Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

6.3.2.5: phosphopantothenate-cysteine ligase (CTP)

This is an abbreviated version!
For detailed information about phosphopantothenate-cysteine ligase (CTP), go to the full flat file.

Reaction

CTP
+
(R)-4'-phosphopantothenate
+
L-cysteine
=
CMP
+
diphosphate
+
N-[(R)-4'-phosphopantothenoyl]-L-cysteine

Synonyms

4’-phosphopantothenoylcysteine synthetase, CoaB, CoaBC, coupling enzyme, Dfp, pantothenate 4´-phosphate:L-cysteine ligase, phosphopantothenate-cysteine ligase, phosphopantothenoyl-cysteine ligase, phosphopantothenoylcysteine synthetase, PPC synthase, PPC synthetase, PPC-S, PPCS, synthetase, phosphopantothenoylcysteine

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.2 Acid—amino-acid ligases (peptide synthases)
                6.3.2.5 phosphopantothenate-cysteine ligase (CTP)

Engineering

Engineering on EC 6.3.2.5 - phosphopantothenate-cysteine ligase (CTP)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A275T
-
temperature sensitive mutant dfp-1
A275V
-
unable to form dimers
D203N
-
unable to form dimers
K289Q
-
complete loss of enzymic activity
N210D
-
complete loss of enzymic activity, but intermediate 4Â’-phosphopanthotenoyl-CMP is formed
N210H
-
used for isolation of reaction intermediate
N210K
-
used for isolation of reaction intermediate
T194V
-
unable to form dimers
T198V
-
unable to form dimers
K310Q
N217H
K310Q
N217H
additional information
-
mutation in dPPCS impair female fecundity and fertility, and disrupts the organization of the somatic and germ line cells, affects F-actin organization and results in abnormal PtdIns(4,5)P2 localization. Improper cell organization coincides with aberrant localization of the membrane molecules Gurken (Grk) and Notch, whose activities are required for specification of the follicle cells that pattern the eggshell. Mutations in dPPCS also induce alterations in scutellar patterning and cause wing vein abnormalities, phenotype, detailed overview