Enzymes
| UniProtKB help_outline | 13,707 proteins |
| GO Molecular Function help_outline |
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- Name help_outline 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) Identifier CHEBI:64716 Charge -1 Formula C8H12O10PR2 SMILEShelp_outline OC[C@H](O)COP([O-])(=O)OC[C@@H](COC([*])=O)OC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 45 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a cardiolipin Identifier CHEBI:62237 Charge -2 Formula C13H16O17P2R4 SMILEShelp_outline OC(COP([O-])(=O)OC[C@@H](COC([*])=O)OC([*])=O)COP([O-])(=O)OC[C@@H](COC([*])=O)OC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 39 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline glycerol Identifier CHEBI:17754 (Beilstein: 635685; CAS: 56-81-5) help_outline Charge 0 Formula C3H8O3 InChIKeyhelp_outline PEDCQBHIVMGVHV-UHFFFAOYSA-N SMILEShelp_outline OCC(O)CO 2D coordinates Mol file for the small molecule Search links Involved in 74 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:31451 | RHEA:31452 | RHEA:31453 | RHEA:31454 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Amplification and substantial purification of cardiolipin synthase of Escherichia coli.
Hiraoka S., Nukui K., Uetake N., Ohta A., Shibuya I.
A simple, specific, and sensitive assay procedure for cardiolipin synthase of Escherichia coli has been developed. This measures the radioactivity of glycerol formed from phosphatidyl [2-3H]glycerol and is mainly based on the findings that 400 mM phosphate and 0.015% Triton X-100 markedly activate ... >> More
A simple, specific, and sensitive assay procedure for cardiolipin synthase of Escherichia coli has been developed. This measures the radioactivity of glycerol formed from phosphatidyl [2-3H]glycerol and is mainly based on the findings that 400 mM phosphate and 0.015% Triton X-100 markedly activate the enzyme. Cardiolipin synthase was amplified 760-fold upon induction with isopropyl beta-D-thiogalactoside in cells harboring a pBR322 derivative in which the cls gene encoding this enzyme was preceded by the tac promoter. Under these conditions, cardiolipin content increased, membrane potential decreased, spheroplasts became fragile, cells lost viability, and inducer-resistant mutants appeared at a high frequency. The amplification enabled the isolation of an enzyme preparation with a specific activity approximately 10,000-times higher than that of wild-type whole cell lysate. This purification was simply achieved by extraction of the crude membrane fraction with Triton X-100 and a single phosphocellulose column chromatography. This preparation, together with the crude envelope fraction, was used to characterize the basic properties of E. coli cardiolipin synthase, some of which were utilized in setting up the assay conditions. << Less
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A second Escherichia coli protein with CL synthase activity.
Guo D., Tropp B.E.
The Escherichia coli open reading frame f413, which has the potential to code for a polypeptide homologous to cardiolipin (CL) synthase, has been cloned. Its polypeptide product has a molecular mass of 48 kDa, is membrane-bound, and catalyzes CL formation but does not hydrolyze CL. A comparison of ... >> More
The Escherichia coli open reading frame f413, which has the potential to code for a polypeptide homologous to cardiolipin (CL) synthase, has been cloned. Its polypeptide product has a molecular mass of 48 kDa, is membrane-bound, and catalyzes CL formation but does not hydrolyze CL. A comparison of the sequences predicted for the polypeptides encoded by f413 and cls indicates that the N-terminal residues specified by cls may be unnecessary for CL synthase activity. Construction of a truncated cls gene and characterization of its polypeptide product have confirmed this conclusion. << Less
Biochim. Biophys. Acta 1483:263-274(2000) [PubMed] [EuropePMC]
Comments
Reaction catalyzed by cardiolipin synthase.