Sequence of LPXC_ECOLI
EC Number:3.5.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Other sequences found for EC No. 3.5.1
EC Number:3.5.1.108
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
UDP-3-O-acyl-N-acetylglucosamine deacetylase
P0A725
Escherichia coli (strain K12)
305
33956
Reaction
a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
Other sequences found for EC No. 3.5.1.108
General information:
Sequence
0 MIKQRTLKRI VQATGVGLHT GKKVTLTLRP APANTGVIYR RTDLNPPVDF PADAKSVRDT
60 MLCTCLVNEH DVRISTVEHL NAALAGLGID NIVIEVNAPE IPIMDGSAAP FVYLLLDAGI
120 DELNCAKKFV RIKETVRVED GDKWAEFKPY NGFSLDFTID FNHPAIDSSN QRYAMNFSAD
180 AFMRQISRAR TFGFMRDIEY LQSRGLCLGG SFDCAIVVDD YRVLNEDGLR FEDEFVRHKM
240 LDAIGDLFMC GHNIIGAFTA YKSGHALNNK LLQAVLAKQE AWEYVTFQDD AELPLAFKAP
300 SAVLA
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
438508
Beall B.,Lutkenhaus J.
Sequence analysis, transcriptional organization, and insertional mutagenesis of the envA gene of Escherichia coli.
J. Bacteriol.
169
5408-5415
1987
438509
Yura T.,Mori H.,Nagai H.,Nagata T.,Ishihama A.,Fujita N.,Isono K.,Mizobuchi K.,Nakata A.
Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region.
Nucleic Acids Res.
20
3305-3308
1992
438510
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
438511
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
438512
Yi Q.-M.,Lutkenhaus J.
The nucleotide sequence of the essential cell-division gene ftsZ of Escherichia coli.
Gene
36
241-247
1985
438513
Young K.,Silver L.L.,Bramhill D.,Cameron P.,Eveland S.S.,Raetz C.R.,Hyland S.A.,Anderson M.S.
The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase.
J. Biol. Chem.
270
30384-30391
1995
438515
Kloser A.W.,Laird M.W.,Misra R.
asmB, a suppressor locus for assembly-defective OmpF mutants of Escherichia coli, is allelic to envA (lpxC).
J. Bacteriol.
178
5138-5143
1996
438516
Sorensen P.G.,Lutkenhaus J.,Young K.,Eveland S.S.,Anderson M.S.,Raetz C.R.
Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase in Escherichia coli. The second enzymatic step of lipid a biosynthesis.
J. Biol. Chem.
271
25898-25905
1996
438517
Jackman J.E.,Raetz C.R.,Fierke C.A.
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme.
Biochemistry
38
1902-1911
1999
438518
Ogura T.,Inoue K.,Tatsuta T.,Suzaki T.,Karata K.,Young K.,Su L.H.,Fierke C.A.,Jackman J.E.,Raetz C.R.,Coleman J.,Tomoyasu T.,Matsuzawa H.
Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli.
Mol. Microbiol.
31
833-844
1999
438519
Jackman J.E.,Raetz C.R.,Fierke C.A.
Site-directed mutagenesis of the bacterial metalloamidase UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC). Identification of the zinc binding site.
Biochemistry
40
514-523
2001
438520
Hernick M.,Gennadios H.A.,Whittington D.A.,Rusche K.M.,Christianson D.W.,Fierke C.A.
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism.
J. Biol. Chem.
280
16969-16978
2005
438521
Fuehrer F.,Langklotz S.,Narberhaus F.
The C-terminal end of LpxC is required for degradation by the FtsH protease.
Mol. Microbiol.
59
1025-1036
2006
438522
Barb A.W.,Zhou P.
Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase of bacterial lipid A synthesis.
Curr. Pharm. Biotechnol.
9
9-15
2008
438523
Hernick M.,Gattis S.G.,Penner-Hahn J.E.,Fierke C.A.
Activation of Escherichia coli UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase by Fe2+ yields a more efficient enzyme with altered ligand affinity.
Biochemistry
49
2246-2255
2010
438524
Gattis S.G.,Hernick M.,Fierke C.A.
Active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions.
J. Biol. Chem.
285
33788-33796
2010
438525
Langsdorf E.F.,Malikzay A.,Lamarr W.A.,Daubaras D.,Kravec C.,Zhang R.,Hart R.,Monsma F.,Black T.,Ozbal C.C.,Miesel L.,Lunn C.A.
Screening for antibacterial inhibitors of the UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) using a high-throughput mass spectrometry assay.
J. Biomol. Screen.
15
52-61
2010
438526
Langklotz S.,Schaekermann M.,Narberhaus F.
Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in enterobacteria but not in all gram-negative bacteria.
J. Bacteriol.
193
1090-1097
2011
438527
Schaekermann M.,Langklotz S.,Narberhaus F.
FtsH-mediated coordination of lipopolysaccharide biosynthesis in Escherichia coli correlates with the growth rate and the alarmone (p)ppGpp.
J. Bacteriol.
195
1912-1919
2013
438528
Clayton G.M.,Klein D.J.,Rickert K.W.,Patel S.B.,Kornienko M.,Zugay-Murphy J.,Reid J.C.,Tummala S.,Sharma S.,Singh S.B.,Miesel L.,Lumb K.J.,Soisson S.M.
Structure of the bacterial deacetylase LpxC bound to the nucleotide reaction product reveals mechanisms of oxyanion stabilization and proton transfer.
J. Biol. Chem.
288
34073-34080
2013
438529
Lee C.J.,Liang X.,Gopalaswamy R.,Najeeb J.,Ark E.D.,Toone E.J.,Zhou P.
Structural basis of the promiscuous inhibitor susceptibility of Escherichia coli LpxC.
ACS Chem. Biol.
9
237-246
2014
