Enzyme - CDP-diacylglycerol diphosphatase

Alternative Name(s)
  • CDP-diacylglycerol pyrophosphatase.
  • CDP-diacylglycerol phosphatidylhydrolase.

Catalytic Activity

CDP-1,2-diacyl-sn-glycerol + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + CMP + 2 H(+)


There are no Cofactors for this Enzyme

Reaction Mechanism

    5-aminoimidazole ribotide (AIR) is a branch point metabolite in the biosynthetic pathways of purines and thiamin. Although AIR cannot be efficiently taken up by most bacteria, 5-aminoimidazole riboside (AIRs) can. Aminoimidazole riboside kinase catalyses the phosphorylation of AIRs into AIR to feed into purine and thiamin biosynthesis pathways.

    The mechanism proposed is mainly by homology to other ribokinases, such as human adenosine kinase. Asp 252 is a general base and deprotonates the 5' hydroxyl group of the ribose. The deprotonated hydroxyl attacks the gamma-phosphate of ATP in an inline displacement mechanism. The backbone amides of Gly 249, Ala 250, Gly 251 and Asp 252 act as an anion hole to stabilise negative charge build-up in the pentacovalent transition state. The products are AIR and ADP.
    Catalytic Residues
    AA Uniprot Uniprot Resid PDB PDB Resid
    Asp Q8ZKR2 252 1tz3 272
    Gly Q8ZKR2 249 1tz3 269
    Ala Q8ZKR2 250 1tz3 270
    Gly Q8ZKR2 251 1tz3 271

Reaction Parameters

There are no kinetic parameters information for this Enzyme

Associated Proteins

Protein name Organism
CDP-diacylglycerol pyrophosphatase Escherichia coli (strain K12)
Probable CDP-diacylglycerol pyrophosphatase Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Putative CDP-diacylglycerol phosphotidylhydrolase Pantoea vagans (strain C9-1)
CDPdiacylglycerol diphosphatase Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
CDP-diacylglycerol pyrophosphatase, putative Edwardsiella ictaluri (strain 93-146)