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Literature summary for 2.7.8.43 extracted from

  • Stojanoski, V.; Sankaran, B.; Prasad, B.V.V.; Poirel, L.; Nordmann, P.; Palzkill, T.
    Structure of the catalytic domain of the colistin resistance enzyme MCR-1 (2016), BMC Biol., 14, 81 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the catalytic domain ofMCR1 at 1.32 A resolution. The putative nucleophile for catalysis, threonine 285, is phosphorylated in MCR1 and a zinc is present at a conserved site in addition to three zincs more peripherally located in the active site. Binding sites for the lipid A and phosphatidylethanolamine substrates are not apparent in the MCR1 structure Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc ion is present at a conserved site in addition to three zincs more peripherally located in the active site Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli A0A0R6L508
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diacylphosphatidylethanolamine + lipid A
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 Escherichia coli diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
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 ?
diacylphosphatidylethanolamine + lipid A
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 Escherichia coli diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
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 ?
additional information transfer may occur both to the 4'- and 1-phospho groups of lipid A Escherichia coli ?
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Synonyms

Synonyms Comment Organism
MCR1
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 Escherichia coli