Information on EC 4.6.1.6 - cytidylate cyclase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
4.6.1.6
-
RECOMMENDED NAME
GeneOntology No.
cytidylate cyclase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
CTP = 3',5'-cyclic CMP + diphosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
P-O bond cleavage
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
CTP diphosphate-lyase (cyclizing; 3',5'-cyclic-CMP-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3',5'-cyclic-CMP synthase
-
-
-
-
CyaA
-
also possesses cytidylyl cyclase activity
cytidyl cyclase
-
-
-
-
cytidylyl cyclase
-
-
-
-
Edema factor
-
also possesses cytidylyl cyclase activity
CAS REGISTRY NUMBER
COMMENTARY
65357-82-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
mouse, strain BAGG-Swiss
-
-
Manually annotated by BRENDA team
rat; strain Lister Hooded
-
-
Manually annotated by BRENDA team
rat; strain Wistar
-
-
Manually annotated by BRENDA team
Rattus norvegicus Lister Hooded
strain Lister Hooded
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
strain Wistar
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP
3',5'-cyclic CMP + diphosphate
show the reaction diagram
-
-
-
-
?
CTP
3',5'-cyclic CMP + diphosphate
show the reaction diagram
-
-
-
-
?
CTP
3',5'-cyclic CMP + diphosphate
show the reaction diagram
-
-
-
-
?
CTP
3',5'-cyclic CMP + diphosphate
show the reaction diagram
-
cCMP biosynthesis
-
-
?
CTP
3',5'-cyclic CMP + diphosphate
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
?
CTP
3',5'-cyclic CMP + diphosphate
show the reaction diagram
Rattus norvegicus Lister Hooded
-
-
-
-
?
additional information
?
-
-
distinct from purine nucleotide cyclases, adenylate cyclase and guanylate cyclase
-
-
-
additional information
?
-
-
cyclic CMP is the major product, beside this cytidine 3',5'-cyclic diphosphate, cytidine 2'-monophosphate 3',5'cyclic monophosphate, 2'-O-glutamyl cytidine 3',5'-cyclic monophosphate, and 2'-O-aspartyl cytidine 3',5'-cyclic monophosphate are found
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CTP
3',5'-cyclic CMP + diphosphate
show the reaction diagram
-
-
-
-
?
CTP
3',5'-cyclic CMP + diphosphate
show the reaction diagram
-
-
-
-
?
CTP
3',5'-cyclic CMP + diphosphate
show the reaction diagram
-
cCMP biosynthesis
-
-
?
CTP
3',5'-cyclic CMP + diphosphate
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
?
CTP
3',5'-cyclic CMP + diphosphate
show the reaction diagram
Rattus norvegicus Lister Hooded
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
-
cyclic CMP formation is enhanced by 0.3 mM
Mg2+
-
complete loss of activity in absence of Mg2+ or Mn2+
Mg2+
-
required
Mn2+
-
cyclic CMP formation is enhanced by 0.3 mM
Mn2+
-
required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9-[2-(phosphonomethoxy)ethyl]adenine diphosphate
-
-
ATP
-
enzyme dispersed from the membrane fraction of brain
deoxycholate
-
-
L-alpha-Phosphatidic acid
-
-
L-alpha-Phosphatidylethanolamine
-
-
L-alpha-Phosphatidylserine
-
-
Mn2+
-
above 3 mM
additional information
-
enzymatic reaction is inhibited by boiling or detergents
-
additional information
-
no inhibition with L-alpha-phosphatidylcholine
-
additional information
-
enzyme dispersed from the membrane fraction of brain is not inhibited by GTP, also forskolin and lanthanum chloride shows no effect
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Guanine nucleotide-binding protein
-
stimulation of cytidylate cyclase activity via activation of a guanine nucleotide-binding protein
-
L-alpha-phosphatidylcholine
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0125
-
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.0156
-
CTP
-
-
0.0686
-
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.16
-
CTP
-
pH 7.4, 37C
0.22
-
CTP
-
pH 7.4, 37C
0.4197
-
CTP
-
in the presence of 5 mM Mg2+, in 75 mM HEPES-NaOH, pH 7.4, at 37C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.3
-
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37C
7.2
-
CTP
-
in the presence of 5 mM Mg2+, in 75 mM HEPES-NaOH, pH 7.4, at 37C
8.8
-
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.37
-
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37C
8829
17.2
-
CTP
-
in the presence of 5 mM Mg2+, in 75 mM HEPES-NaOH, pH 7.4, at 37C
8829
704
-
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37C
8829
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0000011
-
9-[2-(phosphonomethoxy)ethyl]adenine diphosphate
-
in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.0000045
-
9-[2-(phosphonomethoxy)ethyl]adenine diphosphate
-
in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.00058
-
methylanthraniloyl-ATP
-
in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.0044
-
methylanthraniloyl-ATP
-
in 75 mM HEPES-NaOH, pH 7.4,at 37C
0.00008
-
methylanthraniloyl-CTP
-
in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.0013
-
methylanthraniloyl-CTP
-
in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.0028
-
methylanthraniloyl-GTP
-
in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.0061
-
methylanthraniloyl-GTP
-
in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.001
-
methylanthraniloyl-ITP
-
in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.0057
-
methylanthraniloyl-ITP
-
in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.0018
-
methylanthraniloyl-UTP
-
in 75 mM HEPES-NaOH, pH 7.4, at 37C
0.0038
-
methylanthraniloyl-UTP
-
in 75 mM HEPES-NaOH, pH 7.4, at 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0012
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
-
7.5
-
-
liver enzyme
9.4
-
-
enzyme dispersed from the membrane fraction of brain
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
9.5
-
about 35% of activity maximum at pH 5.5, about 55% of activity maximum at pH 9.5
6
8.5
-
-
7.4
9.4
-
20% of activity maximum at physiological pH 7.4, maximal activity at pH 9.4, enzyme dispersed from the membrane fraction of brain
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
45
-
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Rattus norvegicus Lister Hooded, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Lister Hooded
-
;
-
Manually annotated by BRENDA team
Rattus norvegicus Lister Hooded
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Lister Hooded
-
;
-
Manually annotated by BRENDA team
Rattus norvegicus Lister Hooded
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Lister Hooded
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Rattus norvegicus Lister Hooded
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
membrane-bound
-
Manually annotated by BRENDA team