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Information on EC 2.7.8.B10 - cardiolipin synthase A
for references in articles please use BRENDA:EC2.7.8.B10preliminary BRENDA-supplied EC number
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EC Tree
2.7.8.B10 cardiolipin synthase ASpecify your search results
Word Map
- 2.7.8.B10
- phospholipid
- cdp-diacylglycerol
-
phosphatidylglycerolphosphate
-
cl-deficient
-
daptomycin
-
monolysocardiolipin
-
tafazzin
-
liafsr
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cardiolipin synthase, cl synthase, cls_pld, cls447a, cardiolipin synthase a, cardiolipin synthase b, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cardiolipin synthase
CL synthase
CLS
CLS1
cls2
Cls447a
clsA
clsB
clsC
CLS_pld
SA1155
SA1891
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a phosphatidylglycerol + a phosphatidylglycerol = a cardiolipin + glycerol
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-1-phosphatidylglycerol:L-1-phosphatidylglycerol acylphosphatidate transferase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a phosphatidylglycerol + a phosphatidyl-glycerol
a cardiolipin + glycerol
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
cardiolipin + glycerol
-
-
-
?
chicken egg phosphatidylglycerol + chicken egg phosphatidylglycerol
a cardiolipin + glycerol
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
Cafeteria sp.
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
Enterococcus faecium S613
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
the f413 protein catalyzes cardiolipin formation in vitro but not in vivo
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
chicken egg phosphatidylglycerol + chicken egg phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
chicken egg phosphatidylglycerol + chicken egg phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
chicken egg phosphatidylglycerol + chicken egg phosphatidylglycerol
a cardiolipin + glycerol
Enterococcus faecium S613
-
-
-
-
?
additional information
?
-
-
the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin
-
-
?
additional information
?
-
-
the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
Cafeteria sp.
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
Enterococcus faecium S613
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
-
-
-
-
?
additional information
?
-
-
the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin
-
-
?
additional information
?
-
-
the enzyme homologue ClsA uses only phosphatidylglycerol as substrate in the synthesis of cardiolipin
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
divalent metals Mg2+, Co2+, and Cd2+ have no measurable effect on enzyme activity at 4 mM, indicating that metal ions are not required for activity
additional information
Mg2+ concentrations of up to 80 mM has no effect on activity
additional information
-
Mg2+ concentrations of up to 80 mM has no effect on activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by phosphatidylinositol and bis-phosphatidate
-
cardiolipin
-
phosphatidylethanolamine partially offsets inhibition by cardiolipin
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CDP-dipalmitin
-
stimulates the reaction but does not participate as phosphatidyl donor
additional information
enzyme Cls1 can induce CL production in response to broad high osmolality stressors, such as 4 M NaCl, 4 M KCl or 20% raffinose in the cls2 mutant (Ncls2), although not in the wild-type
-
additional information
enzyme Cls1 can induce CL production in response to broad high osmolality stressors, such as 4 M NaCl, 4 M KCl or 20% raffinose in the cls2 mutant (Ncls2), although not in the wild-type
-
additional information
-
enzyme Cls1 can induce CL production in response to broad high osmolality stressors, such as 4 M NaCl, 4 M KCl or 20% raffinose in the cls2 mutant (Ncls2), although not in the wild-type
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Hepatocellular
Reduced cardiolipin content decreases respiratory chain capacities and increases ATP synthesis yield in the human HepaRG cells.
Glioma
Effects of siRNA-dependent knock-down of cardiolipin synthase and tafazzin on mitochondria and proliferation of glioma cells.
Hyperinsulinism
Expression of monolysocardiolipin acyltransferase activity is regulated in concert with the level of cardiolipin and cardiolipin biosynthesis in the mammalian heart.
Hyperthyroidism
Expression of monolysocardiolipin acyltransferase activity is regulated in concert with the level of cardiolipin and cardiolipin biosynthesis in the mammalian heart.
Teratocarcinoma
Expression of monolysocardiolipin acyltransferase activity is regulated in concert with the level of cardiolipin and cardiolipin biosynthesis in the mammalian heart.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.55
a phosphatidylglycerol
-
recombinant wild-type enzyme, residues 52-482, pH 7.4, 37°C
3.66
a phosphatidylglycerol
-
recombinant mutant H215R enzyme, residues 52-482, pH 7.4, 37°C
6.25
a phosphatidylglycerol
-
recombinant mutant R218Q enzyme, residues 52-482, pH 7.4, 37°C
3.55
chicken egg phosphatidylglycerol
-
pH 7.4, 37°C, wild-type enzyme
-
3.6 - 6
chicken egg phosphatidylglycerol
-
pH 7.4, 37°C, mutant enzyme H215R
-
6.25
chicken egg phosphatidylglycerol
-
pH 7.4, 37°C, mutant enzyme R218Q
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160
-
substrate: chicken egg phosphatidylglycerol, pH 7.4, 37°C, wild-type enzyme
260
260
-
substrate: chicken egg phosphatidylglycerol, pH 7.4, 37°C, mutant enzyme H215R
260
-
substrate: chicken egg phosphatidylglycerol, pH 7.4, 37°C, mutant enzyme R218Q
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6.2
-
pH 4.0: about 45% of maximal activity, pH 6.2: about 35% of maximal activity, in phosphate buffer
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Alkalihalophilus pseudofirmus
and methionine auxotroph derivative strain 811M
UniProt
brenda
Alkalihalophilus pseudofirmus OF4
and methionine auxotroph derivative strain 811M
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
septal membranes. Recombinant GFP fusion proteins of enzyme ClsA with N-terminal and internal deletions retain septal localization. Enzyme mutants with deletions starting from the C-terminus (Leu482) cease to localize to the septum once the deletion passes the Ile residue at 448, indicating that the sequence responsible for septal localization is confined within a short distance from the C-terminus. Enzyme ClsA contains a specific region responsible for the septal membrane localization
brenda
-
septal membranes. Recombinant GFP fusion proteins of enzyme ClsA with N-terminal and internal deletions retain septal localization. Enzyme mutants with deletions starting from the C-terminus (Leu482) cease to localize to the septum once the deletion passes the Ile residue at 448, indicating that the sequence responsible for septal localization is confined within a short distance from the C-terminus. Enzyme ClsA contains a specific region responsible for the septal membrane localization
-
brenda
-
enzyme Cls613a is tightly associated with the membrane and colocalizes with its substrate phosphatidylglycerol and product cardiolipin
brenda
-
enzyme Cls613a is tightly associated with the membrane and colocalizes with its substrate phosphatidylglycerol and product cardiolipin
-
brenda
-
enzyme Cls447a is tightly associated with the membrane and colocalizes with its substrate phosphatidylglycerol and product cardiolipin
brenda
-
enzyme Cls447a is tightly associated with the membrane and colocalizes with its substrate phosphatidylglycerol and product cardiolipin
-
brenda
Enterococcus faecium S613
-
enzyme Cls447a is tightly associated with the membrane and colocalizes with its substrate phosphatidylglycerol and product cardiolipin
-
brenda
-
ClsA is membrane-anchored, with dual, cytoplasmic, catalytic domains
brenda
additional information
-
two sequences, Ile436-Leu450 and Leu466-Leu478, individually form an amphipathic alpha-helix. The configuration is a membrane targeting sequence (MTS), MTS2 and MTS1, respectively. Either one has the ability to affect septal localization, and each of these sequences by itself localizes to the septum
-
brenda
additional information
-
two sequences, Ile436-Leu450 and Leu466-Leu478, individually form an amphipathic alpha-helix. The configuration is a membrane targeting sequence (MTS), MTS2 and MTS1, respectively. Either one has the ability to affect septal localization, and each of these sequences by itself localizes to the septum
-
-
brenda
additional information
-
in mitochondrion-related organelles (degenerated mitochondria)
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Cafeteria sp.
-
CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, and CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, function in bacteria and eukaryotes (mitochondria), respectively. Phylogenetic analysis, overview. Exceptions to the above-mentioned hypothesis regarding CLS phylogenetic distribution, in which CLS_pld and CLS_cap are exclusively found in bacteria and eukaryotes, respectively, are found in actinobacteria and proteobacteria, that contain CLS_cap-like proteins. The eukaryotic supergroups Amoebozoa, Excavata, and Alveolata, a subgroup of the supergroup SAR, have only CLS_pld (without phylogenetic affiliation to any particular bacterial homologues), while the supergroups Opisthokonta (including animals and fungi) and Archaeplastida (including land plants) along with another SAR subgroup stramenopiles possess only CLS_cap (closely related to alpha-proteobacterial homologues). Cafeteria sp. Caron contains both, a CLS_cap enzyme homologue, and a CLS_pld homologue
evolution
-
CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, and CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, function in bacteria and eukaryotes (mitochondria), respectively. Phylogenetic analysis, overview. Exceptions to the above-mentioned hypothesis regarding CLS phylogenetic distribution, in which CLS_pld and CLS_cap are exclusively found in bacteria and eukaryotes, respectively, are found in actinobacteria and proteobacteria, that contain CLS_cap-like proteins. The eukaryotic supergroups Amoebozoa, Excavata, and Alveolata, a subgroup of the supergroup SAR, have only CLS_pld (without phylogenetic affiliation to any particular bacterial homologues), while the supergroups Opisthokonta (including animals and fungi) and Archaeplastida (including land plants) along with another SAR subgroup stramenopiles possess only CLS_cap (closely related to alpha-proteobacterial homologues). Cantina marsupialis contains only a CLS_pld enzyme homologue, no CLS_cap, EC 2.7.8.41, homologue
evolution
-
CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, and CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, function in bacteria and eukaryotes (mitochondria), respectively. Phylogenetic analysis, overview. Exceptions to the above-mentioned hypothesis regarding CLS phylogenetic distribution, in which CLS_pld and CLS_cap are exclusively found in bacteria and eukaryotes, respectively, are found in actinobacteria and proteobacteria, that contain CLS_cap-like proteins. The eukaryotic supergroups Amoebozoa, Excavata, and Alveolata, a subgroup of the supergroup SAR, have only CLS_pld (without phylogenetic affiliation to any particular bacterial homologues), while the supergroups Opisthokonta (including animals and fungi) and Archaeplastida (including land plants) along with another SAR subgroup stramenopiles possess only CLS_cap (closely related to alpha-proteobacterial homologues). Wobblia lunata contains both, a CLS_cap enzyme homologue, and a CLS_pld homologue
evolution
phylogenetic analysis reveals that gene cls1 is generated through the duplication of gene cls2 after the divergence of the genus Staphylococcus
evolution
the enzyme is a member of the PLD superfamily of proteins, the enzyme is conserved among Moraxella catarrhalis isolates
evolution
-
phylogenetic analysis reveals that gene cls1 is generated through the duplication of gene cls2 after the divergence of the genus Staphylococcus
-
evolution
-
CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, and CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, function in bacteria and eukaryotes (mitochondria), respectively. Phylogenetic analysis, overview. Exceptions to the above-mentioned hypothesis regarding CLS phylogenetic distribution, in which CLS_pld and CLS_cap are exclusively found in bacteria and eukaryotes, respectively, are found in actinobacteria and proteobacteria, that contain CLS_cap-like proteins. The eukaryotic supergroups Amoebozoa, Excavata, and Alveolata, a subgroup of the supergroup SAR, have only CLS_pld (without phylogenetic affiliation to any particular bacterial homologues), while the supergroups Opisthokonta (including animals and fungi) and Archaeplastida (including land plants) along with another SAR subgroup stramenopiles possess only CLS_cap (closely related to alpha-proteobacterial homologues). Wobblia lunata contains both, a CLS_cap enzyme homologue, and a CLS_pld homologue
-
malfunction
Escherichia coli has three cardiolipin synthases. Cardiolipin synthase A encoded by clsA, cardiolipin synthase B encoded by clsB and cardiolipin synthase C, encoded by clsC. Triple deletions of clsA, clsB, and clsC results in the complete depletion of cardiolipin synthase activity in Escherichia coli cells. The double mutant DELTAclsAB mutant still makes cardiolipin in the stationary phase
malfunction
a cls1 mutant is equal to the wild-type in terms of CL accumulation and stress tolerance. But below pH 2.6, the cls1 mutant (i.e. carrying Cls2 alone) cannot produce cardiolipin
malfunction
a cls2 mutant (carrying Cls1 alone) effectively accumulates cardiolipin at pH 2.6 and below
malfunction
cardiolipin-deficient Moraxella catarrhalis exhibits wild-type growth in complete medium and under osmotic stress
malfunction
Alkalihalophilus pseudofirmus
no detectablecardiolipin is found in DELTAclsA mutants, whereas the cardiolipin precursor phosphatidylglycerol is elevated. The DELTAclsB mutant exhibits no significant reduction in cardiolipin, but at pH 7.5, clsB expression is upregulated and appears growth. In the absence of detectable cardiolipin, the alkaliphile shows no significant deficits in non-fermentative growth, respiration-dependent ATP synthesis, or salt tolerance. In long term survival experiments, significant growth defects are found in DELTAclsA strains and the DELTAclsC strain at pH10.5. Both the single DELTAclsA and triple deletion mutants have a significant reduction in NADH dehydrogenase activity
malfunction
-
a cls1 mutant is equal to the wild-type in terms of CL accumulation and stress tolerance. But below pH 2.6, the cls1 mutant (i.e. carrying Cls2 alone) cannot produce cardiolipin
-
malfunction
-
a cls2 mutant (carrying Cls1 alone) effectively accumulates cardiolipin at pH 2.6 and below
-
malfunction
Alkalihalophilus pseudofirmus OF4
-
no detectablecardiolipin is found in DELTAclsA mutants, whereas the cardiolipin precursor phosphatidylglycerol is elevated. The DELTAclsB mutant exhibits no significant reduction in cardiolipin, but at pH 7.5, clsB expression is upregulated and appears growth. In the absence of detectable cardiolipin, the alkaliphile shows no significant deficits in non-fermentative growth, respiration-dependent ATP synthesis, or salt tolerance. In long term survival experiments, significant growth defects are found in DELTAclsA strains and the DELTAclsC strain at pH10.5. Both the single DELTAclsA and triple deletion mutants have a significant reduction in NADH dehydrogenase activity
-
metabolism
-
cardiolipin is known to be biosynthesized by either of two phylogenetically distinct enzymes: CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, which synthesizes cardiolipin from two molecules of phosphatidylglycerols or CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, which produces this lipid using a phosphatidylglycerol and a cytidine diphosphate diacylglycerol as substrates
metabolism
Cafeteria sp.
-
cardiolipin is known to be biosynthesized by either of two phylogenetically distinct enzymes: CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, which synthesizes cardiolipin from two molecules of phosphatidylglycerols or CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, which produces this lipid using a phosphatidylglycerol and a cytidine diphosphate diacylglycerol as substrates
metabolism
-
cardiolipin is known to be biosynthesized by either of two phylogenetically distinct enzymes: CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, which synthesizes cardiolipin from two molecules of phosphatidylglycerols or CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, which produces this lipid using a phosphatidylglycerol and a cytidine diphosphate diacylglycerol as substrates
metabolism
Alkalihalophilus pseudofirmus
the clsA gene plays a major role in cardiolipin biosynthesis
metabolism
Alkalihalophilus pseudofirmus OF4
-
the clsA gene plays a major role in cardiolipin biosynthesis
-
metabolism
-
cardiolipin is known to be biosynthesized by either of two phylogenetically distinct enzymes: CL synthase (CLS) with two phospholipase D domains, i.e. CLS_pld, which synthesizes cardiolipin from two molecules of phosphatidylglycerols or CLS with one CDP-alcohol phosphatidyltransferase domain, i.e. CLS_cap, which produces this lipid using a phosphatidylglycerol and a cytidine diphosphate diacylglycerol as substrates
-
physiological function
alternative cardiolipin synthase Cls1 compensates for stalled Cls2 function in Staphylococcus aureus under conditions of acute acid stress. Gene cls2 encodes a housekeeping-type CL synthase
physiological function
alternative cardiolipin synthase Cls1 compensates for stalled Cls2 function in Staphylococcus aureus under conditions of acute acid stress. The physiological role of cls1 is to synthesize cardiolipin under conditions of acute low-pH stress
physiological function
Alkalihalophilus pseudofirmus
cardiolipin is not essential for oxidative phosphorylation and the non-fermentative growth it supports in alkaliphilic Bacillus pseudofirmus strain OF4, during growth at either pH 7.5 or pH 10.5. Cardiolipin does not seem be a crucial participant in the proton movements on or near the membrane surface from proton-pumping respiratory chain complexes to the F1F0-ATP synthase complex
physiological function
enzyme MclS is responsible for the synthesis of cardiolipin, which is a major component of the Moraxella catarrhalis cell envelope, constituting 5-30% of the total membrane phospholipid. The mclS gene product is not required for optimal growth of Moraxella catarrhalis in vitro. Expression of the mclS gene product impacts the adherence of Moraxella catarrhalis to human epithelial cells. The contribution of mclS to adherence is indirect, possibly by modulating the proper surface display of Moraxella catarrhalis adhesins on the bacterial surface through its CLS activity
physiological function
-
the synthesis of cardiolipin from phosphatidylglycerol through the enzyme has the potential to alter membrane properties directly thorough the synthesis of cardiolipin or, more indirectly, by altering the amount of phosphatidylglycerol in the membrane
physiological function
-
the synthesis of cardiolipin from phosphatidylglycerol through the enzyme has the potential to alter membrane properties directly thorough the synthesis of cardiolipin or, more indirectly, by altering the amount of phosphatidylglycerol in the membrane
physiological function
a ClsA mutant has no cardiolipin detected within its membrane, grows normally in vitro, and invades cultured epithelial cells, but it fails to form plaques in epithelial cell monolayers. The ClsA mutant is initially motile within the host cell cytoplasm but forms filaments and loses motility during replication and fails to spread efficiently to neighboring cells
physiological function
a minor decrease of cardiolipin content is observed in the ClsA overexpression strain. Phosphatidylethanolamine and phosphatidylglycerol levels remain unaltered upon overexpression of ClsA. ClsA deletion leads to abolishment of phosphytidylcholine-dependent phosphatidylalcohol formation
physiological function
a modest increase of cardiolipin content is observed in the ClsB overexpression strain. Overexpression of ClsB also leads to an increase of phosphatidylethanolamine from 67% to 79% and a decrease of phosphatidylglycerol content from 31% to 14% of phospholipids. Overexpression of ClsB leads to formation of phosphatidylalcohols whereas levels of phosphatidylalcohols are unaltered in the clsB knockout mutant
physiological function
-
ClsA and proteins YdhP, YjbJ interact with transporter ProP. All three proteins are concentrated at the cell poles, but only ClsA localization was cardiolipin-dependent. ClsA is N-terminally processed and membrane-anchored, with dual, cytoplasmic, catalytic domains
physiological function
ClsB additionally catalyzes an alternative mechanism for phosphatidylglycerol synthesis that is PgsA-independent. The reaction in vivo and in vitro converts phosphatidylethanolamine and glycerol into phosphatidylglycerol. When the growth medium is supplemented with glycerol, the expression ClsB significantly increases phosphatidylglycerol and cardiolipin levels, with the growth deficiency of PgsA null strain also being complemented under such conditions
physiological function
-
alternative cardiolipin synthase Cls1 compensates for stalled Cls2 function in Staphylococcus aureus under conditions of acute acid stress. The physiological role of cls1 is to synthesize cardiolipin under conditions of acute low-pH stress
-
physiological function
-
alternative cardiolipin synthase Cls1 compensates for stalled Cls2 function in Staphylococcus aureus under conditions of acute acid stress. Gene cls2 encodes a housekeeping-type CL synthase
-
physiological function
Enterococcus faecium S613
-
the synthesis of cardiolipin from phosphatidylglycerol through the enzyme has the potential to alter membrane properties directly thorough the synthesis of cardiolipin or, more indirectly, by altering the amount of phosphatidylglycerol in the membrane
-
physiological function
Alkalihalophilus pseudofirmus OF4
-
cardiolipin is not essential for oxidative phosphorylation and the non-fermentative growth it supports in alkaliphilic Bacillus pseudofirmus strain OF4, during growth at either pH 7.5 or pH 10.5. Cardiolipin does not seem be a crucial participant in the proton movements on or near the membrane surface from proton-pumping respiratory chain complexes to the F1F0-ATP synthase complex
-
physiological function
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the synthesis of cardiolipin from phosphatidylglycerol through the enzyme has the potential to alter membrane properties directly thorough the synthesis of cardiolipin or, more indirectly, by altering the amount of phosphatidylglycerol in the membrane
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physiological function
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the synthesis of cardiolipin from phosphatidylglycerol through the enzyme has the potential to alter membrane properties directly thorough the synthesis of cardiolipin or, more indirectly, by altering the amount of phosphatidylglycerol in the membrane
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additional information
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daptomycin (DAP) is a cyclic lipopeptide antibiotic, that has demonstrated rapid in vitro bactericidal activity against clinically significant strains of Gram-positive bacteria. DAP inserts into the plasma membrane in a calcium-dependent manner and subsequently disrupts the functional integrity of the cell membrane, altering cell division. DAP forms membrane-associated oligomers on liposomes and bacterial cells, suggesting that it is phosphatidylglycerol-dependent oligomerization of DAP that contributes to its effectiveness in altering membrane homeostasis. Role of Cls and adaptive variants Cls447aR218Q and Cls447aH215R in altering cardiolipin synthesis
additional information
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the fact that the homologues YwiE and YwjE show almost no detectable cardiolipin synthesis activity in Bacillus subtilis cells under laboratory conditions, although both localize septally, suggests a much stricter consensus motif S-P-(I/L)-L for bacterial CL synthase, that is, the two residues in the middle of the four conserved residues may have to be taken into account for activity
additional information
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the fact that the homologues YwiE and YwjE show almost no detectable cardiolipin synthesis activity in Bacillus subtilis cells under laboratory conditions, although both localize septally, suggests a much stricter consensus motif S-P-(I/L)-L for bacterial CL synthase, that is, the two residues in the middle of the four conserved residues may have to be taken into account for activity
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additional information
Enterococcus faecium S613
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daptomycin (DAP) is a cyclic lipopeptide antibiotic, that has demonstrated rapid in vitro bactericidal activity against clinically significant strains of Gram-positive bacteria. DAP inserts into the plasma membrane in a calcium-dependent manner and subsequently disrupts the functional integrity of the cell membrane, altering cell division. DAP forms membrane-associated oligomers on liposomes and bacterial cells, suggesting that it is phosphatidylglycerol-dependent oligomerization of DAP that contributes to its effectiveness in altering membrane homeostasis. Role of Cls and adaptive variants Cls447aR218Q and Cls447aH215R in altering cardiolipin synthesis
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additional information
-
daptomycin (DAP) is a cyclic lipopeptide antibiotic, that has demonstrated rapid in vitro bactericidal activity against clinically significant strains of Gram-positive bacteria. DAP inserts into the plasma membrane in a calcium-dependent manner and subsequently disrupts the functional integrity of the cell membrane, altering cell division. DAP forms membrane-associated oligomers on liposomes and bacterial cells, suggesting that it is phosphatidylglycerol-dependent oligomerization of DAP that contributes to its effectiveness in altering membrane homeostasis. Role of Cls and adaptive variants Cls447aR218Q and Cls447aH215R in altering cardiolipin synthesis
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