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

BRENDA support

Literature summary for 2.7.7.65 extracted from

  • Wan, X.; Saito, J.; Newhouse, J.; Hou, S.; Alam, M.
    The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases (2017), PLoS ONE, 12, e0182782 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.65

Cloned(Commentary)

Cloned (Comment) Organism
gene BP3507, recombinant expression of His6-tagged wild-type enzyme and truncated mutants BpeGReg155, BpeGReg266, and BpeGReg296 in Escherichia coli strain TOP10, recombinant expression of BpeGReg point mutants in Salmonella typhimurium strain ATCC 14028 Bordetella pertussis
gene dosC, recombinant expression in Escherichia coli strain TOP10, recombinant expression of EcGReg point mutants in Salmonella typhimurium strain ATCC 14028 Escherichia coli

Protein Variants

Protein Variants Comment Organism
A68T site-directed mutagenesis, the mutant cell motility and biofilm formation are partially inhibited Escherichia coli
D333A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
D342A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
D350A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
D368A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
D368K site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
D376A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
E377A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
F337A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
F378A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
F42A site-directed mutagenesis Escherichia coli
F42A site-directed mutagenesis Bordetella pertussis
G374A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
G375A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
H223A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
K224A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
K226A site-directed mutagenesis, biofilm formation of the mutant is inhibited Bordetella pertussis
K338A site-directed mutagenesis, the mutant cell motility and biofilm formation are partially inhibited Escherichia coli
L300A site-directed mutagenesis, the mutant biofilm formation is partially inhibited Escherichia coli
L300D site-directed mutagenesis, the mutant cell motility is inhibited, biofilm formation of the mutant is inhibited Escherichia coli
L353A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
L353D site-directed mutagenesis, the mutant cell motility is inhibited, and biofilm formation of the mutant is inhibited Escherichia coli
M69A site-directed mutagenesis Escherichia coli
M69A site-directed mutagenesis Bordetella pertussis
additional information generation of truncated enzyme mutants BpeGReg1-155, BpeGReg1-266, BpeGReg1-296, BpeGReg156-475, BpeGReg267-475, and BpeGReg297-475 Bordetella pertussis
N341A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
R306A site-directed mutagenesis, biofilm formation of the mutant is inhibited Escherichia coli
R372A site-directed mutagenesis, the mutant cell motility is inhibited, and biofilm formation of the mutant is inhibited Escherichia coli
S68A site-directed mutagenesis, biofilm formation of the mutant is inhibited Bordetella pertussis
Y43A site-directed mutagenesis Escherichia coli
Y43A site-directed mutagenesis, biofilm formation of the mutant is partially inhibited, and cell motility is inhibited Bordetella pertussis

Metals/Ions

Metals/Ions Comment Organism Structure
additional information in the EcGReg globin domain, the distal residue Tyr43 stabilizes O2 to ferrous ion Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 GTP Escherichia coli
-
 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP Bordetella pertussis
-
 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP Bordetella pertussis Tohama I
-
 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP Bordetella pertussis ATCC BAA-589
-
 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP Bordetella pertussis NCTC 13251
-
 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?

Organism

Organism UniProt Comment Textmining
Bordetella pertussis Q7VTL8
-
-
Bordetella pertussis ATCC BAA-589 Q7VTL8
-
-
Bordetella pertussis NCTC 13251 Q7VTL8
-
-
Bordetella pertussis Tohama I Q7VTL8
-
-
Escherichia coli P0AA89
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged wild-type enzyme and truncated mutants BpeGReg155, BpeGReg266, and BpeGReg296 from Escherichia coli strain TOP10 by cobalt affinity chromatography Bordetella pertussis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 GTP
-
 Escherichia coli 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP
-
 Bordetella pertussis 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP
-
 Bordetella pertussis Tohama I 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP
-
 Bordetella pertussis ATCC BAA-589 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?
2 GTP
-
 Bordetella pertussis NCTC 13251 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?

Synonyms

Synonyms Comment Organism
BP3507
-
 Bordetella pertussis
Bpe-GReg
-
 Bordetella pertussis
dgcO
-
 Escherichia coli
DosC
-
 Escherichia coli
DosC
-
 Bordetella pertussis
EcGReg
-
 Escherichia coli
GCDC
-
 Escherichia coli
GCDC
-
 Bordetella pertussis
globin-coupled diguanylate cyclase
-
 Escherichia coli
globin-coupled diguanylate cyclase
-
 Bordetella pertussis
heme-based globin-coupled diguanylate cyclase
-
 Escherichia coli
heme-based globin-coupled diguanylate cyclase
-
 Bordetella pertussis
YddV
-
 Escherichia coli

General Information

General Information Comment Organism
malfunction BpeGReg266 (residues 1-266) and BpeGReg296 (residues 1-296), which only contain the globin and middle domains, can inhibit bacterial motility. The distal residues of the globin domain affect diguanylate cyclase activity, Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams Bordetella pertussis
additional information the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ala68, and Met69 are required to maintain full diguanylate cyclase activity. The highly conserved amino acids His223 and Lys224 in the middle domain of EcGReg are essential to diguanylate cyclase activity. Sixteen important residues (Leu300, Arg306, Asp333, Phe337, Lys338, Asn341, Asp342, Asp350, Leu353, Asp368, Arg372, Gly374, Gly375, Asp376, Glu377, and Phe378) are identified in the active site and inhibitory site of the diguanylate cyclase domain of EcGReg Escherichia coli
additional information the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ser68, and Met69 are required to maintain full diguanylatecyclase activity. The highly conserved amino acids His225 and Lys226 in the middle domain of BpeGReg are essential to diguanylate cyclase activity. Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams Bordetella pertussis