu180, Arg186 and Glu187
additional information
-
the enzyme's active site is modeled with residues Tyr28, Val31, Arg35, Asn58, Val61, Gly62, Thr64, Lys66, Ser88, Arg89, Gly90, Tyr91, Glu114, Pro115, Arg72, Arg132, Asp151, Asp152, Gln155, His156, Leu180, Arg186 and Glu187
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additional information
-
the enzyme's active site is modeled with residues Tyr28, Val31, Arg35, Asn58, Val61, Gly62, Thr64, Lys66, Ser88, Arg89, Gly90, Tyr91, Glu114, Pro115, Arg72, Arg132, Asp151, Asp152, Gln155, His156, Leu180, Arg186 and Glu187
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additional information
-
the enzyme's active site is modeled with residues Tyr28, Val31, Arg35, Asn58, Val61, Gly62, Thr64, Lys66, Ser88, Arg89, Gly90, Tyr91, Glu114, Pro115, Arg72, Arg132, Asp151, Asp152, Gln155, His156, Leu180, Arg186 and Glu187
-
additional information
-
the enzyme's active site is modeled with residues Tyr28, Val31, Arg35, Asn58, Val61, Gly62, Thr64, Lys66, Ser88, Arg89, Gly90, Tyr91, Glu114, Pro115, Arg72, Arg132, Asp151, Asp152, Gln155, His156, Leu180, Arg186 and Glu187
-
additional information
-
the enzyme's active site is modeled with residues Tyr28, Val31, Arg35, Asn58, Val61, Gly62, Thr64, Lys66, Ser88, Arg89, Gly90, Tyr91, Glu114, Pro115, Arg72, Arg132, Asp151, Asp152, Gln155, His156, Leu180, Arg186 and Glu187
-
additional information
-
the enzyme's active site is modeled with residues Tyr28, Val31, Arg35, Asn58, Val61, Gly62, Thr64, Lys66, Ser88, Arg89, Gly90, Tyr91, Glu114, Pro115, Arg72, Arg132, Asp151, Asp152, Gln155, His156, Leu180, Arg186 and Glu187
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additional information
-
the enzyme's active site is modeled with residues Tyr28, Val31, Arg35, Asn58, Val61, Gly62, Thr64, Lys66, Ser88, Arg89, Gly90, Tyr91, Glu114, Pro115, Arg72, Arg132, Asp151, Asp152, Gln155, His156, Leu180, Arg186 and Glu187
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apo- and ADP/Mg2+-bound forms, to a resolution of 1.9 A and 2.2 A, respectively. The enzyme consists of two alpha/beta/alpha sandwich domains connected by a two-stranded beta-sheet linker. The N-terminal domain, which has most structural homology to other family members, is responsible for catalysis at the P-loop and positioning of the disaccharide 1-phosphate substrate for phosphoryl transfer on the inner membrane. The smaller C-terminal domain helps to bind the nucleotide substrate and Mg2+ cation using a 25° hinge motion about its base
purified enzyme LpxK in complex with lipid IVA, X-ray diffraction structure determination and analysis at 3.5 A
purified LpxK in complex with the ATP analogue AMPPCP in the closed catalytically competent conformation, sitting drop vapor diffusion method, mixing of 0.70 ml well solution with 0.01 ml sample solution, containing four parts of a reservoir solution consisting of 50% v/v MPD and 0.1 M HEPES, pH 7.5, and one part protein solution containing 13 mg/ml enzyme LpxK, 4.3 mM AMP-PCP, 1 mM EDTA, 0.5% w/v DDM, 540 mM NaCl, 14% v/v glycerol, and 35 mM HEPES, pH 8.0, 20°C, 1 month, or by microseeding, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using ADP-Mg2+ LpxK structure, PDB ID 4EHY, as the search model with all ligands removed, and AMP-PCP is subsequently added to the model. Purified LpxK in complex with ATP in a pre-catalytic binding state, mixing of seventeen parts of a reservoir solution consisting of 60% v/v MPD and 0.1 M HEPES, pH 7.5, and three parts protein solution containing 7.4 mg/ml enzyme LpxK, 10 mM ATP, 1 mM EDTA, 0.35% w/v DDM, 700 mM NaCl, 18.5% v/v glycerol, and 45 mM HEPES, pH 8.0, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement using LpxK structure, PDB ID 4EHX, as the search model, ATP is subsequently added to the model. Purified LpxK in complex with a chloride anion in an inhibitory conformation of the nucleotide-binding P-loop, mixing of three parts of a reservoir solution consisting of 40% v/v MPD and 0.1 M HEPES, pH 7.5, and one part protein solution containing 8.3 mg/ml LpxK, 4 mM methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside, 0.35% w/v DDM, 625 mM NaCl, 17% v/v glycerol, and 45 mM HEPES, pH 8.0, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement using the apo enzyme LpxK structure, PDB ID 4EHX, as search model and spherical active site density refines well as a chloride ion
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D138N
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D139N
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D260A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D99A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D99E
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D99N
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
E100A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
E100D
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
E100Q
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
E172A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
G47A
about 43% of wild-type activity
G48A
about 1.8% of wild-type activity
G50A
about 0.1% of wild-type activity
H143A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
H261A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
N43A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
Q142A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
R119A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
R171A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
R72A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
S49A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
Y74A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
additional information
steady-state kinetic analysis of multiple point mutants of the lipid-binding pocket pinpoints critical residues involved in substrate binding, and construction of two N-terminal helix truncated forms of LpxK, one in which amino acids 2-12 are removed, DELTA12LpxK, and another in which amino acids 2-29 are removed, DELTA29LpxK
D138A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D138A
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity
D139A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D139A
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity
K51A
about 0.1% of wild-type activity
K51A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
S53A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
S53A
about 9.9% of wild-type activity
T52A
about 0.1% of wild-type activity
T52A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
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drug development
the enzyme structure provides a structural template for designing antibiotics and knowledge of catalysis at the membrane interface
drug development
several pharmacoinformatics tools such as comparative metabolic pathway analysis (Metacyc), data mining from a database of essential genes (DEG), homology modeling, molecular docking, pharmacophore based virtual screening, ADMET prediction, and molecular dynamics simulation are used to identify the enzyme as a drug target and identify lead compounds against this target
drug development
-
several pharmacoinformatics tools such as comparative metabolic pathway analysis (Metacyc), data mining from a database of essential genes (DEG), homology modeling, molecular docking, pharmacophore based virtual screening, ADMET prediction, and molecular dynamics simulation are used to identify the enzyme as a drug target and identify lead compounds against this target
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drug development
-
several pharmacoinformatics tools such as comparative metabolic pathway analysis (Metacyc), data mining from a database of essential genes (DEG), homology modeling, molecular docking, pharmacophore based virtual screening, ADMET prediction, and molecular dynamics simulation are used to identify the enzyme as a drug target and identify lead compounds against this target
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drug development
-
several pharmacoinformatics tools such as comparative metabolic pathway analysis (Metacyc), data mining from a database of essential genes (DEG), homology modeling, molecular docking, pharmacophore based virtual screening, ADMET prediction, and molecular dynamics simulation are used to identify the enzyme as a drug target and identify lead compounds against this target
-
drug development
-
several pharmacoinformatics tools such as comparative metabolic pathway analysis (Metacyc), data mining from a database of essential genes (DEG), homology modeling, molecular docking, pharmacophore based virtual screening, ADMET prediction, and molecular dynamics simulation are used to identify the enzyme as a drug target and identify lead compounds against this target
-
drug development
-
several pharmacoinformatics tools such as comparative metabolic pathway analysis (Metacyc), data mining from a database of essential genes (DEG), homology modeling, molecular docking, pharmacophore based virtual screening, ADMET prediction, and molecular dynamics simulation are used to identify the enzyme as a drug target and identify lead compounds against this target
-
drug development
-
several pharmacoinformatics tools such as comparative metabolic pathway analysis (Metacyc), data mining from a database of essential genes (DEG), homology modeling, molecular docking, pharmacophore based virtual screening, ADMET prediction, and molecular dynamics simulation are used to identify the enzyme as a drug target and identify lead compounds against this target
-
drug development
-
several pharmacoinformatics tools such as comparative metabolic pathway analysis (Metacyc), data mining from a database of essential genes (DEG), homology modeling, molecular docking, pharmacophore based virtual screening, ADMET prediction, and molecular dynamics simulation are used to identify the enzyme as a drug target and identify lead compounds against this target
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Ray, B.L.; Raetz, C.R.H.
The biosynthesis of gram-negative endotoxin. A novel kinase in Escherichia coli membranes that incorporates the 4-phosphate of lipid A
J. Biol. Chem.
262
1122-1128
1987
Escherichia coli
brenda
Hampton, R.Y.; Raetz, C.R.H.
Lipid A 4-kinase from Escherichia coli: enzyme assay and preparation of 4-32P-labeled probes of high specific radioactivity
Methods Enzymol.
209
466-475
1992
Escherichia coli
brenda
Garrett, T.A.; Kadrmas, J.L.; Raetz, C.R.
Identification of the gene encoding the Escherichia coli lipid A 4'-kinase. Facile phosphorylation of endotoxin analogs with recombinant LpxK
J. Biol. Chem.
272
21855-21864
1997
Escherichia coli
brenda
Emptage, R.P.; Daughtry, K.D.; Pemble, C.W.; Raetz, C.R.
Crystal structure of LpxK, the 4-kinase of lipid A biosynthesis and atypical P-loop kinase functioning at the membrane interface
Proc. Natl. Acad. Sci. USA
109
12956-12961
2012
Aquifex aeolicus (O67572), Aquifex aeolicus
brenda
Emptage, R.P.; Pemble, C.W.; York, J.D.; Raetz, C.R.; Zhou, P.
Mechanistic characterization of the tetraacyldisaccharide-1-phosphate 4-kinase LpxK involved in lipid A biosynthesis
Biochemistry
52
2280-2290
2013
Aquifex aeolicus (O67572)
brenda
Emptage, R.P.; Tonthat, N.K.; York, J.D.; Schumacher, M.A.; Zhou, P.
Structural basis of lipid binding for the membrane-embedded tetraacyldisaccharide-1-phosphate 4-kinase LpxK
J. Biol. Chem.
289
24059-24068
2014
Aquifex aeolicus (O67572)
brenda
Emiola, A.; Andrews, S.; Heller, C.; George, J.
Crosstalk between the lipopolysaccharide and phospholipid pathways during outer membrane biogenesis in Escherichia coli
Proc. Natl. Acad. Sci. USA
113
3108-3113
2016
Escherichia coli (P27300), Escherichia coli, Escherichia coli K12 (P27300)
brenda
Damale, M.; Pathan, S.; Patil, R.; Sangshetti, J.
Pharmacoinformatics approaches to identify potential hits against tetraacyldisaccharide 4'-kinase (LpxK) of Pseudomonas aeruginosa
RSC Adv.
10
32856-32874
2020
Pseudomonas aeruginosa (Q9HZM3), Pseudomonas aeruginosa ATCC 15692 (Q9HZM3), Pseudomonas aeruginosa 1C (Q9HZM3), Pseudomonas aeruginosa PRS 101 (Q9HZM3), Pseudomonas aeruginosa DSM 22644 (Q9HZM3), Pseudomonas aeruginosa CIP 104116 (Q9HZM3), Pseudomonas aeruginosa LMG 12228 (Q9HZM3), Pseudomonas aeruginosa JCM 14847 (Q9HZM3)
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brenda