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Literature summary extracted from

  • Babinski, K.J.; Ribeiro, A.A.; Raetz, C.R.
    The Escherichia coli gene encoding the UDP-2,3-diacylglucosamine pyrophosphatase of lipid A biosynthesis (2002), J. Biol. Chem., 277, 25937-2546.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.54 lpxH overexpression is toxic to cells Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.54 Triton X-100 0.01% Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.54 0.0617
-
 UDP-N2,O3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine pH 8.0, 30°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.54 Mn2+ stimulates Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.54 26893
-
 x * 26893, calculated from sequence Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.54 UDP-2,3-bis((3R)-3-hydroxymyristoyl)alpha-D-glucosamine + H2O Escherichia coli step of lipid A biosynthesis 2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.54 Escherichia coli P43341
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.54 partial Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.6.1.54 63.2
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.54 additional information no activity with UDP-N-acetylglucosamine and UDP-3-O-(R)-(3-hydroxymyristoyl)glucosamine, LpxH does not cleave CDP-diacylglycerol Escherichia coli ?
-
 ?
3.6.1.54 UDP-2,3-bis((3R)-3-hydroxymyristoyl)alpha-D-glucosamine + H2O step of lipid A biosynthesis Escherichia coli 2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP
-
 ?
3.6.1.54 UDP-N2,O3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + H2O strict requirement for a diacylated substrate. LpxH hydrolysis incorporates H218O into UMP by catalyzing the attack of water on the alpha-phosphorus atom of UDP-2,3-diacylglucosamine Escherichia coli N2,O3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine 1-phosphate + UMP
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.1.54 ? x * 26893, calculated from sequence Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.6.1.54 LpxH
-
 Escherichia coli
3.6.1.54 UDP-2,3-diacylglucosamine hydrolase
-
 Escherichia coli
3.6.1.54 UDP-2,3-diacylglucosamine pyrophosphatase
-
 Escherichia coli
3.6.1.54 YbbF
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.54 30
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.54 8
-
-
 Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.6.1.54 6.5 9.5 pH 6.5: about 50% of maximal activity, pH 9.5: about 50% of maximal activity Escherichia coli