EC 6 - Ligases
EC 6.3 - Forming carbon-nitrogen bonds
EC 6.3.2 - Acid—amino-acid ligases (peptide synthases)
EC 6.3.2.5 - Phosphopantothenate—cysteine ligase (CTP)
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 6.3.2.5
Names
Accepted name:
phosphopantothenate—cysteine ligase (CTP)
Other
names:
phosphopantothenoylcysteine synthetase
[ambiguous]
phosphopantothenate—cysteine ligase [ambiguous]
phosphopantothenate—cysteine ligase [ambiguous]
Systematic name:
(R)-4'-phosphopantothenate:L-cysteine ligase
Reaction
- CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
Comments:
A key enzyme in the production of coenzyme A. The bacterial enzyme requires CTP, in contrast to the eukaryotic enzyme, EC 6.3.2.51, which requires ATP. Cysteine can be replaced by some of its derivatives.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
UniPathway
Gene Ontology:
GO:0004632
CAS Registry Number:
9023-50-1
References
-
The metabolism of pantothenic acid.J. Biol. Chem. 234 : 370-378 (1959). [PMID: 13630913]
-
Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified Coenzyme A biosynthetic enzymes in bacteria.J. Biol. Chem. 276 : 13513-13516 (2001). [PMID: 11278255]
-
Molecular characterization of the 4'-phosphopantothenoylcysteine synthetase domain of bacterial Dfp flavoproteins.J. Biol. Chem. 277 : 36137-36145 (2002). [PMID: 12140293]
-
Structural basis of CTP-dependent peptide bond formation in coenzyme A biosynthesis catalyzed by Escherichia coli PPC synthetase.Structure 12 : 1977-1988 (2004). [PMID: 15530362]
[EC 6.3.2.5 created 1961, modified 2003, modified 2017]