Catalytic Mechanism of Perosamine N -Acetyltransferase Revealed by High-Resolution X-ray Crystallographic Studies and Kinetic Analyses - Wikidata - wikimedia - TriplyDB

Catalytic Mechanism of Perosamine N -Acetyltransferase Revealed by High-Resolution X-ray Crystallographic Studies and Kinetic Analyses

Catalytic Mechanism of Perosamine N -Acetyltransferase Revealed by High-Resolution X-ray Crystallographic Studies and Kinetic Analyses

http://www.wikidata.org/entity/Q27678180

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Biochemical Analysis and Structure Determination of Bacterial Acetyltransferases Responsible for the Biosynthesis of UDP-N,N'-Diacetylbacillosamine Structural and Biochemical Characterization of a Bifunctional Ketoisomerase/ N -Acetyltransferase from Shewanella denitrificans Structure of Soybean Serine Acetyltransferase and Formation of the Cysteine Regulatory Complex as a Molecular Chaperone Structural and Functional Investigation of FdhC from Acinetobacter nosocomialis: A Sugar N-Acyltransferase Belonging to the GNAT Superfamily Potential for reduction of streptogramin A resistance revealed by structural analysis of acetyltransferase VatA.The rare sugar N-acetylated viosamine is a major component of Mimivirus fibers.

P2860

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Catalytic Mechanism of Perosamine N -Acetyltransferase Revealed by High-Resolution X-ray Crystallographic Studies and Kinetic Analyses

http://www.wikidata.org/entity/Q27678180

description

2012 nî lūn-bûn

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2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2012 թվականի ապրիլին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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Catalytic Mechanism of Perosam ...... c Studies and Kinetic Analyses

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Catalytic Mechanism of Perosam ...... c Studies and Kinetic Analyses

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Catalytic Mechanism of Perosam ...... c Studies and Kinetic Analyses

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Catalytic Mechanism of Perosam ...... c Studies and Kinetic Analyses

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Laurie A Reinhardt

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Patrick Menden

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Paul D Cook

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W W Cleland

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P2860

Laboratory investigation of hemorrhagic colitis outbreaks associated with a rare Escherichia coli serotype

Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily

Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6 dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose

Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture

Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution

Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites

Structure of the MUR1 GDP-mannose 4,6-dehydratase from Arabidopsis thaliana: implications for ligand binding and specificity

Crystal structure of a tetrameric GDP-D-mannose 4,6-dehydratase from a bacterial GDP-D-rhamnose biosynthetic pathway

Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni

GDP-perosamine synthase: structural analysis and production of a novel trideoxysugar

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3433-44

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scholarly article

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10.1021/BI300197H

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16

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51

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2012-04-24T00:00:00Z

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221972203

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22443398

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4249942

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