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Information on EC 2.7.7.65 - diguanylate cyclase and Organism(s) Caulobacter vibrioides and UniProt Accession Q9A5I5
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2.7.7.65 diguanylate cyclaseIUBMB Comments
A GGDEF-domain-containing protein that requires Mg2+ or Mn2+ for activity. The enzyme can be activated by BeF3, a phosphoryl mimic, which results in dimerization . Dimerization is required but is not sufficient for diguanylate-cyclase activity . Cyclic di-3',5'-guanylate is an intracellular signalling molecule that controls motility and adhesion in bacterial cells. It was first identified as having a positive allosteric effect on EC 2.4.1.12, cellulose synthase (UDP-forming) .
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Word Map
- 2.7.7.65
- phosphodiesterase
- cyclases
- aeruginosa
- monophosphate
- cyclic-di-gmp
- exopolysaccharide
-
flagellar
-
plankton
-
sessile
-
c-di-gmp-dependent
-
swarming
- caulobacter
- hd-gyp
-
i-site
- crescentus
-
diguanosine
-
c-di-gmp-mediated
-
per-arnt-sim
-
cyanobacteriochromes
- xylinum
-
ggdef-eal
- medicine
- molecular biology
- synthesis
- biotechnology
The taxonomic range for the selected organisms is: Caulobacter vibrioides
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
diguanylate cyclase, tlr0924, pa3177, vc0395_0300, pa0847, all2874, slr1143, xac0610, pgn_1932, pa4367, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PleD
DGC
PleD
PleD
response regulator with diguanylate cyclase (GGDEF) domain, Rec domain (D1) and Rec-like adaptor domain (D2)
SYSTEMATIC NAME
IUBMB Comments
GTP:GTP guanylyltransferase
A GGDEF-domain-containing protein that requires Mg2+ or Mn2+ for activity. The enzyme can be activated by BeF3, a phosphoryl mimic, which results in dimerization [3]. Dimerization is required but is not sufficient for diguanylate-cyclase activity [3]. Cyclic di-3',5'-guanylate is an intracellular signalling molecule that controls motility and adhesion in bacterial cells. It was first identified as having a positive allosteric effect on EC 2.4.1.12, cellulose synthase (UDP-forming) [1].
CAS REGISTRY NUMBER
COMMENTARY
146316-82-7
-
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
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
analyses by pyrophosphatase-coupled spectrophotometric assay
-
?
GTP + GTP
cyclic-di-3',5'-GMP + diphosphate + diphosphate
pH 7.8
reaction stop with 25 mM EDTA, pH 6, KD (cyclic-di-3,5-GMP): 0.3 microM or 0.4 microM (in presence of activator BeF3)
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The DgcP of Caulobacter crescentus binds dimeric c-di-GMP at an allosteric site I-site that is characterized by the RxxD motif. Binding of cyclic-di-GMP at the I-site accounts for a strong non-competitive product inhibition, which establishes a limit on the cellular c-di-GMP concentration
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
diguanylate cyclase activity constitutes the signaling output of the PleD response regulator
-
-
?
additional information
?
-
-
mode of GTPalphaS/Mg2+-binding suggests two-metal catalytic mechanism analogous to adenylate cyclases
-
-
?
additional information
?
-
mode of GTPalphaS/Mg2+-binding suggests two-metal catalytic mechanism analogous to adenylate cyclases
-
-
?
additional information
?
-
-
on-rates constants of substrate and product range between 100/sec and 300/sec
-
-
?
additional information
?
-
on-rates constants of substrate and product range between 100/sec and 300/sec
-
-
?
additional information
?
-
-
analysis of the DGC specificity, overview
-
-
-
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
GTP
cyclic di-3',5'-guanylate + diphosphate
-
diguanylate cyclase activity constitutes the signaling output of the PleD response regulator
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
or Mn2+, strictly required, with Mn2+ resulting in slightly higher activity than Mg2+
Mn2+
or Mg2+, strictly required, with Mn2+ resulting in slightly higher activity than Mg2+
additional information
additional information
PleD contains an extra metal binding site or beryllium metal for activation
additional information
-
PleD contains an extra metal binding site or beryllium metal for activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(5-amino-1,3,4-thiadiazol-2-yl)-N'-[(1E,2E)-3-(3-nitrophenyl)prop-2-en-1-ylidene]acetohydrazide
4% inhibition at 0.1 mM
3-(3,5-dioxo-2,3,4,5-tetrahydro-1,2,4-triazin-6-yl)-N'-[(E)-(4-nitrophenyl)methylidene]propanehydrazide
11.0% inhibition at 0.1 mM
3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
85% inhibition at 0.1 mM, competitive binding
cyclic di-3',5'-guanylate
noncompetitive product inhibition, binding causes crosslinking of diguanylate cyclase (GGDEF) domains within the dimer, integrity of only one inhibitory site required for inhibition
cyclic-di-3',5'-GMP
allosteric feedback, product inhibition, independent of activation status, binding induces change in conformation and protein-solvent interactions
N'-[(E)-(2-hydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
13% inhibition at 0.1 mM
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
83.4% inhibition at 0.1 mM, competitive binding
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
cyclic 3',5'-diguanylate
-
product inhibition is due to domain immobilization and sets an upper limit for the concentration of this second messenger in the cell
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
N'-[(E)-(2,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
6% inhibition at 0.1 mM
N'-[(E)-(2,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
17% inhibition at 0.1 mM
cyclic di-3',5'-guanylate
noncompetitive product inhibition at an allosteric binding site fully contained within the GGDEF domain. Core of the binding site is an RXXD motif formed by residues R359, D362, and R390
cyclic di-3',5'-guanylate
product inhibition, allosteric feedback regualtion is not affected by the activation state of enzyme
additional information
virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. The compounds retrieved from the pharmacophore searches are docked into the active site of PleD, by means of Molegro Virtual Docker (MVD) software (CLCbio), using the three-dimensional structure of PleD (PDB ID 2V0N). Binding of N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide to PleD is stabilized by polar interactions with residues surrounding the GTP binding pocket, namely, N335, D344, and R366. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide share a hydrazine moiety with the previously identified inhibitors LP3134 and LP4010, which has been predicted to interact with the amino group of N335
-
additional information
-
virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. The compounds retrieved from the pharmacophore searches are docked into the active site of PleD, by means of Molegro Virtual Docker (MVD) software (CLCbio), using the three-dimensional structure of PleD (PDB ID 2V0N). Binding of N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide to PleD is stabilized by polar interactions with residues surrounding the GTP binding pocket, namely, N335, D344, and R366. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide share a hydrazine moiety with the previously identified inhibitors LP3134 and LP4010, which has been predicted to interact with the amino group of N335
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-(5-[(E)-[2-(4-amino-1,2,5-oxadiazole-3-carbonyl)hydrazinylidene]methyl]furan-2-yl)benzoic acid
18% activation at 0.1 mM
4-chloro-N'-[(E)-(4-cyanophenyl)methylidene]-3-nitrobenzene-1-sulfonohydrazide
15% activation at 0.1 mM
4-[(E)-[2-(4-hydroxy-6-methylpyrimidin-2-yl)hydrazinylidene]methyl]phenyl 3-nitrobenzoate
8% activation at 0.1 mM
4-[(E)-[2-(4-sulfamoylphenyl)hydrazinylidene]methyl]benzoic acid
6% activation at 0.1 mM
N'-[(E)-(4-chloro-3-nitrophenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
3% activation at 0.1 mM
N'-[(E)-(4-cyanophenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
4% activation at 0.1 mM
beryllium fluoride
BeF3-, pseudo-phosphorylation, enhances dimerisation by lowering KD to less than 10 microM, tightens dimer interface between two D1/D2 domains, modification activates enzyme
beryllium fluoride
BeF3, phosphoryl mimic, optimum concentration: 1 mM BeCl2/10 mM NaF (nonspecifcally inhibitory at higher concentrations), causes dimerisation and cyclic di-3,5-guanylate synthesis, no influence on cyclic-di-GMP binding affinity and thus allosteric regulation
additional information
PleD contains an extra metal binding site or beryllium metal for activation
-
additional information
-
PleD contains an extra metal binding site or beryllium metal for activation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
cyclic di-3',5'-guanylate
triple mutant R148A/R178A/R313A
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00081
cyclic di-3',5'-guanylate
triple mutant R148A/R178A/R313A, inhibited
0.016
cyclic di-3',5'-guanylate
triple mutant R148A/R178A/R313A
additional information
cyclic di-3',5'-guanylate
-
double mutant R148A/R178A, inhibited, no activity detected
additional information
cyclic di-3',5'-guanylate
double mutant R148A/R178A, inhibited, no activity detected
additional information
cyclic di-3',5'-guanylate
-
mutant R313A, inhibited, no activity detected
additional information
cyclic di-3',5'-guanylate
mutant R313A, inhibited, no activity detected
additional information
cyclic di-3',5'-guanylate
-
wild-type, inhibited, no activity detected
additional information
cyclic di-3',5'-guanylate
wild-type, inhibited, no activity detected
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.033
cyclic di-3',5'-guanylate
triple mutant R148A/R178A/R313A
0.0029
cyclic di-3',5'-guanylate
mutant R148A/R178A, 30°C, pH 8.0
0.1
cyclic di-3',5'-guanylate
or above, mutant R359A, 30°C, pH 8.0
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01107
3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
Caulobacter vibrioides
pH 7.5, 22°C
0.01105
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
Caulobacter vibrioides
pH 7.5, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000036
mutant Y26A, in presence of BeF3 (1 mM BeCl2, 10 mM NaF)
0.0011
mutant D53N, in presence of BeF3 (1 mM BeCl2, 10 mM NaF)
0.00004
mutant Y26A in presence of beryllium trifluoride, pH 7.8
0.0011
mutant D53N in presence of beryllium trifluoride, pH 7.8
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
recruitment to predivisional pole during cell cycle of differentiating cells dependends on dimerisation
-
response regulator PleD-GFP protein specifically localizes to the stalked pole and is absent from the flagellated swarmer pole. Targeting of PleD to the cell pole is coupled to the activation of its C-terminal di-guanylate cyclase domain
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
metabolism
-
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
additional information
additional information
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
additional information
-
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
at high protein concentrations and/or presence of divalent metal ions (Mg2+, Mn2+), tightened upon BeF3-modification, exothermic dimerisation, KD: 100 microM, gel filtration chromatography and crystallography
dimer
enzymatically active state, concentration dependent, crosslinking (using disuccinimidyl suberate, DSS)
additional information
-
dimer is the catalytically active state of enzyme
additional information
dimer is the catalytically active state of enzyme
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
phosphoprotein
enzyme is activated by phosphorylation of residue D53. In vitro, enzyme PleD can be activated by beryllium fluoride, resulting in dimerization and synthesis of cyclic diguanylate
phosphoprotein
-
localization of response regulator PleD to the stalked pole requires its activation by phosphorylation and is dependent on the polar kinases DivJ and PleC
additional information
-
pseudo-phosphorylation by beryllium fluoride (BeF3-) modification at residue Asp53 in Rec-domain (D1), tightens dimer
additional information
pseudo-phosphorylation by beryllium fluoride (BeF3-) modification at residue Asp53 in Rec-domain (D1), tightens dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
BeF3-/Mg2+-modified PleD (100 microM) in presence of cyclic di-3,5-guanylate (0.2 mM) and substrate-analog GTPalphaS (1 mM), hanging-drop vapour-diffusion: equal volumes protein solution (10 mg/ml) and precipitant solution (0.1M HEPES pH 8, 0.73 M Na2SO4), crystals: needle shape, space group: P2(1)2(1)2(1), unit cell parameters: a: 128.9, b: 132.6, c: 88.4, resolved by molecular replacement using PDB: 1W25 as model, tightened dimer interface at the dyad symmetric stem between D1/D2 domains of the two monomers upon rotation of D2 relative to D1, restructured beta4alpha4 loop compared to nonactivated state, GTPalphaS bound to both diguanylate cyclase (GGDEF) domain active sites, 2fold symmetric crosslinking of GGDEF domains of the structural dimer in presence of cyclic di-3,5-guanylate, cyclic di-3,5-guanylate bound to allosteric (inhibitory) site similarly to nonactivated state
after activation by berillium trifluoride. Activation causes rearrangement of an adaptor domain which in turn promotes dimer formation. The substrate analogue GTPgammaS and two putative cations are bound to the active sites. Identification of a second cyclic diguanylate binding mode that crosslinks the diguanylate cyclase domains within a protein dimer and results in noncompetitive product inhibition
in complex with product cyclic diguanylate. The guanine base is H-bonded to N335 and D344, whereas the ribosyl and alpha-phosphate moieties extend over the beta2-beta3-hairpin that carries the GGEEF signature motif. In the crystal, cyclic diguanylate molecules are crosslinking active sites of adjacent dimers. In solution, two diguanylate cyclase doamins of a dimer may align in a twofold symmetric way to catalyze synthesis of cyclic diguanylate
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E370Q
mainly dimeric, inactive mutant of the guanylate cyclase domain GG(D/E)EF (Mg2+ coordination), no activation by BeF3 or protein concentration above 50 microM
R148A/R178A/R313A
triple mutant, KD for binding of cyclic di-3,5-guanylate: 4 microM (10fold higher than wild-type), 60fold increased KI for product inhibition by cyclic di-3,5-guanylate, residual catalytic activity
DELTAR359/DELTAD362
mutations in allosteric binding site of cyclic diguanylate, abolish cyclic diguanylate binding, strong decrease in catalytic activity
E370Q
mutation in active site, complete loss of catalytic activity without effect on allosteric binding of cyclic diguanylate
EE370GG
mutation in active site, complete loss of catalytic activity without effect on allosteric binding of cyclic diguanylate
R148A
increase in allosteric binding of cyclic diguanylate and increase in catalytic activity
R148A/R178A
increase in allosteric binding of cyclic diguanylate and increase in catalytic activity
R178A
increase in allosteric binding of cyclic diguanylate and increase in catalytic activity
R359A
mutation in allosteric binding site of cyclic diguanylate, strong decrease in cyclic diguanylate binding, strong decrease in catalytic activity
R390A
mutation in allosteric binding site of cyclic diguanylate, strong decrease in cyclic diguanylate binding. Catalytic activity comaprable to wild-type
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity decreases with increasing NaCl concentration and in presence of KCl (25 mM)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal affinity chromatography followed by dialysis and analytical or preparative size exclusion chromatography on Superdex 200 column
metal affinity chromatography (elution with 200 mM imidazole) followed by size-exclusion chromatography on Superdex 200 HR 26/60 column and analytical size-exclusion chromatography on Superdex 200 HR 10/30 column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
in pBR322 for inducible expression with C-terminal hexa-His-tag in Escherichia coli BL21(DE3)pLysS
expression as GFP fusion protein for subcellular targeting, expression with His-tag in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Paul, R.; Weiser, S.; Amiot, N.C.; Chan, C.; Schirmer, T.; Giese, B.; Jenal, U.
Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain
Genes Dev.
18
715-727
2004
Caulobacter vibrioides
Christen, B.; Christen, M.; Paul, R.; Schmid, F.; Folcher, M.; Jenoe, P.; Meuwly, M.; Jenal, U.
Allosteric control of cyclic di-GMP signaling
J. Biol. Chem.
281
32015-32024
2006
Caulobacter vibrioides (Q9A3B9)
Paul, R.; Abel, S.; Wassmann, P.; Beck, A.; Heerklotz, H.; Jenal, U.
Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization
J. Biol. Chem.
282
29170-29177
2007
Caulobacter vibrioides, Caulobacter vibrioides (Q9A5I5)
Chan, C.; Paul, R.; Samoray, D.; Amiot, N.C.; Giese, B.; Jenal, U.; Schirmer, T.
Structural basis of activity and allosteric control of diguanylate cyclase
Proc. Natl. Acad. Sci. USA
101
17084-17089
2004
Caulobacter vibrioides
Wassmann, P.; Chan, C.; Paul, R.; Beck, A.; Heerklotz, H.; Jenal, U.; Schirmer, T.
Structure of BeF3--modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition
Structure
15
915-927
2007
Caulobacter vibrioides, Caulobacter vibrioides (Q9A5I5)
Dahlstrom, K.M.; O'Toole, G.A.
A symphony of cyclases specificity in diguanylate cyclase signaling
Annu. Rev. Microbiol.
71
179-195
2017
Caulobacter vibrioides, Clostridioides difficile, Pseudomonas aeruginosa, Burkholderia cenocepacia, Vibrio cholerae serotype O1, Komagataeibacter xylinus (O87374), Escherichia coli (P0AA89), Vibrio cholerae serotype O1 A1552
Cho, K.H.; Tryon, R.G.; Kim, J.H.
Screening for diguanylate cyclase (DGC) inhibitors mitigating bacterial biofilm formation
Front. Chem.
8
264
2020
Caulobacter vibrioides (A0A0H3CCZ8), Caulobacter vibrioides (B8GZM2), Caulobacter vibrioides CB15N (A0A0H3CCZ8), Caulobacter vibrioides NA1000 (A0A0H3CCZ8), Caulobacter vibrioides NA1000 (B8GZM2), Clostridioides difficile (A0A170Y3L9), Komagataeibacter xylinus (O87374), Pseudomonas aeruginosa (Q9HT84), Pseudomonas aeruginosa (Q9HXT9), Pseudomonas aeruginosa 1C (Q9HT84), Pseudomonas aeruginosa 1C (Q9HXT9), Pseudomonas aeruginosa ATCC 15692 (Q9HT84), Pseudomonas aeruginosa ATCC 15692 (Q9HXT9), Pseudomonas aeruginosa CIP 104116 (Q9HT84), Pseudomonas aeruginosa CIP 104116 (Q9HXT9), Pseudomonas aeruginosa DSM 22644 (Q9HT84), Pseudomonas aeruginosa DSM 22644 (Q9HXT9), Pseudomonas aeruginosa JCM 14847 (Q9HT84), Pseudomonas aeruginosa JCM 14847 (Q9HXT9), Pseudomonas aeruginosa LMG 12228 (Q9HT84), Pseudomonas aeruginosa LMG 12228 (Q9HXT9), Pseudomonas aeruginosa PRS 101 (Q9HT84), Pseudomonas aeruginosa PRS 101 (Q9HXT9), Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZNT5), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (Q8ZNT5), Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (Q8ZNT5), Synechocystis sp. PCC 6803 (P73272), Vibrio cholerae serotype O1 (Q9KKZ4), Vibrio cholerae serotype O1 ATCC 39315 (Q9KKZ4), Vibrio cholerae serotype O1 El Tor Inaba N16961 (Q9KKZ4)
Fernicola, S.; Paiardini, A.; Giardina, G.; Rampioni, G.; Leoni, L.; Cutruzzolxa0, F.; Rinaldo, S.
In silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD
J. Bacteriol.
198
147-156
2016
Caulobacter vibrioides (Q9A5I5), Caulobacter vibrioides, Caulobacter vibrioides ATCC 19089 (Q9A5I5), Caulobacter vibrioides CB15 (Q9A5I5), Pseudomonas aeruginosa (A0A0C7ADU5), Pseudomonas aeruginosa (Q9HXT9), Pseudomonas aeruginosa 1C (Q9HXT9), Pseudomonas aeruginosa ATCC 15692 (Q9HXT9), Pseudomonas aeruginosa CIP 104116 (Q9HXT9), Pseudomonas aeruginosa DSM 22644 (Q9HXT9), Pseudomonas aeruginosa JCM 14847 (Q9HXT9), Pseudomonas aeruginosa LMG 12228 (Q9HXT9), Pseudomonas aeruginosa PRS 101 (Q9HXT9)
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Transporter Classification Database (TCDB): 9.B.34.1.4, 9.B.34.1.2
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