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
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2.3.1.269
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apolipoproteins
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n-acylation
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triacylated
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membrane-embedded
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prolipoprotein
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diacylglyceryl
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phosphatidylglycerol
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acyl-enzyme
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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
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Crystallization
Crystallization on EC 2.3.1.269 - apolipoprotein N-acyltransferase
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purified recombinant C-terminally His8-tagged enzyme, 15 mg/ml protein in 25 mM Tris, pH 8.0, 100 mM NaCl, 5% glycerol, 0.5 mM TCEP, and 0.02% DDM, is mixed with 25% PEG 2000 MME, 100 mM Na cacodylate, pH 6.4, and 40 mM MgCl2 with a drop ratio of 1:1.75 protein:precipitate, 18°C, 2 weeks. For the N-terminally cleaved detagged enzyme, 36% PEG 200, 400 mM ammonium phosphate dibasic, and 100 mM HEPES, pH 7.2, at 10°C for 3 weeks, are used. X-ray diffraction structure determination and analysis at 3.1-3.5 A resolution, modeling
purified recombinant wild-type and selenomethionine-labeled enzymes, hanging drop vapor diffusion method, 12 mg/ml protein from 50 mM Tris-HCl, pH 7.5, and 26% v/v PEG 550 MME supplemented with two detergents, n-heptyl-beta-D-thioglucopyranoside and CHAPSO, 16°C, X-ray diffraction structure determination and analysis at 2.59 and 3.60 A resolution, respectively
using 8% (w/v) 2-methyl-2,4-pentanediol, 0.1 M MES pH 6.0 and 0.4 M ammonium citrate
using 30% (w/v) PEG-500 DME, 0.1 M sodium citrate pH 5.0 and 0.1 M sodium acetate