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3.5.1.108: UDP-3-O-acyl-N-acetylglucosamine deacetylase

This is an abbreviated version!
For detailed information about UDP-3-O-acyl-N-acetylglucosamine deacetylase, go to the full flat file.

Word Map on EC 3.5.1.108

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

Synonyms

deacetylase, deacetylase LpxC, DHTase, EnvA protein, 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-(R-3-hydroxymyristoyl)-Nacetylglucosamine deacetylase, UDP-3-O-acyl-GlcNAc deacetylase, UDP-3-O-acyl-N-acetylglucosamine deacetylase, UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase, UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase, UDP-3-O-[R-3-hydroxymyristoyl]-GlcNAc deacetylase, UDP-3-O-[R-3-hydroxymyristoyl]-GlcNAc deacetylase enzyme, uridine diphosphate-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase, zinc deacetylase LpxC

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.108 UDP-3-O-acyl-N-acetylglucosamine deacetylase

Application

Application on EC 3.5.1.108 - UDP-3-O-acyl-N-acetylglucosamine deacetylase

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
pharmacology
the enzyme is a target for antibiotic therapy and structure-based drug design
synthesis
-
construction of immobilized metal affinity membrane via coupling of epichlorohydrin, iminodiacetic acid, and nickel ion on a regenerated cellulose membrane. The D-hydantoin-hydrolyzing enzyme harboring a poly-His tagged residue is immobilized on the prepared membrane. By employing a membrane with nickel ion of 155.5 micromol/disc immersed in 0.1 M Tris-HCl buffer pH 8, with 0.8 M sodium chloride, an enzyme activity of 4.2 U/disc is obtained. The immobilized DHTase membrane can achieve a larger pH and thermaltolerance range than the free enzyme. 99% of enzyme activity can be retained after 15 repeated uses