Catalytic Mechanism of Perosamine N-Acetyltransferase Revealed by High-Resolution X-ray Crystallographic Studies and Kinetic Analyses-Reference-Cited by-同舟云学术

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

Published:2012-04-10 Issue:16 Volume:51 Page:3433-3444
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Thoden James B.¹,Reinhardt Laurie A.¹,Cook Paul D.²,Menden Patrick³,Cleland W. W.¹,Holden Hazel M.¹

Affiliation:

1. Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, United States

2. Department of Chemistry and Biochemistry, University of Mount Union, Alliance, Ohio 44601, United States

3. McArdle Laboratory for Cancer Research, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin 53706, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300197h

Reference38 articles.

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

2. Escherichia coli O157:H7

3. Structure of the O-chain polysaccharide of the phenol-phase soluble lipopolysaccharide of Escherichia coli 0:157:H7

4. The Occurrence of α(1 → 2) LinkedN-Acetylperosamine-Homopolymer in Lipopolysaccharides of Non-O1Vibrio choleraePossessing an Antigenic Factor in Common with OlV. cholerae

5. Structures of two O-polysaccharides of the lipopolysaccharide of Citrobacter youngae PCM 1538 (serogroup O9)

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