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EC 3.5.1.104 Details

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EC number

3.5.1.104

Accepted name

peptidoglycan-N-acetylglucosamine deacetylase

Reaction

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

Other name(s)

HP310, PgdA, SpPgdA, BC1960, peptidoglycan deacetylase, N-acetylglucosamine deacetylase, peptidoglycan GlcNAc deacetylase, peptidoglycan N-acetylglucosamine deacetylase, PG N-deacetylase

Systematic name

peptidoglycan-N-acetylglucosamine amidohydrolase

Comment

Modification of peptidoglycan by N-deacetylation is an important factor in virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis [4-6]. The enzyme from Streptococcus pneumoniae is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively [3].

History

created 2010

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.14.1 With NADH or NADPH as one donor (deleted sub-subclass)

1.14.2 With ascorbate as one donor (deleted sub-subclass)

1.14.3 With reduced pteridine as one donor (deleted sub-subclass)

1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor

1.14.11.1 γ-butyrobetaine dioxygenase

1.14.11.2 procollagen-proline 4-dioxygenase

1.14.11.3 pyrimidine-deoxynucleoside 2′-dioxygenase

1.14.11.4 procollagen-lysine 5-dioxygenase

1.14.11.5 created 1972, deleted 1976

1.14.11.6 thymine dioxygenase

1.14.11.7 procollagen-proline 3-dioxygenase

1.14.11.8 trimethyllysine dioxygenase

1.14.11.9 flavanone 3-dioxygenase

1.14.11.10 pyrimidine-deoxynucleoside 1′-dioxygenase

1.14.11.11 hyoscyamine (6S)-dioxygenase

1.14.11.12 gibberellin-44 dioxygenase

1.14.11.13 gibberellin 2β-dioxygenase

1.14.11.14 6β-hydroxyhyoscyamine epoxidase

1.14.11.15 gibberellin 3β-dioxygenase

1.14.11.16 peptide-aspartate β-dioxygenase

1.14.11.17 taurine dioxygenase

1.14.11.18 phytanoyl-CoA dioxygenase

1.14.11.19 anthocyanidin synthase

1.14.11.20 deacetoxyvindoline 4-hydroxylase

1.14.11.21 clavaminate synthase

1.14.11.22 flavone synthase

1.14.11.23 flavonol synthase

1.14.11.24 2′-deoxymugineic-acid 2′-dioxygenase

1.14.11.25 mugineic-acid 3-dioxygenase

1.14.11.26 deacetoxycephalosporin-C hydroxylase

1.14.11.27 [histone H3]-dimethyl-L-lysine³⁶ demethylase

1.14.11.28 proline 3-hydroxylase

1.14.11.29 hypoxia-inducible factor-proline dioxygenase

1.14.11.30 hypoxia-inducible factor-asparagine dioxygenase

1.14.11.31 thebaine 6-O-demethylase

1.14.11.32 codeine 3-O-demethylase

1.14.11.33 DNA oxidative demethylase

1.14.11.34 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)

1.14.11.35 1-deoxypentalenic acid 11β-hydroxylase

1.14.11.36 pentalenolactone F synthase

1.14.11.37 kanamycin B dioxygenase

1.14.11.38 verruculogen synthase

1.14.11.39 L-asparagine hydroxylase

1.14.11.40 enduracididine β-hydroxylase

1.14.11.41 L-arginine hydroxylase

1.14.11.42 tRNA^Phe (7-(3-amino-3-carboxypropyl)wyosine³⁷-C²)-hydroxylase

1.14.11.43 (S)-dichlorprop dioxygenase (2-oxoglutarate)

1.14.11.44 (R)-dichlorprop dioxygenase (2-oxoglutarate)

1.14.11.45 L-isoleucine 4-hydroxylase

1.14.11.46 2-aminoethylphosphonate dioxygenase

1.14.11.47 [50S ribosomal protein L16]-arginine 3-hydroxylase

1.14.11.48 xanthine dioxygenase

1.14.11.49 uridine-5′-phosphate dioxygenase

1.14.11.50 (–)-deoxypodophyllotoxin synthase

1.14.11.51 DNA N⁶-methyladenine demethylase

1.14.11.52 validamycin A dioxygenase

1.14.11.53 mRNA N⁶-methyladenine demethylase

1.14.11.54 mRNA N¹-methyladenine demethylase

1.14.11.55 ectoine hydroxylase

1.14.11.56 L-proline cis-4-hydroxylase

1.14.11.57 L-proline trans-4-hydroxylase

1.14.11.58 ornithine lipid ester-linked acyl 2-hydroxylase

1.14.11.59 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase

1.14.11.60 scopoletin 8-hydroxylase

1.14.11.61 feruloyl-CoA 6-hydroxylase

1.14.11.62 trans-4-coumaroyl-CoA 2-hydroxylase

1.14.11.63 peptidyl-lysine (3S)-dioxygenase

1.14.11.64 glutarate dioxygenase

1.14.11.65 [histone H3]-dimethyl-L-lysine⁹ demethylase

1.14.11.66 [histone H3]-trimethyl-L-lysine⁹ demethylase

1.14.11.67 [histone H3]-trimethyl-L-lysine⁴ demethylase

1.14.11.68 [histone H3]-trimethyl-L-lysine²⁷ demethylase

1.14.11.69 [histone H3]-trimethyl-L-lysine³⁶ demethylase

1.14.11.70 7-deoxycylindrospermopsin hydroxylase

1.14.11.71 methylphosphonate hydroxylase

1.14.11.72 [2-(trimethylamino)ethyl]phosphonate dioxygenase

1.14.11.73 [protein]-arginine 3-hydroxylase

1.14.11.74 L-isoleucine 3¹-dioxygenase

1.14.11.75 3¹-hydroxy-L-isoleucine 4-dioxygenase

1.14.11.76 L-glutamate 3(R)-hydroxylase

1.14.11.77 alkyl sulfatase

1.14.11.78 (R)-3-[(carboxymethyl)amino]fatty acid dioxygenase/decarboxylase

1.14.11.79 protein-L-histidine (3S)-3-hydroxylase

1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor

1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor

1.14.16 With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor

1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor

1.14.18 With another compound as one donor, and incorporation of one atom of oxygen into the other donor

1.14.19 With oxidation of a pair of donors resulting in the reduction of O₂ to two molecules of water

1.14.20 With 2-oxoglutarate as one donor, and the other dehydrogenated

1.14.21 With NADH or NADPH as one donor, and the other dehydrogenated

1.14.99 Miscellaneous

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

3.1 Acting on ester bonds

3.2 Glycosylases

3.3 Acting on ether bonds

3.4 Acting on peptide bonds (peptidases)

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.6 Acting on acid anhydrides

3.7 Acting on carbon-carbon bonds

3.8 Acting on halide bonds

3.9 Acting on phosphorus-nitrogen bonds

3.10 Acting on sulfur-nitrogen bonds

3.10.1 Acting on sulfur-nitrogen bonds (only sub-subclass identified to date)

3.11 Acting on carbon-phosphorus bonds

3.12 Acting on sulfur-sulfur bonds

3.13 Acting on carbon-sulfur bonds

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Release 2023.1 (January 2023)