N-acetylglucosamine-6-phosphate deacetylase [Pediococcus damnosus]

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Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase. [Biochemistry. 2007]
Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase.
Hall RS, Brown S, Fedorov AA, Fedorov EV, Xu C, Babbitt PC, Almo SC, Raushel FM. Biochemistry. 2007 Jul 10; 46(27):7953-62. Epub 2007 Jun 13.
N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion. [Biochemistry. 2007]
N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion.
Hall RS, Xiang DF, Xu C, Raushel FM. Biochemistry. 2007 Jul 10; 46(27):7942-52. Epub 2007 Jun 13.
An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. [Proteins. 1997]
An evolutionary treasure: unification of a broad set of amidohydrolases related to urease.
Holm L, Sander C. Proteins. 1997 May; 28(1):72-82.

RefSeq protein
See the reference protein sequence for N-acetylglucosamine-6-phosphate deacetylase (WP_056986112.1).

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N-acetylglucosamine-6-phosphate deacetylase [Pediococcus damnosus]
N-acetylglucosamine-6-phosphate deacetylase [Pediococcus damnosus]
gi|1015509205|gnl|Pda21533|ADU70_20 |AMV63544.1|

Protein
PTS system, IIC component, putative [Streptococcus sanguinis SK36]
PTS system, IIC component, putative [Streptococcus sanguinis SK36]
gi|125496855|gnl|vcu|SSA_0055|gb|AB 1.1|

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