MetaCyc Enzyme: N-acetylglucosamine-6-phosphate deacetylase

Gene: nagA Accession Number: G-14699 (MetaCyc)

Synonyms: VC0994

Species: Vibrio cholerae non-O1

Subunit composition of N-acetylglucosamine-6-phosphate deacetylase = [NagA]4
         N-acetylglucosamine-6-phosphate deacetylase subunit = NagA

The native apparent molecular mass was determined by gel filtration chromatography [Yamano96].

This enzyme functions in the chitin catabolic cascade in Vibrio cholerae non-O1. It was purified from cell extracts and characterized [Yamano96] and the gene encoding it was cloned [Yamano97].
The subunit apparent molecular mass was determined by SDS-PAGE [Yamano96].

Locations: cytosol

Map Position: [1,059,719 <- 1,060,855]

Molecular Weight of Polypeptide: 40.956 kD (from nucleotide sequence), 45.0 kD (experimental) [Yamano96 ]

Molecular Weight of Multimer: 190.0 kD (experimental) [Yamano96]

Unification Links: Entrez-gene:2614247 , Protein Model Portal:O32445 , SMR:O32445 , String:243277.VC0994 , UniProt:O32445

Relationship Links: InterPro:IN-FAMILY:IPR003764 , InterPro:IN-FAMILY:IPR006680 , InterPro:IN-FAMILY:IPR011059 , PDB:Structure:3EGJ , PDB:Structure:3IV8 , Pfam:IN-FAMILY:PF01979

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Cellular Component: GO:0005829 - cytosol Inferred from experiment [Yamano96]

Created 30-Sep-2011 by Fulcher CA , SRI International

Enzymatic reaction of: N-acetylglucosamine-6-phosphate deacetylase

EC Number:

N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Alternative Substrates for N-acetyl-D-glucosamine 6-phosphate: N-acetyl-D-glucosamine 6-sulfate [Yamano96 ] , N-acetyl-D-glucosamine [Yamano96 ]

In Pathways: chitin derivatives degradation

Enzyme activity was assayed by measuring the amount of hexosamine produced. The temperature optimum was determined in phosphate buffer at pH 7.8. Co2+ at 4 mM activated the enzyme 200%. The enzyme also utilized N-acetyl-D-glucosamine (GlnNAc) as substrate. It did not utilize chitooligosaccharides ((GlcNAc)2-6) or N-acetyl-β-D-galactosamine as substrate [Yamano96].

Activators (Unknown Mechanism): Co2+ [Yamano96]

Inhibitors (Unknown Mechanism): N-ethylmaleimide [Yamano96] , p-chloromercuribenzoate [Yamano96] , Cu2+ [Yamano96] , EDTA [Yamano96]

Kinetic Parameters:

Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
N-acetyl-D-glucosamine 6-phosphate

T(opt): 37 °C [Yamano96]

pH(opt): 7.8-8.5 [Yamano96]


Yamano96: Yamano N, Matsushita Y, Kamada Y, Fujishima S, Arita M (1996). "Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from Vibrio cholerae non-O1." Biosci Biotechnol Biochem 60(8);1320-3. PMID: 8987551

Yamano97: Yamano N, Oura N, Wang J, Fujishima S (1997). "Cloning and sequencing of the genes for N-acetylglucosamine use that construct divergent operons (nagE-nagAC) from Vibrio cholerae non-O1." Biosci Biotechnol Biochem 61(8);1349-53. PMID: 9301118

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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