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Information on EC 2.3.1.269 - apolipoprotein N-acyltransferase
for references in articles please use BRENDA:EC2.3.1.269
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.269 apolipoprotein N-acyltransferase
IUBMB Comments
This bacterial enzyme transfers a fatty acid from a membrane phospholipid to form an amide linkage with the N-terminal cysteine residue of apolipoproteins, generating a triacylated molecule.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 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
- prolipoprotein
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diacylglyceryl
- phosphatidylglycerol
- acyl-enzyme
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braun
Reaction Schemes
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an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
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a [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
Synonyms
apolipoprotein n-acyltransferase, alp n-acyltransferase, apolipoprotein n-acyl transferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALP N-acyltransferase
apolipoprotein N-acyl transferase
lnt
LntMs
NMB0713
Ppm1Tb
lnt
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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PATHWAY SOURCE
PATHWAYS
MetaCyc
lipoprotein posttranslational modification
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SYSTEMATIC NAME
IUBMB Comments
phosphoglyceride:[apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine N-acyltransferase
This bacterial enzyme transfers a fatty acid from a membrane phospholipid to form an amide linkage with the N-terminal cysteine residue of apolipoproteins, generating a triacylated molecule.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-alkyne-2-acyl-phosphatidylethanolamine + [FSL-1 apolipopeptide]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-2-acyl-phosphatidylethanolamine + [FSL-1 lipopeptide]-N-alkyne-S-1,2-diacyl-sn-glyceryl-L-cysteine
Substrates: -
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1-palmitoyl alkyne-2-oleoyl-sn-glycero-3-phosphatidylethanolamine + [FSL-1 apolipopeptide]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-2-oleoyl-sn-glycero-3-phosphatidylethanolamine + [FSL-1 lipopeptide]-N-palmitoyl alkyne-S-1,2-diacyl-sn-glyceryl-L-cysteine
Substrates: -
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1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine + [apolipoprotein Pal]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-2-oleoyl-sn-glycero-3-phosphoethanolamine + [lipoprotein Pal]-N-palmitoyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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1-palmitoyl-2-vaccenoyl-sn-glycero-3-phosphoethanolamine + an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
? + a [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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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
a phosphoglycerolipid + [apolipoprotein LolC]-S-1,2-diacyl-sn-glyceryl-L-cysteine
a 1-lyso-phosphoglycerolipid + [lipoprotein LolC]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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a phosphoglycerolipid + [apolipoprotein LolE]-S-1,2-diacyl-sn-glyceryl-L-cysteine
a 1-lyso-phosphoglycerolipid + [lipoprotein LolE]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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a phosphoglycerolipid + [apolipoprotein Lppx]-S-1,2-diacyl-sn-glyceryl-L-cysteine
a 1-lyso-phosphoglycerolipid + [lipoprotein Lppx]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
a phosphoglycerolipid + [apolipoprotein Lpp]-S-1,2-diacyl-sn-glyceryl-L-cysteine
a 1-lyso-phosphoglycerolipid + [lipoprotein Lpp]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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a phosphoglycerolipid + [apolipoprotein MalE]-S-1,2-diacyl-sn-glyceryl-L-cysteine
a 1-lyso-phosphoglycerolipid + [lipoprotein MalE]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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a phosphoglycerolipid + [apolipoprotein NlpD]-S-1,2-diacyl-sn-glyceryl-L-cysteine
a 1-lyso-phosphoglycerolipid + [lipoprotein NlpD]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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a phosphoglycerolipid + [apolipoprotein OmpA]-S-1,2-diacyl-sn-glyceryl-L-cysteine
a 1-lyso-phosphoglycerolipid + [lipoprotein OmpA]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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a phosphoglycerolipid + [apolipoprotein Pal]-S-1,2-diacyl-sn-glyceryl-L-cysteine
a 1-lyso-phosphoglycerolipid + [lipoprotein Pal]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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cardiolipin + [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-cardiolipin + [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
Substrates: -
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phosphatidylethanolamine + [apolipoprotein FSL-1]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-phosphatidylethanolamine + [lipoprotein FSL-1]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
phosphatidylethanolamine + [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-phosphatidylethanolamine + [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
phosphatidylethanolamine+ [apolipeptide FSL-1]-S-1,2-diacyl-sn-glyceryl-L-cysteine
?
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Substrates: -
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phosphatidylglycerol + [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-phosphatidylglycerol + [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
Substrates: -
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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
Substrates: -
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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
Acinetobacter baumannii AB5075-UW
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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
Substrates: -
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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
Substrates: -
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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
Substrates: -
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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
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Substrates: -
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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
Substrates: -
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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
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Substrates: -
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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
Substrates: -
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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
Substrates: Lnt can use all available phospholipids such as phosphatidylglycerol (PG), phosphatidylethanolamine (PE), and cardiolipin (CL) as acyl donors. The preferred substrate is PE
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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
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Substrates: -
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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
Substrates: -
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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
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Substrates: -
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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
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Substrates: -
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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
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Substrates: -
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a phosphoglycerolipid + [apolipoprotein Lppx]-S-1,2-diacyl-sn-glyceryl-L-cysteine
a 1-lyso-phosphoglycerolipid + [lipoprotein Lppx]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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a phosphoglycerolipid + [apolipoprotein Lppx]-S-1,2-diacyl-sn-glyceryl-L-cysteine
a 1-lyso-phosphoglycerolipid + [lipoprotein Lppx]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
Mycobacterium tuberculosis Rv2051c
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a phosphoglycerolipid + [factor H binding protein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
?
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a phosphoglycerolipid + [factor H binding protein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
?
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phosphatidylethanolamine + [apolipoprotein FSL-1]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-phosphatidylethanolamine + [lipoprotein FSL-1]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
Substrates: -
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phosphatidylethanolamine + [apolipoprotein FSL-1]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-phosphatidylethanolamine + [lipoprotein FSL-1]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
Substrates: -
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phosphatidylethanolamine + [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-phosphatidylethanolamine + [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
Substrates: -
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phosphatidylethanolamine + [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-phosphatidylethanolamine + [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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additional information
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Substrates: in vivo activity assay is performed using Para-lntEc Escherichia coli strain PAP8504
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additional information
?
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Substrates: in vivo activity assay is performed using Para-lntEc Escherichia coli strain PAP8504
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additional information
?
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Substrates: enzyme Lnt uses apolipoprotein (S-diacylglyceryl protein) as protein substrate in the reaction. Lnt catalyzes a two-step reaction via a ping-pong mechanism, whereby in the first step, a stable thioester acyl-enzyme intermediate is formed upon hydrolysis of phospholipid. 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylethanolamine (POPE) is the preferred substrate for Lnt. When the lysophospholipid by-product is released, N-acyl transfer onto apolipoprotein occurs in the second step of the reaction. The enzyme is unable to catalyze the N-acyl transferase reaction in the presence of POPE and no effect is observed with PE-biotin. Various FSL-1 peptide substrates are N-acylated by Lnt in vitro. N-acyltransferase activity of Lnt is monitored as a shift in migration of the lipopeptide FSL-1 conjugated either with biotin or fluorescein, and detection of Lnt activity by fluorescence spectroscopy, method evaluation and optimization, overview
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additional information
?
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Substrates: the short loop containing W237 might help to locally stabilize the N-terminal tail from the opposite side to allow transfer of the palmitoylate from the C387 to the apolipoprotein to produce the final mature lipoprotein
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additional information
?
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Substrates: the short loop containing W237 might help to locally stabilize the N-terminal tail from the opposite side to allow transfer of the palmitoylate from the C387 to the apolipoprotein to produce the final mature lipoprotein
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additional information
?
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Substrates: the substrate for N-acylation is a C16 fatty acid, whereas the two fatty acids of the diacylglycerol residue are identified as C16 and C19:0 fatty acid, the latter most likely tuberculostearic acid
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additional information
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Mycobacterium tuberculosis Rv2051c
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Substrates: the substrate for N-acylation is a C16 fatty acid, whereas the two fatty acids of the diacylglycerol residue are identified as C16 and C19:0 fatty acid, the latter most likely tuberculostearic acid
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-vaccenoyl-sn-glycero-3-phosphoethanolamine + an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
? + a [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
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Substrates: -
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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
phosphatidylethanolamine + [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine
1-lyso-phosphatidylethanolamine + [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
Substrates: -
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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
Substrates: -
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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
Acinetobacter baumannii AB5075-UW
Substrates: -
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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
Substrates: -
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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
Substrates: -
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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
Substrates: -
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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
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Substrates: -
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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
Substrates: -
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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
-
Substrates: -
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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
Substrates: -
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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
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Substrates: -
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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
Substrates: -
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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
-
Substrates: -
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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
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Substrates: -
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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
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Substrates: -
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additional information
?
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Substrates: in vivo activity assay is performed using Para-lntEc Escherichia coli strain PAP8504
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additional information
?
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Substrates: in vivo activity assay is performed using Para-lntEc Escherichia coli strain PAP8504
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
-
2 mM Cu2+ does not affect enzyme activity in the wild type strain. Cu2+ (0.1-0.25 mM) causes an accumulation of apolipoprotein in the SE5312 mutant at 30°C
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
apolipoprotein N-acyltransferase (Lnt) belongs to the nitrilase superfamily. Nitrilases are multimeric proteins that contain a common Glu-Lys-Cys catalytic triad that hydrolyse carbon-nitrogen bonds
evolution
apolipoprotein N-acyltransferase Lnt is Lnt is a reverse amidase and belongs to the nitrilase superfamily. Nitrilases generally require the Glu/Lys/Cys catalytic triad's conformation, also found in Lnt, and have a conserved alphabetabetaalpha sandwich fold. First, the intermediate is formed by the nucleophilic attack on the sn-1-glycerophospholipid's carbonyl (in phosphatidylethanolamine (PE), preferentially). Second, the intermediate (acyl-Lnt) undergoes a nucleophilic attack by the alpha-amino group of the protein substrate generating the triacylated lipoprotein
evolution
the enzyme is a member of the nitrilase superfamily which catalyses hydrolysis or condensation of carbon-nitrogen amine and nitrile bonds
malfunction
-
depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli
malfunction
Acinetobacter species can tolerate a complete loss-of-function mutation in gene lnt. Absence of a fully functional Lnt impairs modification of lipoproteins, increases outer membrane permeability and susceptibility to antibiotics, and alters normal cellular morphology. In addition, loss of lnt triggers a global transcriptional response to this added cellular stress. Without Lnt, the bacterial cell envelope becomes more permeable and modification of outer membrane lipoproteins is impaired. Cells of the lnt mutant have structural defects. The genome expression profile of Acinetobacter baylyi changes in response to lnt mutation. Phenotypes, overview
malfunction
Acinetobacter species can tolerate a complete loss-of-function mutation in gene lnt. Absence of a fully functional Lnt impairs modification of lipoproteins, increases outer membrane permeability and susceptibility to antibiotics, and alters normal cellular morphology. In addition, loss of lnt triggers a global transcriptional response to this added cellular stress. Without Lnt, the bacterial cell envelope becomes more permeable and modification of outer membrane lipoproteins is impaired. Phenotypes, overview
malfunction
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Acinetobacter species can tolerate a complete loss-of-function mutation in gene lnt. Absence of a fully functional Lnt impairs modification of lipoproteins, increases outer membrane permeability and susceptibility to antibiotics, and alters normal cellular morphology. In addition, loss of lnt triggers a global transcriptional response to this added cellular stress. Without Lnt, the bacterial cell envelope becomes more permeable and modification of outer membrane lipoproteins is impaired. Cells of the lnt mutant have structural defects. The genome expression profile of Acinetobacter baylyi changes in response to lnt mutation. Phenotypes, overview
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malfunction
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Acinetobacter species can tolerate a complete loss-of-function mutation in gene lnt. Absence of a fully functional Lnt impairs modification of lipoproteins, increases outer membrane permeability and susceptibility to antibiotics, and alters normal cellular morphology. In addition, loss of lnt triggers a global transcriptional response to this added cellular stress. Without Lnt, the bacterial cell envelope becomes more permeable and modification of outer membrane lipoproteins is impaired. Cells of the lnt mutant have structural defects. The genome expression profile of Acinetobacter baylyi changes in response to lnt mutation. Phenotypes, overview
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malfunction
Acinetobacter baumannii AB5075-UW
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Acinetobacter species can tolerate a complete loss-of-function mutation in gene lnt. Absence of a fully functional Lnt impairs modification of lipoproteins, increases outer membrane permeability and susceptibility to antibiotics, and alters normal cellular morphology. In addition, loss of lnt triggers a global transcriptional response to this added cellular stress. Without Lnt, the bacterial cell envelope becomes more permeable and modification of outer membrane lipoproteins is impaired. Phenotypes, overview
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metabolism
genome expression profile of Acinetobacter baylyi changes in response to gene lnt mutation, overview
metabolism
in Gram-negative bacteria, lipid modification of proteins is catalysed in a three-step pathway. Apolipoprotein N-acyl transferase (Lnt) catalyses the third step in this pathway, whereby it transfers an acyl chain from a phospholipid to the amine group of the N-terminal cysteine residue of the apolipoprotein
metabolism
three membrane proteins are involved in processing precursors of lipoproteins, in the following order: the diacylglyceryl transferase Lgt, the signal peptidase LspA, and the N-acyltransferase Lnt
metabolism
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genome expression profile of Acinetobacter baylyi changes in response to gene lnt mutation, overview
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metabolism
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genome expression profile of Acinetobacter baylyi changes in response to gene lnt mutation, overview
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physiological function
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the enzyme is essential for the growth and viability of Salmonella typhimurium
physiological function
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the enzyme required for in vitro and in vivo growth
physiological function
lipoproteins are important components of the cell envelope and are responsible for many essential cellular functions. They are produced by the post-translational covalent attachment of lipids that occurs via a sequential 3-step process controlled by three integral membrane enzymes. The last step of this process, unique to Gram-negative bacteria, is the N-acylation of the terminal cysteine by apolipoprotein N-acyltransferase (Lnt) to form the final mature lipoprotein
physiological function
Lnt acts on apolipoproteins. It catalyzes the transfer of an acyl chain from the sn-1 position of a lipid to the N-terminal cysteine, generating a triacylated lipoprotein. In its structure, a catalytic triad (E267/K335/C387) is accessible near TMHs 3, 4 and 5, and a long and unique loop (also described as an arm, lid, etc.) containing a short helix
physiological function
proper acylation of outer membrane lipoprotein BamD requires enzyme Lnt in Acinetobacter baylyi. Lnt is required for full maturation of outer membrane lipoprotein BamD
physiological function
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proper acylation of outer membrane lipoprotein BamD requires enzyme Lnt in Acinetobacter baylyi. Lnt is required for full maturation of outer membrane lipoprotein BamD
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physiological function
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proper acylation of outer membrane lipoprotein BamD requires enzyme Lnt in Acinetobacter baylyi. Lnt is required for full maturation of outer membrane lipoprotein BamD
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additional information
catalytic mechanism two-step reaction catalysed by Lnt, catalytic residue Cys387, the transacylation reaction uses a ping-pong mechanism, structure of the active site with catalytic triad and Glu343, overview. Lnt activity depends on its affinity to the lipid substrate. 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. Essential Lnt residues are located within the central cavity. Molecular dynamics simulations
additional information
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catalytic mechanism two-step reaction catalysed by Lnt, catalytic residue Cys387, the transacylation reaction uses a ping-pong mechanism, structure of the active site with catalytic triad and Glu343, overview. Lnt activity depends on its affinity to the lipid substrate. 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. Essential Lnt residues are located within the central cavity. Molecular dynamics simulations
additional information
structure-function analysis of enzyme Lnt, significance of unique features in terms of substrate's recognition and binding mechanism influenced by exclusive residues, two transmembrane helices, and a flexible loop, structure comparisons, detailed overview. In the Lnt structure, a catalytic triad (E267/K335/C387) is accessible near TMHs 3, 4 and 5, and a long and unique loop (also described as an arm, lid, etc.) containing a short helix. The Lnt full reaction occurs as a two-step ping-pong. E343 as an important and conserved residue
additional information
two crystal forms of Lnt from Escherichia coli are observed. In one form a highly dynamic arm occurs that is able to restrict access to the active site as well as a covalent modification to the active site cysteine consistent with the thioester acyl-intermediate. In the second form, the enzyme crystallizes in an open conformation exposing the active site to the environment. Three unique Lnt molecules that when taken together suggest the movement of essential loops and residues are triggered by substrate binding that could control the interaction between Lnt and the incoming substrate apolipoprotein, mechanism, detailed overview. In the case of Lnt, the nitrilase domain catalyzes the attachment of a fatty acid derived from a phospholipid to the alpha-amino group of the N-terminal cysteine of the apolipoprotein creating the final mature lipoprotein. This attachment occurs via a proposed 2-step ping-pong mechanism where the first step is the acyl transfer of the phospholipid substrate to create a thioester linkage on the active site cysteine. The second step is the transfer of the acyl chain from this cysteine to the N-terminal cysteine of the apolipoprotein. This occurs at the catalytic triad of E267-K335-C387 where E267 acts as a general base to activate the nucleophile of the thiol group of C387 that can then attack the ester linkage between the acyl chain and the glycerol backbone of the phospholipid substrate to form the thioester acyl intermediate. K335 provides part of the oxyanion hole to stabilize this tetrahedral intermediate of the reaction. In the second step, with Lnt now in its thioester-acyl intermediate state, the alpha-amino group at the N-terminus of the incoming apolipoprotein attacks the thioester linkage to transfer the acyl chain to produce the final mature lipoprotein. Similar to the first step, K335 stabilizes the tetrahedral intermediate of the reaction. Docking study and molecular dynamics simulations
additional information
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two crystal forms of Lnt from Escherichia coli are observed. In one form a highly dynamic arm occurs that is able to restrict access to the active site as well as a covalent modification to the active site cysteine consistent with the thioester acyl-intermediate. In the second form, the enzyme crystallizes in an open conformation exposing the active site to the environment. Three unique Lnt molecules that when taken together suggest the movement of essential loops and residues are triggered by substrate binding that could control the interaction between Lnt and the incoming substrate apolipoprotein, mechanism, detailed overview. In the case of Lnt, the nitrilase domain catalyzes the attachment of a fatty acid derived from a phospholipid to the alpha-amino group of the N-terminal cysteine of the apolipoprotein creating the final mature lipoprotein. This attachment occurs via a proposed 2-step ping-pong mechanism where the first step is the acyl transfer of the phospholipid substrate to create a thioester linkage on the active site cysteine. The second step is the transfer of the acyl chain from this cysteine to the N-terminal cysteine of the apolipoprotein. This occurs at the catalytic triad of E267-K335-C387 where E267 acts as a general base to activate the nucleophile of the thiol group of C387 that can then attack the ester linkage between the acyl chain and the glycerol backbone of the phospholipid substrate to form the thioester acyl intermediate. K335 provides part of the oxyanion hole to stabilize this tetrahedral intermediate of the reaction. In the second step, with Lnt now in its thioester-acyl intermediate state, the alpha-amino group at the N-terminus of the incoming apolipoprotein attacks the thioester linkage to transfer the acyl chain to produce the final mature lipoprotein. Similar to the first step, K335 stabilizes the tetrahedral intermediate of the reaction. Docking study and molecular dynamics simulations
Show AA Sequence and Transmembrane Helices (27185 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C387A
C387S
E389A
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
R352A
site-directed mutagenesis, a Nit domain residue, the mutant cannot complement enzyme-deficient mutant DELTAlnt cells
V339A
site-directed mutagenesis, a Nit domain residue, the mutant cannot complement enzyme-deficient mutant DELTAlnt cells
W237A
Y388A
additional information
C387S
site-directed mutagenesis, the mutant catalyzes the 1st step of the N-acyl transfer reaction and forms a oxygen-ester acyl intermediate but is unable to transfer the acyl group onto apolipoprotein
E389A
site-directed mutagenesis, a Nit domain residue, the mutant cannot complement enzyme-deficient mutant DELTAlnt cells
Y388A
site-directed mutagenesis, a Nit domain residue, the mutant cannot complement enzyme-deficient mutant DELTAlnt cells
additional information
generation of loss-of-function mutants of Lnt, i.e. lnt153::T26, phenotypes, overview
additional information
Acinetobacter baumannii AB5075-UW
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generation of loss-of-function mutants of Lnt, i.e. lnt153::T26, phenotypes, overview
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additional information
generation of loss-of-function mutants of Lnt, phenotypes, overview
additional information
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generation of loss-of-function mutants of Lnt, phenotypes, overview
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additional information
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generation of loss-of-function mutants of Lnt, phenotypes, overview
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additional information
generation of a DELTAlnt knockout strain, complementation by expression of the wild-type Lnt enzyme
additional information
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generation of a DELTAlnt knockout strain, complementation by expression of the wild-type Lnt enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
recombinant His-tagged wild-type enzyme from Escherichia coli strain C41(DE3) and His-tagged Se-Met-labeled Lnt from Escherichia coli strain B834 (DE3), both by nickel affinity chromatography, desalting gel filtration, ion exchange chromatography, and ultrafiltration and gel filtration
recombinant His8-tagged enzyme from Escherichia coli strain C41(DE3) membrane fraction by nickel affinity chromatography, ultrafiltration, gel filtration, and again ultrafiltration
recombinant Strep-tagged wild-type and mutant enzymes from Escherichia coli by affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41(DE3) cells
gene lnt, recombinant expression of C-terminally His8-tagged enzyme in Escherichia coli strain C41(DE3)
gene lnt, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain C41(DE3), the His-tagged selenomethionine (Se-Met) labeled Lnt is expressed in Escherichia coli methionine-auxotrophy strain B834 (DE3), recombinant expression of enzyme point mutants in Escherichia coli DELTAlnt knockout strain for complementation studies
gene lnt, recombinant overexpression of Strep-tagged wild-type and mutant enzymes in Escherichia coli
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REF.