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

BRENDA support

Literature summary extracted from

  • Tang, Q.; Luo, Y.; Zheng, C.; Yin, K.; Ali, M.; Li, X.; He, J.
    Functional analysis of a c-di-AMP-specific phosphodiesterase MsPDE from Mycobacterium smegmatis (2015), Int. J. Biol. Sci., 11, 813-824 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.59 D134a/H135A/H136A mutation in DHH domain, complete loss of catalytic activity Mycolicibacterium smegmatis
3.1.4.59 G313A/G314A/G315A/H316A mutation in DHHA1 domain, mutasnt displays residual activity Mycolicibacterium smegmatis
3.1.4.60 D134a/H135A/H136A mutation in DHH domain, complete loss of catalytic activity Mycolicibacterium smegmatis
3.1.4.60 G313A/G314A/G315A/H316A mutation in DHHA1 domain, mutant displays residual activity Mycolicibacterium smegmatis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.4.59 0.0068
-
cyclic di-3',5'-adenylate pH 7.8, 37°C Mycolicibacterium smegmatis
3.1.4.59 0.0809
-
cyclic di-3',5'-guanylate pH 7.8, 37°C Mycolicibacterium smegmatis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.59 Co2+ Pde is strictly dependent on Co2+, Mn2+, Mg2+ or Fe2+, with maximum activity with Mn2+ as a cofactor Mycolicibacterium smegmatis
3.1.4.59 Fe2+ Pde is strictly dependent on Co2+, Mn2+, Mg2+ or Fe2+, with maximum activity with Mn2+ as a cofactor Mycolicibacterium smegmatis
3.1.4.59 Mg2+ Pde is strictly dependent on Co2+, Mn2+, Mg2+ or Fe2+, with maximum activity with Mn2+ as a cofactor Mycolicibacterium smegmatis
3.1.4.59 Mn2+ Pde is strictly dependent on Co2+, Mn2+, Mg2+ or Fe2+, with maximum activity with Mn2+ as a cofactor Mycolicibacterium smegmatis
3.1.4.60 Co2+ Pde is strictly dependent on Co2+, Mn2+, Mg2+ or Fe2+, with maximum activity with Mn2+ as a cofactor Mycolicibacterium smegmatis
3.1.4.60 Fe2+ Pde is strictly dependent on Co2+, Mn2+, Mg2+ or Fe2+, with maximum activity with Mn2+ as a cofactor Mycolicibacterium smegmatis
3.1.4.60 Mg2+ Pde is strictly dependent on Co2+, Mn2+, Mg2+ or Fe2+, with maximum activity with Mn2+ as a cofactor Mycolicibacterium smegmatis
3.1.4.60 Mn2+ Pde is strictly dependent on Co2+, Mn2+, Mg2+ or Fe2+, with maximum activity with Mn2+ as a cofactor Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.59 cyclic di-3',5'-adenylate + H2O Mycolicibacterium smegmatis
-
5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
?
3.1.4.59 cyclic di-3',5'-adenylate + H2O Mycolicibacterium smegmatis ATCC 700084
-
5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
?
3.1.4.60 5'-O-phosphonoadenylyl-(3'->5')-adenosine + H2O Mycolicibacterium smegmatis
-
2 AMP
-
?
3.1.4.60 5'-O-phosphonoadenylyl-(3'->5')-adenosine + H2O Mycolicibacterium smegmatis ATCC 700084
-
2 AMP
-
?
3.1.4.60 cyclic di-3',5'-adenylate + H2O Mycolicibacterium smegmatis
-
5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
?
3.1.4.60 cyclic di-3',5'-adenylate + H2O Mycolicibacterium smegmatis ATCC 700084
-
5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.59 Mycolicibacterium smegmatis A0QVM9 protein contains a DHH-DHHAI domain
-
3.1.4.59 Mycolicibacterium smegmatis ATCC 700084 A0QVM9 protein contains a DHH-DHHAI domain
-
3.1.4.60 Mycolicibacterium smegmatis A0QVM9 protein contains a DHH-DHHAI domain
-
3.1.4.60 Mycolicibacterium smegmatis ATCC 700084 A0QVM9 protein contains a DHH-DHHAI domain
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.59 cyclic di-3',5'-adenylate + H2O
-
Mycolicibacterium smegmatis 5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
?
3.1.4.59 cyclic di-3',5'-adenylate + H2O
-
Mycolicibacterium smegmatis ATCC 700084 5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
?
3.1.4.59 cyclic di-3',5'-guanylate + H2O
-
Mycolicibacterium smegmatis 5'-phosphoguanylyl-(3'->5')guanosine
-
?
3.1.4.59 cyclic di-3',5'-guanylate + H2O
-
Mycolicibacterium smegmatis ATCC 700084 5'-phosphoguanylyl-(3'->5')guanosine
-
?
3.1.4.59 additional information Pde is capable of converting c-di-AMP to pApA, i.e. 5'-O-phosphonoadenylyl-(3'->5')-adenosine and AMP, and hydrolyzing pApA to AMP Mycolicibacterium smegmatis ?
-
?
3.1.4.59 additional information Pde is capable of converting c-di-AMP to pApA, i.e. 5'-O-phosphonoadenylyl-(3'->5')-adenosine and AMP, and hydrolyzing pApA to AMP Mycolicibacterium smegmatis ATCC 700084 ?
-
?
3.1.4.60 5'-O-phosphonoadenylyl-(3'->5')-adenosine + H2O
-
Mycolicibacterium smegmatis 2 AMP
-
?
3.1.4.60 5'-O-phosphonoadenylyl-(3'->5')-adenosine + H2O
-
Mycolicibacterium smegmatis ATCC 700084 2 AMP
-
?
3.1.4.60 cyclic di-3',5'-adenylate + H2O
-
Mycolicibacterium smegmatis 5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
?
3.1.4.60 cyclic di-3',5'-adenylate + H2O
-
Mycolicibacterium smegmatis ATCC 700084 5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.4.59 MSMEG_2630
-
Mycolicibacterium smegmatis
3.1.4.59 PDE
-
Mycolicibacterium smegmatis
3.1.4.60 MSMEG_2630
-
Mycolicibacterium smegmatis
3.1.4.60 PDE
-
Mycolicibacterium smegmatis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.4.59 37
-
assay at Mycolicibacterium smegmatis
3.1.4.59 37 50
-
Mycolicibacterium smegmatis
3.1.4.60 37
-
assay at Mycolicibacterium smegmatis
3.1.4.60 37 50
-
Mycolicibacterium smegmatis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.4.59 0.03
-
cyclic di-3',5'-guanylate pH 7.8, 37°C Mycolicibacterium smegmatis
3.1.4.59 0.52
-
cyclic di-3',5'-adenylate pH 7.8, 37°C Mycolicibacterium smegmatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.4.59 7.5
-
-
Mycolicibacterium smegmatis
3.1.4.60 7.5
-
-
Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
3.1.4.59 physiological function deficiency of Pde significantly enhances intracellular C12-C20 fatty acid accumulation. Superfluous c-di-AMP in Mycobacterium smegmatis may lead to abnormal colonial morphology Mycolicibacterium smegmatis
3.1.4.60 physiological function deficiency of Pde significantly enhances intracellular C12-C20 fatty acid accumulation. Superfluous c-di-AMP in Mycobacterium smegmatis may lead to abnormal colonial morphology Mycolicibacterium smegmatis