ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP. The reaction involves the formation of a new alpha (1''->2') glycosidic bond between the two ribosyl moieties, with concomitant displacement of the adenine moiety of ATP [1,4]. The 2'-(5-triphosphoribosyl)-3'-dephospho-CoA produced can be transferred by EC 2.7.7.61, citrate lyase holo-[acyl-carrier protein] synthase, to the apo-acyl-carrier protein subunit (gamma-subunit) of EC 4.1.3.6, citrate (pro-3S) lyase, thus converting it from an apo-enzyme into a holo-enzyme [1,3]. Alternatively, it can be transferred to the apo-ACP subunit of malonate decarboxylase by the action of EC 2.7.7.66, malonate decarboxylase holo-[acyl-carrier protein] synthase .
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP. The reaction involves the formation of a new alpha (1''->2') glycosidic bond between the two ribosyl moieties, with concomitant displacement of the adenine moiety of ATP [1,4]. The 2'-(5-triphosphoribosyl)-3'-dephospho-CoA produced can be transferred by EC 2.7.7.61, citrate lyase holo-[acyl-carrier protein] synthase, to the apo-acyl-carrier protein subunit (gamma-subunit) of EC 4.1.3.6, citrate (pro-3S) lyase, thus converting it from an apo-enzyme into a holo-enzyme [1,3]. Alternatively, it can be transferred to the apo-ACP subunit of malonate decarboxylase by the action of EC 2.7.7.66, malonate decarboxylase holo-[acyl-carrier protein] synthase [4].
accessory enzyme required for synthesis of an active citrate lyase complex, part of the operon encoding the citrate lyase complex, acid-inducible transcription of the operon encoding the citrate lysae complex
CitG catalyzes the conversion of ATP and dephospho-CoA to adenine and 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA, the predicted precursor of the prosthetic group of the gamma-subunit of citrate lyase EC 4.1.3.6. This precursor is transferred by CitX to apo-acyl carrier protein, yielding holo-acyl carrier protein
holo-acyl carrier protein formation proceeds as follows. First, a prosthetic group precursor, presumably 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA, is formed from ATP and dephospho-CoA in a reaction catalyzed by CitG. Second, holo-ACP is formed from apo-ACP and the prosthetic group precursor in a reaction catalyzed by CitX. The conversion of apo-cyl carrier protein into holo-cyl carrier protein is achieved in vitro by incubation of apo-cyl carrier protein with proteins CitX, CitG, ATP, and dephospho-CoA. ATP cannot be substituted with GTP, CTP, UTP, ADP, or AMP. In the absence of CitG or dephospho-CoA, AMP-cyl carrier protein is formed. It is not possible to further convert AMP-cyl carrier protein to holo-cyl carrier protein by subsequent incubation with CitG and dephospho-CoA
holo-acyl carrier protein formation proceeds as follows. First, a prosthetic group precursor, presumably 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA, is formed from ATP and dephospho-CoA in a reaction catalyzed by CitG. Second, holo-ACP is formed from apo-ACP and the prosthetic group precursor in a reaction catalyzed by CitX. The conversion of apo-cyl carrier protein into holo-cyl carrier protein is achieved in vitro by incubation of apo-cyl carrier protein with proteins CitX, CitG, ATP, and dephospho-CoA. ATP cannot be substituted with GTP, CTP, UTP, ADP, or AMP. In the absence of CitG or dephospho-CoA, AMP-cyl carrier protein is formed. It is not possible to further convert AMP-cyl carrier protein to holo-cyl carrier protein by subsequent incubation with CitG and dephospho-CoA
enzyme catalyzes starting reaction in biosynthesis of holo acyl carrier protein from the unmodified apoprotein, catalyzed by MdcB and MdcG and involving the formation of an activated precursor of the prosthetic group. In a first step, the ATP:dephospho-CoA 5¢-triphosphoribosyl transferase MdcB catalyzes the formation of the glycosidic bond between the ribosyl moieties from ATP and dephospho-CoA, displacing the adenine moiety of ATP
holo-acyl carrier protein formation proceeds as follows. First, a prosthetic group precursor, presumably 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA, is formed from ATP and dephospho-CoA in a reaction catalyzed by CitG. Second, holo-ACP is formed from apo-ACP and the prosthetic group precursor in a reaction catalyzed by CitX. The conversion of apo-cyl carrier protein into holo-cyl carrier protein is achieved in vitro by incubation of apo-cyl carrier protein with proteins CitX, CitG, ATP, and dephospho-CoA. ATP cannot be substituted with GTP, CTP, UTP, ADP, or AMP. In the absence of CitG or dephospho-CoA, AMP-cyl carrier protein is formed. It is not possible to further convert AMP-cyl carrier protein to holo-cyl carrier protein by subsequent incubation with CitG and dephospho-CoA
accessory enzyme required for synthesis of an active citrate lyase complex, part of the operon encoding the citrate lyase complex, acid-inducible transcription of the operon encoding the citrate lysae complex