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Literature summary for 3.5.4.31 extracted from

  • Miller, D.; O'Brien, K.; Xu, H.; White, R.H.
    Identification of a 5'-deoxyadenosine deaminase in Methanocaldococcus jannaschii and its possible role in recycling the radical S-adenosylmethionine enzyme reaction product 5'-deoxyadenosine (2013), J. Bacteriol., 196, 1064-1072.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
EDTA stimulates Methanocaldococcus jannaschii

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli CodonPlus(DE3)-RIL cells Methanocaldococcus jannaschii
expression in Escherichia coli Methanocaldococcus jannaschii

Protein Variants

Protein Variants Comment Organism
C294S the wild-type and the C294S mutant strains are stable after heating for 10 min at 60°C Methanocaldococcus jannaschii
E150R less thermostable than wild-type enzyme, stable for only 10 min at 50°C Methanocaldococcus jannaschii
E150R the mutant shows about 4fold increased activity compared to the wild type Methanocaldococcus jannaschii
Y136R less thermostable than wild-type enzyme, stable for only 10 min at 50°C Methanocaldococcus jannaschii
Y136R the mutant shows about 10fold increased activity compared to the wild type Methanocaldococcus jannaschii
Y136R/E150R no activity with adenosine Methanocaldococcus jannaschii
Y136R/E150R the mutant shows strongly reduced activity compared to the wild type Methanocaldococcus jannaschii

Inhibitors

Inhibitors Comment Organism Structure
additional information the presence of 0.02 M dithiothreitol has no effect on the enzymatic activity Methanocaldococcus jannaschii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.022
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
0.022
-
S-methyl-5'-thioadenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
0.048
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
0.048
-
S-methyl-5'-thioadenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
0.072
-
adenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
0.073
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii
0.073
-
S-methyl-5'-thioadenosine mutant enzyme Y136R/E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
0.11
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
0.11
-
S-methyl-5'-thioadenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii
0.15
-
adenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
0.15
-
adenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal Methanocaldococcus jannaschii
additional information metal-dependent enzyme. The metal can not be removed from the enzyme nor can the nature of the catalytic metal be established. Dialysis of the wild-type enzyme for 3 days against a dipicolinic acid containing buffer fails to show any lowering enzyme activity, again indicating that chelation is not able to remove the bound metal in the active site. The catalytic metal is not removed by EDTA Methanocaldococcus jannaschii
Ni2+ the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal Methanocaldococcus jannaschii
Zn2+ the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal Methanocaldococcus jannaschii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57500
-
4 * 57500 Methanocaldococcus jannaschii
230000
-
gel filtration Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-methyl-5'-thioadenosine + H2O Methanocaldococcus jannaschii
-
S-methyl-5'-thioinosine + NH3
-
?
S-methyl-5'-thioadenosine + H2O Methanocaldococcus jannaschii DSM 2661
-
S-methyl-5'-thioinosine + NH3
-
?

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q58936
-
-
Methanocaldococcus jannaschii DSM 2661 Q58936
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanocaldococcus jannaschii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenosine + H2O low activity Methanocaldococcus jannaschii inosine + NH3
-
?
adenosine + H2O low activity Methanocaldococcus jannaschii DSM 2661 inosine + NH3
-
?
S-methyl-5'-thioadenosine + H2O
-
Methanocaldococcus jannaschii S-methyl-5'-thioinosine + NH3
-
?
S-methyl-5'-thioadenosine + H2O catalytic efficiency of the enzyme for 5'-deoxyadenosine is 1000fold higher than for S-methyl-5'-thioadenosine, and 10000fold higher than with S-adenosyl-L-homocysteine or adenosine Methanocaldococcus jannaschii S-methyl-5'-thioinosine + NH3
-
?
S-methyl-5'-thioadenosine + H2O
-
Methanocaldococcus jannaschii DSM 2661 S-methyl-5'-thioinosine + NH3
-
?
S-methyl-5'-thioadenosine + H2O catalytic efficiency of the enzyme for 5'-deoxyadenosine is 1000fold higher than for S-methyl-5'-thioadenosine, and 10000fold higher than with S-adenosyl-L-homocysteine or adenosine Methanocaldococcus jannaschii DSM 2661 S-methyl-5'-thioinosine + NH3
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 57500 Methanocaldococcus jannaschii

Synonyms

Synonyms Comment Organism
DadD
-
Methanocaldococcus jannaschii
MJ1541
-
Methanocaldococcus jannaschii
MJ1541 locus name Methanocaldococcus jannaschii
MtaD
-
Methanocaldococcus jannaschii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Methanocaldococcus jannaschii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
10 min, mutant enzyme Y136R/E150R loses 65% of its activity, mutant enzyme Y136R loses 20% of its activity, mutant enzyme E150R loses% of its activity Methanocaldococcus jannaschii
60
-
10 min, wild-type enzyme loses 10% of its activity, mutant enzyme Y136R loses 60% of its activity, mutant enzyme E150R loses 75% of its activity Methanocaldococcus jannaschii
60 70 the enzyme shows 90% of retained activity after 10 min at 60°C and 34% of retained activity after 10 min at 70°C Methanocaldococcus jannaschii
70
-
10 min, mutant enzyme loses 66% of its activity Methanocaldococcus jannaschii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.39
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii
1.39
-
S-methyl-5'-thioadenosine mutant enzyme Y136R/E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
110
-
adenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
110
-
adenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii
140
-
adenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
160
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
160
-
S-methyl-5'-thioadenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii
200
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
200
-
S-methyl-5'-thioadenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
220
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
220
-
S-methyl-5'-thioadenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
Methanocaldococcus jannaschii

General Information

General Information Comment Organism
metabolism the enzyme is involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens Methanocaldococcus jannaschii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
19
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii
19
-
S-methyl-5'-thioadenosine mutant enzyme Y136R/E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
750
-
adenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
750
-
adenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii
1100
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
1100
-
S-methyl-5'-thioadenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii
2900
-
adenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
4200
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
4200
-
S-methyl-5'-thioadenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
11000
-
S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
11000
-
S-methyl-5'-thioadenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii