Literature summary for 3.6.1.54 extracted from

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 (2019), J. Biol. Chem., 294, 7982-7989 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in E. coli strain BL21(DE3) and Bordetella pertussis strain B213	Neisseria meningitidis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O	Neisseria meningitidis	-	2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP	-	?

Organism

Organism	UniProt	Comment	Textmining
Neisseria meningitidis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O	-	Neisseria meningitidis	2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP	-	?

Synonyms

Synonyms	Comment	Organism
LpxH	-	Neisseria meningitidis
UDP-diacylglucosamine pyrophosphohydrolase	-	Neisseria meningitidis

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Release 2023.1 (January 2023)