Enzymes
| UniProtKB help_outline | 20,897 proteins |
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- Name help_outline a CDP-1,2-diacyl-sn-glycerol Identifier CHEBI:58332 Charge -2 Formula C14H17N3O15P2R2 SMILEShelp_outline Nc1ccn([C@@H]2O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@@H](COC([*])=O)OC([*])=O)[C@@H](O)[C@H]2O)c(=O)n1 2D coordinates Mol file for the small molecule Search links Involved in 19 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-serine Identifier CHEBI:33384 Charge 0 Formula C3H7NO3 InChIKeyhelp_outline MTCFGRXMJLQNBG-REOHCLBHSA-N SMILEShelp_outline [NH3+][C@@H](CO)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 78 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1,2-diacyl-sn-glycero-3-phospho-L-serine Identifier CHEBI:57262 Charge -1 Formula C8H11NO10PR2 SMILEShelp_outline [NH3+][C@@H](COP([O-])(=O)OC[C@@H](COC([*])=O)OC([*])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 46 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CMP Identifier CHEBI:60377 Charge -2 Formula C9H12N3O8P InChIKeyhelp_outline IERHLVCPSMICTF-XVFCMESISA-L SMILEShelp_outline Nc1ccn([C@@H]2O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]2O)c(=O)n1 2D coordinates Mol file for the small molecule Search links Involved in 164 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:16913 | RHEA:16914 | RHEA:16915 | RHEA:16916 | |
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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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Ribosomal-associated phosphatidylserine synthetase from Escherichia coli: purification by substrate-specific elution from phosphocellulose using cytidine 5'-diphospho-1,2-diacyl-sn-glycerol.
Larson T.J., Dowhan W.
Cytidine 5'-diphospho-1,2-diacyl-sn-glycerol (CDPdiglyceride):L-serine O-phosphatidyltransferase (EC 2.7.8.8, phosphatidylserine synthetase) is bound tightly to the ribosomes in crude extracts of Escherichia coli. After separation of the enzyme from the ribosomes by the method of Raetz and Kennedy ... >> More
Cytidine 5'-diphospho-1,2-diacyl-sn-glycerol (CDPdiglyceride):L-serine O-phosphatidyltransferase (EC 2.7.8.8, phosphatidylserine synthetase) is bound tightly to the ribosomes in crude extracts of Escherichia coli. After separation of the enzyme from the ribosomes by the method of Raetz and Kennedy (Raetz, C.R.H., and Kennedy, E.P. (1974), J. Biol. Chem. 249, 5038), we have purified the enzyme to 97% of homogenekty. The major portion of the overall 5500-fold purification was attained by substrate-specific elution from phosphocellulose using CDP-diglyceride in the presence of detergent. The purified enzyme migrated as a single band with an apparent minimum molecular weight of 54 000 when subjected to electrophoresis on polyacrylamide disc gels containing sodium dodecyl sulfate. The purified enzyme catalyzed exchange reactions between cytidine 5'-monophosphate (CMP) and CDP-diglyceride and between serine and phosphatidylserine. The enzyme also catalyzed the hydrolysis of CDP-diglyceride to form CMP and phosphatidic acid. dCDP-diglyceride was equivalent to CDP-diglyceride in all reactions catalyzed by the enzyme. In addition, the purified enzyme catalyzed the formation of phosphatidylglycerol or phosphatidylglycerophosphate at a very slow rate when serine was replaced as substrate by glycerol or sn-glycero-3-phosphate, respectively. These results suggest catalysis occurs via a ping-pong mechanism through the formation of a phosphatidyl-enzyme intermediate. << Less