Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.6.1.54: UDP-2,3-diacylglucosamine diphosphatase

This is an abbreviated version!
For detailed information about UDP-2,3-diacylglucosamine diphosphatase, go to the full flat file.

Word Map on EC 3.6.1.54

Reaction

a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
+
H2O
=
a lipid X
 +
UMP

Synonyms

LpxH, LpxI, UDP-2, 3-diacylglucosamine hydrolase, UDP-2,3-bis[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine 2,3-bis[(3R)-3-hydroxymyristoyl]-beta-D-glucosaminyl 1-phosphate phosphohydrolase, UDP-2,3-diacylglucosamine hydrolase, UDP-2,3-diacylglucosamine pyrophosphatase, UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate phosphohydrolase, UDP-diacylglucosamine pyrophosphatase, UDP-diacylglucosamine pyrophosphohydrase, UDP-diacylglucosamine pyrophosphohydrolase, YbbF

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.54 UDP-2,3-diacylglucosamine diphosphatase

Reference

topprint

Reference on EC 3.6.1.54 - UDP-2,3-diacylglucosamine diphosphatase

Please use the Reference Search for a specific query.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Babinski, K.J.; Ribeiro, A.A.; Raetz, C.R.
The Escherichia coli gene encoding the UDP-2,3-diacylglucosamine pyrophosphatase of lipid A biosynthesis
J. Biol. Chem.
277
25937-2546
2002
Escherichia coli (P43341), Escherichia coli
Manually annotated by BRENDA team
Babinski, K.J.; Kanjilal, S.J.; Raetz, C.R.
Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene
J. Biol. Chem.
277
25947-25956
2002
Escherichia coli, Pseudomonas aeruginosa
Manually annotated by BRENDA team
Metzger, L.E.; Raetz, C.R.
An alternative route for UDP-diacylglucosamine hydrolysis in bacterial lipid A biosynthesis
Biochemistry
49
6715-6726
2010
Caulobacter vibrioides (A0A0H3C8Q1), Caulobacter vibrioides, Caulobacter vibrioides CB15 (A0A0H3C8Q1)
Manually annotated by BRENDA team
Dimou, M.; Venieraki, A.; Liakopoulos, G.; Kouri, E.D.; Tampakaki, A.; Katinakis, P.
Gene expression and biochemical characterization of Azotobacter vinelandii cyclophilins and protein interaction studies of the cytoplasmic isoform with dnaK and lpxH
J. Mol. Microbiol. Biotechnol.
20
176-190
2011
Azotobacter vinelandii (C1DHE3)
Manually annotated by BRENDA team
Young, H.E.; Donohue, M.P.; Smirnova, T.I.; Smirnov, A.I.; Zhou, P.
The UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis utilizes Mn2+ cluster for catalysis
J. Biol. Chem.
288
26987-27001
2013
Haemophilus influenzae (P44046), Haemophilus influenzae, Haemophilus influenzae DSM 11121 (P44046)
Manually annotated by BRENDA team
Lee, M.; Zhao, J.; Kwak, S.H.; Cho, J.; Lee, M.; Gillespie, R.A.; Kwon, D.Y.; Lee, H.; Park, H.J.; Wu, Q.; Zhou, P.; Hong, J.
Structure-activity relationship of sulfonyl piperazine LpxH inhibitors analyzed by an LpxE-coupled malachite green assay
ACS Infect. Dis.
5
641-651
2019
Escherichia coli
Manually annotated by BRENDA team
Bohl, T.; Ieong, P.; Lee, J.; Lee, T.; Kankanala, J.; Shi, K.; Demir, A.; Kurahashi, K.; Amaro, R.; Wang, Z.; Aihara, H.
The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release
J. Biol. Chem.
293
7969-7981
2018
Escherichia coli (P43341)
Manually annotated by BRENDA team
Arenas, J.; Pupo, E.; De Jonge, E.; Perez-Ortega, J.; Schaarschmidt, J.; Van Der Ley, P.; Tommassen, J.
Substrate specificity of the pyrophosphohydrolase LpxH determines the asymmetry of Bordetella pertussis lipid A
J. Biol. Chem.
294
7982-7989
2019
Neisseria meningitidis
Manually annotated by BRENDA team
Cho, J.; Lee, C.; Zhao, J.; Young, H.; Zhou, P.
Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis
Nat. Microbiol.
1
16154
2016
Haemophilus influenzae
Manually annotated by BRENDA team
Richie, D.; Takeoka, K.; Bojkovic, J.; Metzger, L.; Rath, C.; Sawyer, W.; Wei, J.; Dean, C.
Toxic accumulation of lps pathway intermediates underlies the requirement of LpxH for growth of acinetobacter Baumannii ATCC 19606
PLoS ONE
11
e0160918
2016
Acinetobacter baumannii, Acinetobacter baumannii (D0C652), Acinetobacter baumannii ATCC 19606, Acinetobacter baumannii ATCC 19606 (D0C652)
Manually annotated by BRENDA team
Okada, C.; Wakabayashi, H.; Kobayashi, M.; Shinoda, A.; Tanaka, I.; Yao, M.
Crystal structures of the UDP-diacylglucosamine pyrophosphohydrase LpxH from Pseudomonas aeruginosa
Sci. Rep.
6
32822
2016
Pseudomonas aeruginosa (Q9I2V0), Pseudomonas aeruginosa
Manually annotated by BRENDA team