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Information on EC 3.5.1.108 - UDP-3-O-acyl-N-acetylglucosamine deacetylase
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EC Tree
3.5.1.108 UDP-3-O-acyl-N-acetylglucosamine deacetylaseIUBMB Comments
A zinc protein. The enzyme catalyses a committed step in the biosynthesis of lipid A.
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Word Map
- 3.5.1.108
- histone
- sirt1
-
deacetylation
- sirtuins
-
nad+-dependent
- chromatin
- hdacs
- nicotinamide
- acetyltransferase
- resveratrol
- nad+
- nucleosome
-
trichostatin
- repressor
-
longevity
-
lifespan
-
hyperacetylation
-
corepressors
-
calorie
-
coactivator
-
sirt1-mediated
- tubulin
-
forkhead
-
non-histone
-
proliferator-activated
-
hydroxamic
- panobinostat
- microtubule
- heterochromatin
- pgc-1alpha
-
foxos
- phenacetin
- mef2
-
deacylase
-
suberoylanilide
- romidepsin
-
aggresome
- sirtinol
-
sirt1-dependent
- synthesis
-
pan-hdac
- cortactin
- pharmacology
- medicine
- drug development
-
chromodomain
-
chromatin-remodeling
-
ubiquitin-binding
- saha
- nampt
- vorinostat
- paraoxon
-
dinucleotide-dependent
-
chromatin-modifying
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
=
+
+
=
a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
+
Synonyms
deacetylase, udp-3-o-(r-3-hydroxymyristoyl)-n-acetylglucosamine deacetylase, deacetylase lpxc, lpxc enzyme, udp-3-o-acyl-n-acetylglucosamine deacetylase, enva protein, udp-3-o-[(r)-3-hydroxymyristoyl]-n-acetylglucosamine deacetylase, udp-3-o-[r-3-hydroxymyristoyl]-glcnac deacetylase, udp-3-o-(r-3-hydroxyacyl)-n-acetylglucosamine deacetylase, lpxc protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deacetylase LpxC
LpxC
LpxC deacetylase
LpxC enzyme
LpxC protein
UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase
UDP-(3-O-acyl)-N-acetylglucosamine deacetylase
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
UDP-3-O-(acyl)-N-acetylglucosamine deacetylase
UDP-3-O-(R-3-hydroxyacyl)-N-acetylglucosamine deacetylase
UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc deacetylase
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
UDP-3-O-acyl-GlcNAc deacetylase
UDP-3-O-acyl-N-acetylglucosamine deacetylase
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase
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UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
UDP-3-O-[R-3-hydroxymyristoyl]-GlcNAc deacetylase
uridine diphosphate-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase
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deacetylase LpxC
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LpxC
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LpxC deacetylase
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LpxC enzyme
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LpxC protein
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UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase
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UDP-(3-O-acyl)-N-acetylglucosamine deacetylase
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UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
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UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
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UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
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UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
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UDP-3-O-acyl-GlcNAc deacetylase
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UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
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UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine amidohydrolase
A zinc protein. The enzyme catalyses a committed step in the biosynthesis of lipid A.
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CAS REGISTRY NUMBER
COMMENTARY
157971-99-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-(2-acetamino)-2-deoxy-3-O-[2-(hexylamino)-1-methyl-2-oxoethyl]-D-glucopyranose + H2O
UDP-2-amino-2-deoxy-3-O-[2-(hexylamino)-1-methyl-2-oxoethyl]-D-glucopyranose + acetate
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a homogenous fluorescence-based assay is developed that uses UDP3-O-(N-hexyl-propionamide)-N-acetylglucosamine as a surrogate substrate. This surrogate can be prepared from commercially available UDP-GlcNAc by enzymatic conversion to UDP-MurNAc, which is then chemically coupled to n-hexylamine. Following the LpxC reaction, the free amine of the deacetylation product can be derivatized by fluorescamine, thus generating a fluorescent signal
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-
?
UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + acetate
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-
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-alpha-D-glucosamine + acetate
UDP-3-O-[(3R)-3-hydroxydecanoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxydecanoyl]-alpha-D-glucosamine + acetate
-
-
-
-
?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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-
-
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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-
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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LpxC catalyzes a step in the biosynthesis of lipid A in Gram-negative bacteria
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-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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LpxC catalyzes the first committed step in the biosynthesis of lipid A, the hydrophobic anchor of lipopolysaccharide (LPS) that constitutes the outermost monolayer of Gram-negative bacteria. As LpxC is crucial for the survival of Gram-negative organisms and has no sequence homology to known mammalian deacetylases or amidases
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-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
LpxC catalyzes the first committed step in the biosynthesis of lipid A, the hydrophobic anchor of lipopolysaccharide (LPS) that constitutes the outermost monolayer of Gram-negative bacteria. As LpxC is crucial for the survival of Gram-negative organisms and has no sequence homology to known mammalian deacetylases or amidases
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-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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LpxC is a key enzyme in the biochemical synthesis of Lipid A
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-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
LpxC catalyzes deacetylation by using Glu78 and His265 as a general acid-base pair and the zinc-bound water as a nucleophile
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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the mechanism of LpxC proceeds via four steps: (1) initial hydroxylation of the substrates carbonyl carbon to give a gem-diolate intermediate, (2) protonation of the amide nitrogen by the histidine His265-H+, (3) a barrier-less change in the active site-intermediate hydrogen-bond network and finally, (4) C-N bond cleavage. The rate-determining step of the mechanism of LpxC is the initial hydroxylation while the final C-N bond cleavage occurs with an overall barrier of 23.6 kJ/mol. LpxC uses a general acid/base pair mechanism as indicated by the fact that both His265-H+ and Glu78 are accordingly involved
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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486257, 681983, 695538, 695629, 696180, 696193, 696198, 696206, 696209, 696210, 696322, 698451, 698550, 698700, 699038, 699421
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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natural substrate
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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biosynthesis of lipid A in Gram negarive bacteria
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
committed step in the biosynthesis of lipid A
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-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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committed step of lipopolysaccharide biosynthesis
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-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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first committed step of lipid A biosynthesis, regulation of enzyme activity, overview
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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LpxC catalyzes a step in the biosynthesis of lipid A in Gram-negative bacteria
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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LpxC is one of the key enzymes of bacterial lipid A biosynthesis, catalyzing the removal of the N-acetyl group of UD-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine. The lpxC gene is essential in Gram-negative bacteria but absent from mammalian genomes, making it an attractive target for antibacterial drug discovery
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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second enzymatic step of lipid A biosynthesis
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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the enzyme is involved in lipid A biosynthesis
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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this reaction is essential in the biosynthesis of lipopolysaccharide (LPS) of Gram-negative bacteria and is an attractive target for the development of new antibacterial agents
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
LpxC catalyzes deacetylation by using Glu78 and His265 as a general acid-base pair and the zinc-bound water as a nucleophile
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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natural substrate
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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-
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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-
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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first committed step of lipid A biosynthesis, regulation of enzyme activity, overview
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
Escherichia coli W3110 / ATCC 27325
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
Escherichia coli W3110 / ATCC 27325
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the enzyme is involved in lipid A biosynthesis
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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-
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?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
a committed step of lipopolysaccharide biosynthesis
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-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
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by placing the lpxC gene of Pseudomonas aeruginosa under tight control of an arabinose-inducible promoter, the essentiality of LpxC activity for Pseudomonas aeruginosa is demonstrated
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?
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-alpha-D-glucosamine + acetate
-
-
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?
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-alpha-D-glucosamine + acetate
-
-
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?
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-alpha-D-glucosamine + acetate
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-
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?
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-alpha-D-glucosamine + acetate
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-
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?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
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-
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?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
-
-
-
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?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
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the product diphosphate group covalently links to the glucosamine directly interacted with Lys227 and a protein loop between beta6' and alpha2' of domain II
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r
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
the enzyme catalyzes the first committed step in the biosynthesis of lipid A, an essential component of the outer membrane of Gram-negative bacteria
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?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
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-
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?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
-
-
-
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r
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
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-
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?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
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via tetrahedral transition state
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r
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
Escherichia coli W3110 / ATCC 27325
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r
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
-
-
-
-
?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
-
-
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r
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
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-
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?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
-
first committed step in the biosynthesis of lipid A
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-
?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
-
-
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?
UDP-N-acetyl-alpha-D-glucosamine + H2O
UDP-alpha-D-glucosamine + acetate
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-
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?
UDP-N-acetyl-alpha-D-glucosamine + H2O
UDP-alpha-D-glucosamine + acetate
-
kcat/KM fo UDP-N-acetylglucosamine is 5000000-fold lower than the kcat/Km for UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine
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-
?
UDP-N-acetylglucosamine + H2O
UDP-D-glucosamine + acetate
-
-
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?
UDP-N-acetylglucosamine + H2O
UDP-D-glucosamine + acetate
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-
-
?
additional information
?
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-
catalyses the second step of lipid A biosynthesis in Gram-negative bacteria
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-
?
additional information
?
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catalyzes the second step in the biosynthesis of lipid A
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?
additional information
?
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catalyzes the second step in the biosynthesis of lipid A
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-
?
additional information
?
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catalyzes the second step of lipid A biosynthesis in Gram negative bacteria
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?
additional information
?
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analysis of recognition of substrates and products by the enzyme, phosphate binding is stabilized by the catalytic Zn2+ and an extensive network of hydrogen bonds to key active site residues and myr-UDP-GlcN, overview
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?
additional information
?
-
-
catalyzes the second step in the biosynthesis of lipid A
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-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
LpxC catalyzes a step in the biosynthesis of lipid A in Gram-negative bacteria
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
LpxC catalyzes the first committed step in the biosynthesis of lipid A, the hydrophobic anchor of lipopolysaccharide (LPS) that constitutes the outermost monolayer of Gram-negative bacteria. As LpxC is crucial for the survival of Gram-negative organisms and has no sequence homology to known mammalian deacetylases or amidases
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
LpxC catalyzes the first committed step in the biosynthesis of lipid A, the hydrophobic anchor of lipopolysaccharide (LPS) that constitutes the outermost monolayer of Gram-negative bacteria. As LpxC is crucial for the survival of Gram-negative organisms and has no sequence homology to known mammalian deacetylases or amidases
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
LpxC is a key enzyme in the biochemical synthesis of Lipid A
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
-
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
natural substrate
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
biosynthesis of lipid A in Gram negarive bacteria
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
committed step in the biosynthesis of lipid A
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
committed step of lipopolysaccharide biosynthesis
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
first committed step of lipid A biosynthesis, regulation of enzyme activity, overview
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
LpxC catalyzes a step in the biosynthesis of lipid A in Gram-negative bacteria
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
LpxC is one of the key enzymes of bacterial lipid A biosynthesis, catalyzing the removal of the N-acetyl group of UD-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine. The lpxC gene is essential in Gram-negative bacteria but absent from mammalian genomes, making it an attractive target for antibacterial drug discovery
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
second enzymatic step of lipid A biosynthesis
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
the enzyme is involved in lipid A biosynthesis
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
this reaction is essential in the biosynthesis of lipopolysaccharide (LPS) of Gram-negative bacteria and is an attractive target for the development of new antibacterial agents
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
natural substrate
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
first committed step of lipid A biosynthesis, regulation of enzyme activity, overview
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
Escherichia coli W3110 / ATCC 27325
-
the enzyme is involved in lipid A biosynthesis
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
a committed step of lipopolysaccharide biosynthesis
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
by placing the lpxC gene of Pseudomonas aeruginosa under tight control of an arabinose-inducible promoter, the essentiality of LpxC activity for Pseudomonas aeruginosa is demonstrated
-
-
?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
-
-
-
r
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
the enzyme catalyzes the first committed step in the biosynthesis of lipid A, an essential component of the outer membrane of Gram-negative bacteria
-
-
?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
-
-
-
-
?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
-
-
-
-
r
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
r
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
-
-
-
-
r
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
-
first committed step in the biosynthesis of lipid A
-
-
?
additional information
?
-
-
catalyses the second step of lipid A biosynthesis in Gram-negative bacteria
-
-
?
additional information
?
-
-
catalyzes the second step in the biosynthesis of lipid A
-
-
?
additional information
?
-
-
catalyzes the second step in the biosynthesis of lipid A
-
-
?
additional information
?
-
-
catalyzes the second step of lipid A biosynthesis in Gram negative bacteria
-
-
?
additional information
?
-
-
catalyzes the second step in the biosynthesis of lipid A
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
Mn2+
-
incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+)
Ni2+
-
incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+)
Zn2+
additional information
Co2+
-
incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+)
Fe2+
-
LpxC exhibits 6-8fold higher activity with a single bound Fe2+ as the cofactor compared to Zn2+-LpxC. The catalytic metal ion bound to Fe2+-EcLpxC is five-coordinate. Both metalloenzymes have a bell-shaped dependence on pH with similar pKa values. Ligand affinity of Fe2+-LpxC compared to the Zn2+ enzyme is altered by up to 6fold. In contrast to Zn2+-LpxC, the activity of Fe2+-LpxC is redox-sensitive, and a time-dependent decrease in activity is observed under aerobic conditions
Fe2+
-
the metal bound to LpxC purified from Escherichia coli grown in minimal medium is mainly Fe(II). However, the ratio of iron/zinc bound to LpxC varies with the metal content of the medium. Fe(II) is the thermodynamically favored metal cofactor for LpxC under cellular conditions, but the metal cofactor in LpxC can switch between iron and zinc in response to perturbations in available metal ions
Zn2+
the native state of this metallohydrolase may contain a pentacoordinate zinc ion
Zn2+
-
the solution structure of LpxC in complex with the substrate-analog inhibitor 1,5-anhydro-2-C-(carboxymethyl-N-hydroxyamide)-2-deoxy-3-O-myristoyl-D-glucitol, reveals a novel alpha/beta fold, a unique zinc-binding motif and a hydrophobic passage that captures the acyl chain of the inhibitor
Zn2+
-
the substrate preferentially coordinates to the active site Zn2+ via its carbonyl oxygen between a Zn2+-bound H2O and an adjacent threonine. Furthermore, upon substrate binding a nearby Glu78 residue is found to readily deprotonate the remaining Zn2+-bound H2O
Zn2+
-
wild-type enzyme contains 0.98 mg of Zn2+ per g of protein. The low activity of LpxC variants at positions H79 and H238, coupled with the ability of Zn2+ to stimulate the activity of these enzymes and the low Zn2+ content of the purified variant enzymes suggests that these residues directly coordinate a catalytic Zn2+ in LpxC. The variants with alanine substituted at H265 or D246 also exhibit large decreases in LpxC activity, suggesting that one of these residues may constitute a third protein ligand to the active-site Zn2+
Zn2+
zinc-binding motif. The catalytic zinc ion resides at the base of an active-site cleft and adjacent to a hydrophobic tunnel occupied by a fatty acid
Zn2+
zinc-dependent enzyme. LpxC catalyzes deacetylation by using Glu78 and His265 as a general acid-base pair and the zinc-bound water as a nucleophile
Zn2+
a mechanism is suggested that includes a transition state pentacoordinate system while the zinc is tetracoordinated in the absence of substrate
Zn2+
-
incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+)
Zn2+
-
LpxC is a metalloenzyme that requires bound Zn2+ for optimal activity. The actual concentration of bound Zn2+ varies with different enzyme preparations from 1.3-3.2 mol of Zn2+/mol of LpxC with an average Zn2+ content of about 2 mol of Zn2+/mol of LpxC. No other bound metal ions are detected in purified LpxC. The bound Zn2+ can be removed from LpxC by incubation with DPA, and the bound zinc ions can be easily reconstituted by incubation with Zn2+. Reconstitution of LpxC in presence of Cd2+, Ca2+, Cu2+, or Mg2+ is equal to or below the activity of apo-LpxC, indicating that these metal ions are ineffective at substituting for Zn2+. Incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+)
Zn2+
-
the low activity of LpxC variants at positions H79 and H238, coupled with the ability of Zn2+ to stimulate the activity of these enzymes and the low Zn2+ content of the purified variant enzymes suggests that these residues directly coordinate a catalytic Zn2+ in LpxC. The variants with alanine substituted at H265 or D246 also exhibit large decreases in LpxC activity, suggesting that one of these residues may constitute a third protein ligand to the active-site Zn2+
Zn2+
-
zinc-dependent enzyme. LpxC catalyzes deacetylation by using Glu78 and His265 as a general acid-base pair and the zinc-bound water as a nucleophile
Zn2+
-
LpxC exhibits 6-8fold higher activity with a single bound Fe2+ as the cofactor compared to Zn2+-LpxC. Both metalloenzymes have a bell-shaped dependence on pH with similar pKa values. Ligand affinity of Fe2+-LpxC compared to the Zn2+ enzyme is altered by up to 6fold. In contrast to Zn2+-LpxC, the activity of Fe2+-LpxC is redox-sensitive, and a time-dependent decrease in activity is observed under aerobic conditions
Zn2+
-
the metal bound to LpxC purified from Escherichia coli grown in minimal medium is mainly Fe(II). However, the ratio of iron/zinc bound to LpxC varies with the metal content of the medium. The metal cofactor in LpxC can switch between iron and zinc in response to perturbations in available metal ions
Zn2+
zinc-dependent metalloamidase, binding structure analysis from crystal structure
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE