Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.108
Description:UDP-3-O-acyl-N-acetylglucosamine deacetylase.
Alternative Name: UDP-3-O-acyl-GlcNAc deacetylase.
UDP-3-O-(3-hydroxymyristoyl) N-acetylglucosamine deacetylase.
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase.
Cath: 3.30.1700.10; 3.30.230.20;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.108
BRENDA Enzyme Link: BRENDA 3.5.1.108
KEGG Enzyme Link: KEGG3.5.1.108
BioCyc Enzyme Link: BioCyc 3.5.1.108
ExPASy Enzyme Link: ExPASy3.5.1.108
EC2PDB Enzyme Link: EC2PDB 3.5.1.108
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.108
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.108
IntEnz Enzyme Link: IntEnz 3.5.1.108
MEDLINE Enzyme Link: MEDLINE 3.5.1.108
MSA:

3.5.1.108;

Phylogenetic Tree:

3.5.1.108;

Uniprot:
M-CSA:
RHEA:25209 H2O + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine = acetate + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine
RULE(radius=1) [*:1]-[NH;+0:2]-[C;H0;+0:3](=[*:4])-[*:5].[OH2;+0:6]>>[*:1]-[NH2;+0:2].[*:4]=[C;H0;+0:3](-[*:5])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway.Hyland SA, Eveland SS, Anderson MS1997 Mar9068651
Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase in Escherichia coli. The second enzymatic step of lipid a biosynthesis.Sorensen PG, Lutkenhaus J, Young K, Eveland SS, Anderson MS, Raetz CR1996 Oct 188824222
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.Young K, Silver LL, Bramhill D, Cameron P, Eveland SS, Raetz CR, Hyland SA, Anderson MS1995 Dec 228530464
Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor.Mochalkin I, Knafels JD, Lightle S2008 Mar18287278
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism.Hernick M, Gennadios HA, Whittington DA, Rusche KM, Christianson DW, Fierke CA2005 Apr 2915705580
Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis.Whittington DA, Rusche KM, Shin H, Fierke CA, Christianson DW2003 Jul 812819349
Site-directed mutagenesis of the bacterial metalloamidase UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC). Identification of the zinc binding site.Jackman JE, Raetz CR, Fierke CA2001 Jan 1611148046
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme.Jackman JE, Raetz CR, Fierke CA1999 Feb 910026271