If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
|Superclasses:||Biosynthesis → Cofactors, Prosthetic Groups, Electron Carriers Biosynthesis|
The ACP component of active citrate lyase, CitD, contains the prosthetic group 2'-(5'-phosphoribosyl)-3'-dephospho-CoA.
CitG catalyzes the synthesis of prosthetic group precursor 2'-(5''-triphospho-α-D-ribosyl)-3'-dephospho-CoA from dephospho-CoA and ATP. CitX subsequently transfers the prosthetic group to the apo-ACP protein of citrate lyase, converting it to the active holo-ACP form [Schneider00b, Schneider00a].
Schneider00a: Schneider K, Dimroth P, Bott M (2000). "Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group." FEBS Lett 2000;483(2-3);165-8. PMID: 11042274
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Hoenke00a: Hoenke S, Schmid M, Dimroth P (2000). "Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ancient class of nucleotidyltransferases." Biochemistry 39(43);13233-40. PMID: 11052676
Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554
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