Information on EC 2.7.7.61 - citrate lyase holo-[acyl-carrier protein] synthase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
2.7.7.61
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RECOMMENDED NAME
GeneOntology No.
citrate lyase holo-[acyl-carrier protein] synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2'-(5-triphosphoribosyl)-3'-dephospho-CoA + citrate lyase apo-[acyl-carrier protein] = citrate lyase holo-[acyl-carrier protein] + diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenylyl group transfer
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nucleotidyl group transfer
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transfer of phosphoribosyl-dephospho-CoA
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
citrate lyase activation
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SYSTEMATIC NAME
IUBMB Comments
2'-(5-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate-lyase 2'-(5-phosphoribosyl)-3'-dephospho-CoA-transferase
The gamma-subunit of EC 4.1.3.6, citrate (pro-3S) lyase, serves as an acyl-carrier protein (ACP) and contains the prosthetic group 2'-(5-triphosphoribosyl)-3'-dephospho-CoA [1,3]. Synthesis and attachment of the prosthetic group requires the concerted action of this enzyme and EC 2.4.2.52, triphosphoribosyl-dephospho-CoA synthase [1]. In the enzyme from Escherichia coli, the prosthetic group is attached to serine-14 of the ACP via a phosphodiester bond.
CAS REGISTRY NUMBER
COMMENTARY hide
312492-44-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
biovar diacetylactis CRL264
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-(5''-triphosphoribosyl)-3'-dephospho-CoA + apo-citrate lyase
holo-citrate lyase + diphosphate
show the reaction diagram
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?
apo-ACP + ATP
AMP-ACP + diphosphate
show the reaction diagram
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side activity of the CitX in absence of its natural substrates, besides ATP, CTP, GTP, and UTP serve as nucleotidyl donors in vitro, ACP: acyl carrier protein, gamma-subunit of the citrate lyase
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?
additional information
?
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no substrate in vitro: NAD+
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2'-(5''-triphosphoribosyl)-3'-dephospho-CoA + apo-citrate lyase
holo-citrate lyase + diphosphate
show the reaction diagram
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20100
calculated from the amino acids number
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 20300, SDS-PAGE, autoradiography
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-DE3
Show AA Sequence (697 entries)
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