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Literature summary for 2.7.7.65 extracted from

  • Oliveira, M.C.; Teixeira, R.D.; Andrade, M.O.; Pinheiro, G.M.; Ramos, C.H.; Farah, C.S.
    Cooperative substrate binding by a diguanylate cyclase (2015), J. Mol. Biol., 427, 415-432.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K759A mutagenesis of a conserved lysine residue, results in a severe reduction in dihuanylate cyclase activity, kcat value is almost 100fold lower than that of the wild-type protein while the K1 and K2 values do not change very much Xanthomonas citri pv. citri

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibitory: cyclic di-GMP Xanthomonas citri pv. citri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.038
-
GTP mutant K759A, Michaelis-Menten model, pH 8.0, 30°C Xanthomonas citri pv. citri
0.061
-
GTP Michaelis-Menten model, pH 8.0, 30°C Xanthomonas citri pv. citri

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ or Mn2+, strictly required Xanthomonas citri pv. citri
Mn2+ or Mg2+, strictly required Xanthomonas citri pv. citri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
94500
-
-
Xanthomonas citri pv. citri
360000
-
gel filtration Xanthomonas citri pv. citri

Organism

Organism UniProt Comment Textmining
Xanthomonas citri pv. citri Q8PPS5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 GTP
-
Xanthomonas citri pv. citri 2 diphosphate + cyclic di-3',5'-guanylate
-
?
additional information sequential random binding model of two identical substrates binding to two equivalent GGDEF domains that come together to form a symmetrical active site Xanthomonas citri pv. citri ?
-
?

Subunits

Subunits Comment Organism
More at micromolar concentrations, the protein exists predominantly as a dimeric species Xanthomonas citri pv. citri
multimer x * 94500, calculated Xanthomonas citri pv. citri

Synonyms

Synonyms Comment Organism
XAC0610
-
Xanthomonas citri pv. citri

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.014
-
GTP mutant K759A, Michaelis-Menten model, pH 8.0, 30°C Xanthomonas citri pv. citri
1.2
-
GTP wild-type, Michaelis-Menten model, pH 8.0, 30°C Xanthomonas citri pv. citri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.5
-
Xanthomonas citri pv. citri

General Information

General Information Comment Organism
physiological function protein has in vivo and in vitro diguanylate cyclase activity that leads to the production of cyclic di-GMP. Protein XAC0610 plays a role in the regulation of Xanthomonas citri motility and resistance to H2O2. XAC0610 is not subject to allosteric product inhibition. Instead, steady-state kinetics reveal a positive cooperative effect of the GTP substrate with a dissociation constant for the binding of the first GTP molecule (K1) approximately 5 times greater than the dissociation constant for the binding of the second GTP molecule (K2). The N-terminal GAF and PAS domains are required for high levels of XAC0610 diguanylate cyclase activity Xanthomonas citri pv. citri