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Information on EC 2.7.8.B10 - cardiolipin synthase A and Organism(s) Escherichia coli and UniProt Accession P0AA84

for references in articles please use BRENDA:EC2.7.8.B10
preliminary BRENDA-supplied EC number
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Escherichia coli
UNIPROT: P0AA84 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cardiolipin synthase B
-
cardiolipin synthase A
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
L-1-phosphatidylglycerol:L-1-phosphatidylglycerol acylphosphatidate transferase
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
show the reaction diagram
the f413 protein catalyzes cardiolipin formation in vitro but not in vivo
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
cardiolipin + glycerol
show the reaction diagram
-
-
-
?
a phosphatidylglycerol + a phosphatidyl-glycerol
a cardiolipin + glycerol
show the reaction diagram
-
-
-
?
a phosphatidylglycerol + a phosphatidylglycerol
a cardiolipin + glycerol
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
potassium phosphate
maximal stimulation at 400 mM
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cardiolipin
-
phosphatidylethanolamine partially offsets inhibition by cardiolipin
EDTA
80 mM, 30% inhibition
phosphatidate
-
MgCl2 partially offsets inhibition by phosphatidate
additional information
-
not inhibited by phosphatidylinositol and bis-phosphatidate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CDP-dipalmitin
-
stimulates the reaction but does not participate as phosphatidyl donor
Triton
maximal activation at 0.015%
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
pH 7.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
x * 45000, SDS-PAGE
46000
-
x * 46000, SDS-PAGE
48000
x * 48000, deletion mutant that is missing residues 2–60, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
ClsA is N-terminally processed
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H113A
mutation in HKD motif, catalyticlly inactive
H291A
mutation in HKD motif, catalyticlly inactive
delT2-E60
a deletion mutant that is missing residues 2–60 produces a fully active protein
G59A
mutation has little if any effect on cardiolipin synthase processing or activity
H224A/H404A
-
mutations inactivate ClsA and compromise transporter ProP localization
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
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
loses almost all of its activity after 5 min
55
15 min, stable
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team