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3.5.1.104: peptidoglycan-N-acetylglucosamine deacetylase

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

Word Map on EC 3.5.1.104

Reaction

peptidoglycan-N-acetyl-D-glucosamine
+
H2O
=
peptidoglycan-D-glucosamine
 +
acetate

Synonyms

BA1961, BA1977, BA2944, BC1960, Bc1974, BC3618, BC_1960, BC_1974, enzyme BC1960, enzyme BC3618, GlcNAc deacetylase, HP0310, HP310, HpPgdA, Lmo0415, MurNAc deacetylase, N-acetylglucosamine deacetylase, N-acetylglucosamine deacetylase BC1960, PdaC, peptidoglycan deacetlyase, peptidoglycan deacetylase, peptidoglycan GlcNAc deacetylase, peptidoglycan GlcNAc deacetylases, peptidoglycan N-acetylglucosamine deacetylase, peptidoglycan N-acetylglucosamine deacetylase BC1960, PG N-deacetylase, Pgd, pgdA, pgdA_1, pgdA_2, PGNG-dac, PGNGdacs, polysaccharide deacetylase, polysaccharide deacetylase C, Rv1096 protein, SfPgdA, SpPgdA, yheN, YjeA

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.104 peptidoglycan-N-acetylglucosamine deacetylase

Crystallization

Crystallization on EC 3.5.1.104 - peptidoglycan-N-acetylglucosamine deacetylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of Zn-bound enzyme
crystal structure analysis of Zn-bound and acetate-bound Bc1974 enzyme, PDB ID 5N1J, structure comparisons. Analysis of X-ray crystal structures of the NodB domain of Bc1974, the conserved catalytic core of CE4s, in the unliganded form and in complex with four known metalloenzyme inhibitors and two amino acid hydroxamates that target the active site metal
crystal structure analysis of Zn-bound enzyme
hanging-drop vapour diffusion method
hanging-drop vapour diffusion method, enzyme is crystallized in the presence of (GlcNAc)6
crystal structure analysis of Zn-bound enzyme
-
purified recombinant N-terminally His6-tagged enzyme, vapor diffusion technique, mixing of 18 mg/ml protein solution with 0.2 M ammonium sulfate, 0.1 M tris sodium citrate, pH 5.6, and 15% w/v PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution
purified recombinant N-terminally His6-tagged enzyme, vapor diffusion technique, mixing of 18 mg/ml protein solution with precipitant solution containing 0.2 M ammonium sulfate, 0.1 M tris sodium citrate, pH 5.6, and 15% w/v PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement and modeling
to 2.57 A resolution. The polypeptide folds into a single domain, characterized by a non-canonical TIM-barrel fold. Nine beta-strands are arranged in a central barrel surrounded by six alpha-helices. Four monomers are present in the asymmetric unit, arranged around a four-fold rotation axis
sitting-drop vapor diffusion method, native crystal structure and product complexes of SpPgdA