UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism. (Q34393182)

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8 January 2020

title

UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism (English)

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8 January 2020

Heather A Gennadios

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8 January 2020

Douglas A Whittington

series ordinal

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8 January 2020

Kristin M Rusche

series ordinal

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8 January 2020

David W Christianson

series ordinal

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8 January 2020

language of work or name

English

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publication date

10 February 2005

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Journal of Biological Chemistry

8 January 2020

published in

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8 January 2020

volume

280

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8 January 2020

issue

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8 January 2020

page(s)

16969-16978

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Lipopolysaccharide endotoxins

8 January 2020

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UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme

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The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase

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Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase in Escherichia coli. The second enzymatic step of lipid a biosynthesis.

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20 May 2022

https://opencitations.net/index/coci/api/v1/citations/10.1107/S0907444998003254

Identifiers

DOI

10.1074/JBC.M413560200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15705580%20AND%20SRC:MED&resulttype=core&format=json

8 January 2020

1 reference

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