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Information on EC 2.7.8.B10 - cardiolipin synthase A and Organism(s) Escherichia coli and UniProt Accession P0A6H8
for references in articles please use BRENDA:EC2.7.8.B10preliminary BRENDA-supplied EC number
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2.7.8.B10 cardiolipin synthase ASpecify your search results
Word Map
- 2.7.8.B10
- phospholipid
- cdp-diacylglycerol
-
phosphatidylglycerolphosphate
-
cl-deficient
-
daptomycin
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monolysocardiolipin
-
tafazzin
-
liafsr
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
BRENDA
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
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-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
cardiolipin + glycerol
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
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-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
the f413 protein catalyzes cardiolipin formation in vitro but not in vivo
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cardiolipin
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phosphatidylethanolamine partially offsets inhibition by cardiolipin
additional information
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not inhibited by phosphatidylinositol and bis-phosphatidate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CDP-dipalmitin
-
stimulates the reaction but does not participate as phosphatidyl donor
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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ClsA is membrane-anchored, with dual, cytoplasmic, catalytic domains
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
physiological function
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
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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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48000
x * 48000, deletion mutant that is missing residues 260, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
delT2-E60
a deletion mutant that is missing residues 260 produces a fully active protein
G59A
mutation has little if any effect on cardiolipin synthase processing or activity
L7S/V8S
an EYMPE epitope tag is introduced into the interior of Cardiolipin synthase. The tagged polypeptide retains the biological properties of wild type enzyme, including full enzymatic activity. Site-directed mutagenesis is used to alter conserved residues in the N-terminal region. An tagged cardiolipin synthase in which Leu7 and Val8 are both replaced by Ser residues retains in vitro activity but loses most of its in vivo activity. The mutant protein has a higher apparent molecular mass than its parent protein. That conserved residues L7 and V8 play a role in polypeptide processing, topology, or both
H224A/H404A
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mutations inactivate ClsA and compromise transporter ProP localization
additional information
additional information
cls has about 100 residues at the N-terminus that are missing from the polypeptide specified by the homologous gene f413 (cardiolipin synthase B). The f413 protein catalyzes cardiolipin formation in vitro but not in vivo. Amino acid residues specified by the first 60 codons in cls are not essential for catalytic activity
additional information
cls has about 100 residues at the N-terminus that are missing from the polypeptide specified by the homologous gene f413 (cardiolipin synthase B). The f413 protein catalyzes cardiolipin formation in vitro but not in vivo. Amino acid residues specified by the first 60 codons in cls are not essential for catalytic activity
additional information
-
cls has about 100 residues at the N-terminus that are missing from the polypeptide specified by the homologous gene f413 (cardiolipin synthase B). The f413 protein catalyzes cardiolipin formation in vitro but not in vivo. Amino acid residues specified by the first 60 codons in cls are not essential for catalytic activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ragolia, L.; Tropp, B.E.
The effects of phosphoglycerides on Escherichia coli cardiolipin synthase
Biochim. Biophys. Acta
1214
323-332
1994
Escherichia coli
Guo, D.; Tropp, B.E.
A second Escherichia coli protein with CL synthase activity
Biochim. Biophys. Acta
1483
263-274
2000
Escherichia coli (P0A6H8), Escherichia coli (P0AA84), Escherichia coli
Quigley, B.R.; Tropp, B.E.
E. coli cardiolipin synthase: function of N-terminal conserved residues
Biochim. Biophys. Acta
1788
2107-2113
2009
Escherichia coli (P0A6H8), Escherichia coli
Hiraoka, S.; Nukui, K.; Uetake, N.; Ohta, A.; Shibuya, I.
Amplification and substantial purification of cardiolipin synthase of Escherichia coli
J. Biochem.
110
443-449
1991
Escherichia coli (P0A6H8), Escherichia coli
Tan, B.K.; Bogdanov, M.; Zhao, J.; Dowhan, W.; Raetz, C.R.; Guan, Z.
Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates
Proc. Natl. Acad. Sci. USA
109
16504-16509
2012
Escherichia coli (P0A6H8), Escherichia coli (P0AA84), Escherichia coli
Hirschberg, C.B.; Kennedy, E.P.
Mechanism of the enzymatic synthesis of cardiolipin in Escherichia coli
Proc. Natl. Acad. Sci. USA
69
648-651
1972
Escherichia coli
Jeucken, A.; Helms, J.; Brouwers, J.
Cardiolipin synthases of Escherichia coli have phospholipid class specific phospholipase D activity dependent on endogenous and foreign phospholipids
Biochim. Biophys. Acta
1863
1345-1353
2018
Escherichia coli (P0A6H8), Escherichia coli (P0AA84)
Li, C.; Tan, B.K.; Zhao, J.; Guan, Z.
In vivo and in vitro synthesis of phosphatidylglycerol by an Escherichia coli cardiolipin synthase
J. Biol. Chem.
291
25144-25153
2016
Escherichia coli (P0AA84), Escherichia coli
Romantsov, T.; Gonzalez, K.; Sahtout, N.; Culham, D.E.; Coumoundouros, C.; Garner, J.; Kerr, C.H.; Chang, L.; Turner, R.J.; Wood, J.M.
Cardiolipin synthase A colocalizes with cardiolipin and osmosensing transporter ProP at the poles of Escherichia coli cells
Mol. Microbiol.
107
623-638
2018
Escherichia coli
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