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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

Reaction

a phosphoglycerolipid
+
an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
=
a 1-lyso-phosphoglycerolipid
 +
a [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine

Synonyms

ALP N-acyltransferase, apolipoprotein N-acyl transferase, BCG_2070c, lnt, LntMs, NMB0713, Ppm1Tb

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.269 apolipoprotein N-acyltransferase

Engineering

Engineering on EC 2.3.1.269 - apolipoprotein N-acyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C23A/C62A
site-directed mutagenesis
C387A
C387S
E267A
-
the mutation affects the N-acylation activity of the enzyme
E343A
-
the mutation affects the N-acylation activity of the enzyme
E389A
F358V
-
inactive
F416A
site-directed mutagenesis, a Nit domain residue, the mutant cannot complement enzyme-deficient mutant DELTAlnt cells
G145A
site-directed mutagenesis, G145 is located in a highly conserved region C-terminal to TM5, the mutant cannot complement enzyme-deficient mutant DELTAlnt cells
G342A
site-directed mutagenesis, a Nit domain residue, the mutant cannot complement enzyme-deficient mutant DELTAlnt cells
K335A
L392H
-
the mutation results in functional enzyme
N244I
-
the mutation results in functional enzyme
P147L
-
inactive
P353S
-
the mutation results in functional enzyme
R352A
site-directed mutagenesis, a Nit domain residue, the mutant cannot complement enzyme-deficient mutant DELTAlnt cells
T481R
-
inactive
V339A
site-directed mutagenesis, a Nit domain residue, the mutant cannot complement enzyme-deficient mutant DELTAlnt cells
W148A
-
the mutation does not affect the N-acylation activity of the enzyme
W237A
Y388A
Y406C
-
the mutation results in functional enzyme
additional information