2.3.1.269: apolipoprotein N-acyltransferase
This is an abbreviated version!
For detailed information about apolipoprotein N-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.269
-
2.3.1.269
-
apolipoproteins
-
n-acylation
-
triacylated
-
membrane-embedded
-
prolipoprotein
-
diacylglyceryl
-
phosphatidylglycerol
-
acyl-enzyme
-
braun
- 2.3.1.269
-
apolipoproteins
-
n-acylation
-
triacylated
-
membrane-embedded
- prolipoprotein
-
diacylglyceryl
- phosphatidylglycerol
- acyl-enzyme
-
braun
Reaction
Synonyms
ALP N-acyltransferase, apolipoprotein N-acyl transferase, BCG_2070c, lnt, LntMs, NMB0713, Ppm1Tb
ECTree
Advanced search results
Subunits
Subunits on EC 2.3.1.269 - apolipoprotein N-acyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
additional information
the enzyme contains an exo-membrane nitrilase domain fused to a transmembrane (TM) domain. The TM domain of Lnt contains eight TM helices which form a membrane-embedded cavity with a lateral opening and a periplasmic exit. The nitrilase domain is located on the periplasmic side of the membrane, with its catalytic cavity connected to the periplasmic exit of the TM domain. An amphipathic lid loop from the nitrilase domain interacts with the periplasmic lipid leaflet, forming an interfacial entrance from the lipid bilayer to the catalytic centre for both the lipid donor and acceptor substrates. Crystal structure analysis, overview
additional information
-
the enzyme contains an exo-membrane nitrilase domain fused to a transmembrane (TM) domain. The TM domain of Lnt contains eight TM helices which form a membrane-embedded cavity with a lateral opening and a periplasmic exit. The nitrilase domain is located on the periplasmic side of the membrane, with its catalytic cavity connected to the periplasmic exit of the TM domain. An amphipathic lid loop from the nitrilase domain interacts with the periplasmic lipid leaflet, forming an interfacial entrance from the lipid bilayer to the catalytic centre for both the lipid donor and acceptor substrates. Crystal structure analysis, overview