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Information on EC 2.7.8.B11 - cardiolipin synthase C and Organism(s) Escherichia coli and UniProt Accession P75919

for references in articles please use BRENDA:EC2.7.8.B11
preliminary BRENDA-supplied EC number
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Escherichia coli
UNIPROT: P75919 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Escherichia coli
Synonyms
cardiolipin synthase, clsC, ClsC1, YmdC, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cardiolipin synthase
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
L-1-phosphatidylglycerol:phosphatidylethanolamine acylphosphatidate phosphotransferase
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(1-heptadecanoyl-2-((9Z)-tetradec-9-enoyl)-sn-glycero-3-phospho)-sn-glycerol + 1-dodecanoyl-2-tridecanoyl-sn-glycero-3-phosphoethanolamine
1-(1-heptadecanoyl-2-((9Z)-tetradec-9-enoyl)-sn-glycero-3-phospho)-3-(1-dodecanoyl-2-tridecanoyl-sn-glycero-3-phospho)glycerol + ethanolamine
show the reaction diagram
synthetic phosphatidylglycerol (17:0/14:1) and synthetic phosphatidylethanolamine (12:0/13:0). Reaction is catalyzed by the two-component complex YmdB-ClsC. 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. Deletion of all three genes (DELTAclsABC) results in a complete lack of cardiolipin. Restoration of near–wild-type levels of cardiolipin production in the stationary phase by expression of clsC in the triple mutant requires the coexpression from the same operon of the preceding gene ymdB. The mode of cardiolipin biosynthesis by the combined YmdB-ClsC follows neither the “eukaryotic” nor “prokaryotic” pathway but involves the transfer of a phosphatidyl moiety from phosphatidylethanolamine to the terminal free hydroxyl of phosphatidylglycerol to form cardiolipin
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-
?
a phosphatidylglycerol + a phosphatidylethanolamine
a cardiolipin + ethanolamine
show the reaction diagram
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?
additional information
?
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the enzyme homologue ClsC1 (YmdC) uses both phosphatidylethanolamine and phoshatidylglycerol as substrates for cardiolipin synthesis with the assistance of YmdB (ClsC2), the product of a neighboring gene. Enzyme homologue ClsB may also use some phospholipid other than phosphatidylglycerol
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?
NATURAL SUBSTRATE
NATURAL 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 phosphatidylethanolamine
a cardiolipin + ethanolamine
show the reaction diagram
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-
-
-
?
additional information
?
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the enzyme homologue ClsC1 (YmdC) uses both phosphatidylethanolamine and phoshatidylglycerol as substrates for cardiolipin synthesis with the assistance of YmdB (ClsC2), the product of a neighboring gene. Enzyme homologue ClsB may also use some phospholipid other than phosphatidylglycerol
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
reaction is catalyzed by the two-component complex YmdB-ClsC
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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. Deletion of all three genes (DELTAclsABC) results in a complete lack of cardiolipin. Restoration of near–wild-type levels of cardiolipin production in the stationary phase by expression of clsC in the triple mutant requires the coexpression from the same operon of the preceding gene ymdB. The mode of cardiolipin biosynthesis by the combined YmdB-ClsC follows neither the “eukaryotic” nor “prokaryotic” pathway but involves the transfer of a phosphatidyl moiety from PE to the terminal free hydroxyl of PG to form cardiolipin
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (P75919)
Manually annotated by BRENDA team
Kusaka, J.; Shuto, S.; Imai, Y.; Ishikawa, K.; Saito, T.; Natori, K.; Matsuoka, S.; Hara, H.; Matsumoto, K.
Septal localization by membrane targeting sequences and a conserved sequence essential for activity at the COOH-terminus of Bacillus subtilis cardiolipin synthase
Res. Microbiol.
167
202-214
2016
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 (P75919)
Manually annotated by BRENDA team