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Literature summary extracted from

  • Barends, T.R.; Hartmann, E.; Griese, J.J.; Beitlich, T.; Kirienko, N.V.; Ryjenkov, D.A.; Reinstein, J.; Shoeman, R.L.; Gomelsky, M.; Schlichting, I.
    Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase (2009), Nature, 459, 1015-1018.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.52
-
 Klebsiella pneumoniae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.4.52 BlrP1 is crystallized at 4°C in the dark using polyethyleneglycol in the presence of cyclic-di-GMP and Ca2+ Klebsiella pneumoniae

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.52 L128C/G353C the mutant shows higher catalytic efficiency at pH 7.5 and 20°C compared to the wild type enzyme under light and dark conditions Klebsiella pneumoniae
3.1.4.52 R93S the mutant shows higher catalytic efficiency at pH 7.5 and 20°C compared to the wild type enzyme under light and dark conditions Klebsiella pneumoniae
3.1.4.52 S309C/S312C inactive at pH 7.5 and 20°C under dark and light conditions Klebsiella pneumoniae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.4.52 Ca2+ complete inhibition at 10 mM Klebsiella pneumoniae
3.1.4.52 Cu2+ complete inhibition at 10 mM Klebsiella pneumoniae
3.1.4.52 Zn2+ complete inhibition at 10 mM Klebsiella pneumoniae

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.52 Klebsiella pneumoniae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.4.52
-
 Klebsiella pneumoniae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.52 cyclic di-3',5'-guanylate + H2O
-
 Klebsiella pneumoniae 5'-phosphoguanylyl(3'-5')guanosine
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.4.52 dimer
-
 Klebsiella pneumoniae

Synonyms

EC Number Synonyms Comment Organism
3.1.4.52 BlrP1 also known as KPN 01598, BlrP1 consists of a BLUF sensor domain and a phosphodiesterase EAL output domain which hydrolyses cyclic dimeric GMP, so BlrP1 possesses c-di-GMP-phosphodiesterase activity Klebsiella pneumoniae
3.1.4.52 cyclic nucleotide phosphodiesterase
-
 Klebsiella pneumoniae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.4.52 0.13
-
 cyclic di-3',5'-guanylate wild type enzyme, at pH 7.5, 20°C, under dark conditions Klebsiella pneumoniae
3.1.4.52 0.27
-
 cyclic di-3',5'-guanylate mutant enzyme R93S, at pH 7.5, 20°C, under dark conditions Klebsiella pneumoniae
3.1.4.52 0.54
-
 cyclic di-3',5'-guanylate wild type enzyme, at pH 7.5, 20°C, under light conditions Klebsiella pneumoniae
3.1.4.52 0.64
-
 cyclic di-3',5'-guanylate wild type enzyme, in the presence of 10 mM Mn2+, at pH 7.5, 20°C, under dark conditions Klebsiella pneumoniae
3.1.4.52 1.17
-
 cyclic di-3',5'-guanylate wild type enzyme, in the presence of 10 mM Mn2+, at pH 7.5, 20°C, under light conditions Klebsiella pneumoniae
3.1.4.52 1.42
-
 cyclic di-3',5'-guanylate mutant enzyme R93S, at pH 7.5, 20°C, under light conditions Klebsiella pneumoniae
3.1.4.52 1.84
-
 cyclic di-3',5'-guanylate wild type enzyme, at pH 8.0, 20°C, under dark conditions Klebsiella pneumoniae
3.1.4.52 2.06
-
 cyclic di-3',5'-guanylate mutant enzyme L128C/G353C, at pH 7.5, 20°C, under dark conditions Klebsiella pneumoniae
3.1.4.52 2.54
-
 cyclic di-3',5'-guanylate wild type enzyme, at pH 8.0, 20°C, under light conditions Klebsiella pneumoniae
3.1.4.52 3.48
-
 cyclic di-3',5'-guanylate mutant enzyme L128C/G353C, at pH 7.5, 20°C, under light conditions Klebsiella pneumoniae
3.1.4.52 6.17
-
 cyclic di-3',5'-guanylate wild type enzyme, at pH 9.3, 20°C, under light conditions Klebsiella pneumoniae
3.1.4.52 6.7
-
 cyclic di-3',5'-guanylate wild type enzyme, at pH 9.3, 20°C, under dark conditions Klebsiella pneumoniae

Cofactor

EC Number Cofactor Comment Organism Structure
3.1.4.52 Calmodulin
-
 Klebsiella pneumoniae