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Literature summary for 3.1.4.59 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
Search for more literature for 3.1.4.59

Protein Variants

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

KM Value [mM]

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

Metals/Ions

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

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

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclic di-3',5'-adenylate + H2O
-
 Mycolicibacterium smegmatis 5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
 ?
cyclic di-3',5'-adenylate + H2O
-
 Mycolicibacterium smegmatis ATCC 700084 5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
 ?
cyclic di-3',5'-guanylate + H2O
-
 Mycolicibacterium smegmatis 5'-phosphoguanylyl-(3'->5')guanosine
-
 ?
cyclic di-3',5'-guanylate + H2O
-
 Mycolicibacterium smegmatis ATCC 700084 5'-phosphoguanylyl-(3'->5')guanosine
-
 ?
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 ?
-
 ?
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 ?
-
 ?

Synonyms

Synonyms Comment Organism
MSMEG_2630
-
 Mycolicibacterium smegmatis
PDE
-
 Mycolicibacterium smegmatis

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Mycolicibacterium smegmatis

General Information

General Information Comment Organism
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