The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily
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The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuationInsight into the induction mechanism of the GntR/HutC bacterial transcription regulator YvoACrystal structure of a metal-dependent phosphoesterase (YP_910028.1) from Bifidobacterium adolescentis: Computational prediction and experimental validation of phosphoesterase activityThe mononuclear metal center of type-I dihydroorotase from aquifex aeolicusProteomics analysis of Lactobacillus casei Zhang, a new probiotic bacterium isolated from traditional home-made koumiss in Inner Mongolia of China.N-acetylglucosamine 6-phosphate deacetylase (nagA) is required for N-acetyl glucosamine assimilation in Gluconacetobacter xylinus.Uptake and metabolism of N-acetylglucosamine and glucosamine by Streptococcus mutansThe use of amino sugars by Bacillus subtilis: presence of a unique operon for the catabolism of glucosamine.Structure-guided engineering of molinate hydrolase for the degradation of thiocarbamate pesticidesN-acetylglucosamine-6-phosphate deacetylase (NagA) of Listeria monocytogenes EGD, an essential enzyme for the metabolism and recycling of amino sugars.Intensity statistics in the presence of translational noncrystallographic symmetry.Microbial production of glucosamine and N-acetylglucosamine: advances and perspectives.Structural and functional characterization of the Clostridium perfringens N-acetylmannosamine-6-phosphate 2-epimerase essential for the sialic acid salvage pathwayCloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of YvoA from Bacillus subtilis.Regulon of the N-acetylglucosamine utilization regulator NagR in Bacillus subtilis.N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ionStructural insight into operator dre-sites recognition and effector binding in the GntR/HutC transcription regulator NagR.Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamine.Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: missing link of the NagB superfamily?Inverse nickel-responsive regulation of two urease enzymes in the gastric pathogen Helicobacter mustelae.Activation of Latent Dihydroorotase from Aquifex aeolicus by Pressure.Structural and functional determination of homologs of the Mycobacterium tuberculosis N-acetylglucosamine-6-phosphate deacetylase (NagA).A GFP-strategy for efficient recombinant protein overexpression and purification inA metabolic checkpoint protein GlmR is important for diverting carbon into peptidoglycan biosynthesis in Bacillus subtilis
P2860
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P2860
The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The three-dimensional structur ...... mber of the urease superfamily
@ast
The three-dimensional structur ...... mber of the urease superfamily
@en
The three-dimensional structur ...... mber of the urease superfamily
@nl
type
label
The three-dimensional structur ...... mber of the urease superfamily
@ast
The three-dimensional structur ...... mber of the urease superfamily
@en
The three-dimensional structur ...... mber of the urease superfamily
@nl
prefLabel
The three-dimensional structur ...... mber of the urease superfamily
@ast
The three-dimensional structur ...... mber of the urease superfamily
@en
The three-dimensional structur ...... mber of the urease superfamily
@nl
P2860
P50
P356
P1476
The three-dimensional structur ...... mber of the urease superfamily
@en
P2093
David Yates
James A Brannigan
P2860
P304
P356
10.1074/JBC.M310165200
P407
P577
2004-01-23T00:00:00Z