3.5.1.25: N-acetylglucosamine-6-phosphate deacetylase
This is an abbreviated version!
For detailed information about N-acetylglucosamine-6-phosphate deacetylase, go to the full flat file.
Word Map on EC 3.5.1.25
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3.5.1.25
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deaminase
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chitin
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fructose-6-phosphate
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glcn-6-phosphate
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non-o1
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drug development
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diagnostics
- 3.5.1.25
- deaminase
- chitin
- fructose-6-phosphate
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glcn-6-phosphate
- non-o1
- drug development
- diagnostics
Reaction
Synonyms
2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase, acetylaminodeoxyglucosephosphate acetylhydrolase, acetylglucosamine phosphate deacetylase, CaNAG2/Dac1, deacetylase, acetylglucosaminephosphate, EC 3.5.1.80, GlcNAc 6-P deacetylase, GlcNAc-6-phosphate deacetylase, GlnNAc6P deacetylase, Lmo0956, Lmo0956 protein, Lmo2108, Lmo2108 protein, MMNagA, MSNagA, N-acetyl-D-glucosamine-6-phosphate deacetylase, N-acetylglucosamine 6-phosphate deacetylase, N-acetylglucosamine-6-P deacetylase, N-acetylglucosamine-6-phosphate de-N-acetylase, N-acetylglucosamine-6-phosphate deacetylase, NAG2, NagA, NAGPase
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Metals Ions
Metals Ions on EC 3.5.1.25 - N-acetylglucosamine-6-phosphate deacetylase
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1,10-phenanthroline
results in unfolding and loss of catalytic activity at 10 mM
Co2+
EDTA
results in unfolding and loss of catalytic activity at 10 mM
Fe2+
the protein contains predominantly more zinc in a 12:1 zinc:iron ratio
Zn
Zn2+
additional information
Co2+
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restores activity after treatment with EDTA and stimulates above the control value
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1 equivalent of zinc bound at the Mbeta site, the enzyme contains a binuclear metal center at the active site
Zn2+
zinc metalloenzyme, Zn2+ is bound to the enzyme, 1.4 Zn2+ per polypeptide chain, the metal binding site also binds a phosphate ion
Zn2+
the protein contains predominantly more zinc in a 12:1 zinc:iron ratio
enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations
additional information
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enzyme inactivation by metal-sequestering agents and subsequent reactivation by the addition of several divalent cations
additional information
after treatment with 10 mM 1,10-phenanthroline or 10 mM EDTA, resulting in unfolding and loss of catalytic activity, the activity cannot be restored by addition of ZnCl2 to the metal-free enzyme, indicating that the metal ions are tightly coordinated in the active site and have an essential structural role in mycobacterial NagA enzymes
additional information
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after treatment with 10 mM 1,10-phenanthroline or 10 mM EDTA, resulting in unfolding and loss of catalytic activity, the activity cannot be restored by addition of ZnCl2 to the metal-free enzyme, indicating that the metal ions are tightly coordinated in the active site and have an essential structural role in mycobacterial NagA enzymes
additional information
structure of the metal-binding site in MSNagA, overview
additional information
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structure of the metal-binding site in MSNagA, overview