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Information on EC 4.6.1.6 - cytidylate cyclase
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4.6.1.6 cytidylate cyclaseIUBMB Comments
In bacteria and archaea the enzyme's product, cCMP, functions as a second messenger in bacterial immunity against viruses. The enzyme is synthesized following phage infection and activates immune effectors that execute an antiviral response.
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Word Map
- 4.6.1.6
- cytidine
- 5'-triphosphate
- gtp
-
3',5'-monophosphate
- triton
- pyrophosphate
-
immunoassay
-
ignarro
-
radiometric
- detergent
-
bombardment
- toxin
- adenylate
The enzyme appears in viruses and cellular organisms
Synonyms
cytidylate cyclase, cytidylyl cyclase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3',5'-cyclic-CMP synthase
-
-
-
-
cytidyl cyclase
-
-
-
-
cytidylyl cyclase
cytidylyl cyclase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP = 3',5'-cyclic CMP + diphosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P-O bond cleavage
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
CTP diphosphate-lyase (cyclizing; 3',5'-cyclic-CMP-forming)
In bacteria and archaea the enzyme's product, cCMP, functions as a second messenger in bacterial immunity against viruses. The enzyme is synthesized following phage infection and activates immune effectors that execute an antiviral response.
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CAS REGISTRY NUMBER
COMMENTARY
65357-82-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP
3',5'-cyclic CMP + diphosphate
-
-
-
-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP
3',5'-cyclic CMP + diphosphate
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzymatic reaction is inhibited by boiling or detergents
-
additional information
-
enzyme dispersed from the membrane fraction of brain is not inhibited by GTP, also forskolin and lanthanum chloride shows no effect
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Guanine nucleotide-binding protein
-
stimulation of cytidylate cyclase activity via activation of a guanine nucleotide-binding protein
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cholera
Cytidylate cyclase activity is stimulated via activation of a guanine nucleotide-binding protein.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0125
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37°C
0.0686
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37°C
0.4197
CTP
-
in the presence of 5 mM Mg2+, in 75 mM HEPES-NaOH, pH 7.4, at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37°C
7.2
CTP
-
in the presence of 5 mM Mg2+, in 75 mM HEPES-NaOH, pH 7.4, at 37°C
8.8
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.37
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37°C
17.2
CTP
-
in the presence of 5 mM Mg2+, in 75 mM HEPES-NaOH, pH 7.4, at 37°C
704
CTP
-
in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000011
9-[2-(phosphonomethoxy)ethyl]adenine diphosphate
-
in 75 mM HEPES-NaOH, pH 7.4, at 37°C
0.0000011
9-[2-(phosphonomethoxy)ethyl]adenine diphosphate
-
in 75 mM HEPES-NaOH, pH 7.4, at 37°C
0.0000045
9-[2-(phosphonomethoxy)ethyl]adenine diphosphate
-
in 75 mM HEPES-NaOH, pH 7.4, at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9.5
-
about 35% of activity maximum at pH 5.5, about 55% of activity maximum at pH 9.5
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q88CF9_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
951
0
108384
TrEMBL
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cech, S.Y.; Ignarro, L.J.
Cytidine 3,5-monophosphate (cyclic CMP) formation by homogenates of mouse liver
Biochem. Biophys. Res. Commun.
80
119-125
1978
Mus musculus
brenda
Newton, R.P.; Salih, S.A.G.; Hakeem, N.A.; Kingston, E.E.; Beynon, J.H.
3',5'-cyclic UMP, -cyclic IMP, -cyclic TMP and related enzymes in mammalian tissue
Biochem. Soc. Trans.
13
1134-1135
1985
Rattus norvegicus, Rattus norvegicus Lister Hooded
-
brenda
Newton, R.P.; Kingston, E.E.; Hakeem, N.A.; Salih, S'A.G.; Beynon, J.H.; Moyse, C.D.
Extraction, purification, identification and metabolism of 3',5'-cyclic UMP, 3',5'-cyclic IMP, and 3',5'-cyclic dTMP from rat tissues
Biochem. J.
236
431-439
1986
Rattus norvegicus
brenda
Newton, R.P.; Kingston, E.E.; Salvage, B.J.; Beynon, J.H.; Hakeem, N.A.; Wassenaar, T.
Identification of the products of putative cytidylate cyclase activity
Biochem. Soc. Trans.
14
964-965
1986
Rattus norvegicus
-
brenda
Mori, S.; Muto, N.; Yamamoto, I.
Interaction of rat brain cytidylate cyclase with phospholipids
Biochem. Biophys. Res. Commun.
162
1502-1507
1989
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Mori, S.; Yanagida, M.; Kubotsu, K.; Yamamoto, I.
Characterization of detergent dispersed cytidylate cyclase of rat brain
Second Messengers Phosphoproteins
13
1-12
1990
Rattus norvegicus
brenda
Newton, R.P.; Salvage, B.J.; Hakeem, N.A.
Cytidylate cyclase: development of assay and determination of kinetic properties of a cytidine 3,5-cyclic monophosphate-synthesizing enzyme
Biochem. J.
265
581-586
1990
Rattus norvegicus
brenda
Muto, N.; Kanoh, M.; Yamamoto, I.
Cytidylate cyclase activity is stimulated via activation of a guanine nucleotide-binding protein
Life Sci.
52
13-20
1993
Rattus norvegicus
brenda
Newton, R.P.; Groot, N.; van Geyschem, J.; Diffley, P.E.; Walton, T.J.; Bayliss, M.A.; Harris, F.M.; Games, D.E.; Brenton, A.G.
Estimation of cytidylyl cyclase activity and monitoring of side-product formation by fast-atom bombardment mass spectrometry
Rapid Commun. Mass. Spectrom.
11
189-194
1997
Rattus norvegicus, Rattus norvegicus Lister Hooded
brenda
Goettle, M.; Dove, S.; Kees, F.; Schlossmann, J.; Geduhn, J.; Koenig, B.; Shen, Y.; Tang, W.J.; Kaever, V.; Seifert, R.
Cytidylyl and uridylyl cyclase activity of Bacillus anthracis edema factor and Bordetella pertussis CyaA
Biochemistry
49
5494-5503
2010
Bacillus anthracis, Bordetella pertussis
brenda
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