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Literature summary 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

EC Number Activating Compound Comment Organism Structure
3.5.4.4 EDTA stimulates Methanocaldococcus jannaschii
3.5.4.28 EDTA stimulates Methanocaldococcus jannaschii
3.5.4.31 EDTA stimulates Methanocaldococcus jannaschii
3.5.4.41 EDTA stimulates Methanocaldococcus jannaschii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.4.4 expression in Escherichia coli Methanocaldococcus jannaschii
3.5.4.28 expression in Escherichia coli Methanocaldococcus jannaschii
3.5.4.31 expressed in Escherichia coli CodonPlus(DE3)-RIL cells Methanocaldococcus jannaschii
3.5.4.31 expression in Escherichia coli Methanocaldococcus jannaschii
3.5.4.41 expression in Escherichia coli Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
3.5.4.4 C294S the wild-type and the C294S mutant strains are stable after heating for 10 min at 60°C Methanocaldococcus jannaschii
3.5.4.4 E150R less thermostable than wild-type enzyme, stable for only 10 min at 50°C Methanocaldococcus jannaschii
3.5.4.4 Y136R less thermostable than wild-type enzyme, stable for only 10 min at 50°C Methanocaldococcus jannaschii
3.5.4.4 Y136R/E150R no activity with adenosine Methanocaldococcus jannaschii
3.5.4.28 C294S the wild-type and the C294S mutant strains are stable after heating for 10 min at 60°C Methanocaldococcus jannaschii
3.5.4.28 E150R less thermostable than wild-type enzyme, stable for 10 min at 50°C Methanocaldococcus jannaschii
3.5.4.28 Y136R less thermostable than wild-type enzyme, stable for 10 min at 50°C Methanocaldococcus jannaschii
3.5.4.28 Y136R/E150R no activity with adenosine Methanocaldococcus jannaschii
3.5.4.31 C294S the wild-type and the C294S mutant strains are stable after heating for 10 min at 60°C Methanocaldococcus jannaschii
3.5.4.31 E150R less thermostable than wild-type enzyme, stable for only 10 min at 50°C Methanocaldococcus jannaschii
3.5.4.31 E150R the mutant shows about 4fold increased activity compared to the wild type Methanocaldococcus jannaschii
3.5.4.31 Y136R less thermostable than wild-type enzyme, stable for only 10 min at 50°C Methanocaldococcus jannaschii
3.5.4.31 Y136R the mutant shows about 10fold increased activity compared to the wild type Methanocaldococcus jannaschii
3.5.4.31 Y136R/E150R no activity with adenosine Methanocaldococcus jannaschii
3.5.4.31 Y136R/E150R the mutant shows strongly reduced activity compared to the wild type Methanocaldococcus jannaschii
3.5.4.41 C294S the wild-type and the C294S mutant strains are stable after heating for 10 min at 60°C Methanocaldococcus jannaschii
3.5.4.41 E150R less thermostable than wild-type enzyme, stable for 10 min at 50°C, showing a significant loss of activity at 60°C. kcat/Km for 5'-deoxyadenosine is 93fold lower than the kcat/Km for the wild-type enzyme Methanocaldococcus jannaschii
3.5.4.41 Y136R less thermostable than wild-type enzyme, stable for 10 min at 50°C, showing a significant loss of activity at 60°C. kcat/Km for 5'-deoxyadenosine is 535fold lower than the kcat/Km for the wild-type enzyme Methanocaldococcus jannaschii
3.5.4.41 Y136R/E150R less thermostable than wild-type enzyme. kcat/Km for 5'-deoxyadenosine is 290000fold lower than the kcat/Km for the wild-type enzyme Methanocaldococcus jannaschii

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.4.4 0.072
-
 adenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.4 0.15
-
 adenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
3.5.4.4 0.15
-
 adenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.28 0.16
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.28 0.4
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii
3.5.4.28 1.1
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
3.5.4.28 3.9
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.31 0.022
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.31 0.022
-
 S-methyl-5'-thioadenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 0.048
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.31 0.048
-
 S-methyl-5'-thioadenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 0.072
-
 adenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 0.073
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii
3.5.4.31 0.073
-
 S-methyl-5'-thioadenosine mutant enzyme Y136R/E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 0.11
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
3.5.4.31 0.11
-
 S-methyl-5'-thioadenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 0.15
-
 adenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 0.15
-
 adenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.41 0.014
-
 5'-deoxyadenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
3.5.4.41 0.021
-
 5'-deoxyadenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.41 0.032
-
 5'-deoxyadenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.41 0.05
-
 5'-deoxyadenosine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.4.4 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
3.5.4.4 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
3.5.4.4 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
3.5.4.4 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
3.5.4.28 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
3.5.4.28 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
3.5.4.28 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
3.5.4.28 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
3.5.4.31 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
3.5.4.31 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
3.5.4.31 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
3.5.4.31 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
3.5.4.41 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
3.5.4.41 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
3.5.4.41 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
3.5.4.41 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.4.4 57500
-
 4 * 57500 Methanocaldococcus jannaschii
3.5.4.4 230000
-
 gel filtration Methanocaldococcus jannaschii
3.5.4.28 57500
-
 4 * 57500 Methanocaldococcus jannaschii
3.5.4.28 230000
-
 gel filtration Methanocaldococcus jannaschii
3.5.4.31 57500
-
 4 * 57500 Methanocaldococcus jannaschii
3.5.4.31 230000
-
 gel filtration Methanocaldococcus jannaschii
3.5.4.41 57500
-
 4 * 57500 Methanocaldococcus jannaschii
3.5.4.41 230000
-
 gel filtration Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.4.31 S-methyl-5'-thioadenosine + H2O Methanocaldococcus jannaschii
-
 S-methyl-5'-thioinosine + NH3
-
 ?
3.5.4.31 S-methyl-5'-thioadenosine + H2O Methanocaldococcus jannaschii DSM 2661
-
 S-methyl-5'-thioinosine + NH3
-
 ?
3.5.4.41 5'-deoxyadenosine + H2O Methanocaldococcus jannaschii 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 5'-deoxyinosine + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.4 Methanocaldococcus jannaschii Q58936
-
-
3.5.4.4 Methanocaldococcus jannaschii DSM 2661 Q58936
-
-
3.5.4.28 Methanocaldococcus jannaschii Q58936
-
-
3.5.4.28 Methanocaldococcus jannaschii DSM 2661 Q58936
-
-
3.5.4.31 Methanocaldococcus jannaschii Q58936
-
-
3.5.4.31 Methanocaldococcus jannaschii DSM 2661 Q58936
-
-
3.5.4.41 Methanocaldococcus jannaschii Q58936
-
-
3.5.4.41 Methanocaldococcus jannaschii DSM 2661 Q58936
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.4.4
-
 Methanocaldococcus jannaschii
3.5.4.28
-
 Methanocaldococcus jannaschii
3.5.4.31
-
 Methanocaldococcus jannaschii
3.5.4.41
-
 Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.4 adenosine + H2O catalytic efficiency of the enzyme for 5'-deoxyadenosine is 1000fold higher than for S-methyl-5'-thioadenosine, and 10000fold hgher than with S-adenosyl-L-homocysteine or adenosine Methanocaldococcus jannaschii inosine + NH3
-
 ?
3.5.4.4 adenosine + H2O catalytic efficiency of the enzyme for 5'-deoxyadenosine is 1000fold higher than for S-methyl-5'-thioadenosine, and 10000fold hgher than with S-adenosyl-L-homocysteine or adenosine Methanocaldococcus jannaschii DSM 2661 inosine + NH3
-
 ?
3.5.4.28 S-adenosyl-L-homocysteine + 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 adenosine + L-homocysteine
-
 ?
3.5.4.28 S-adenosyl-L-homocysteine + 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 adenosine + L-homocysteine
-
 ?
3.5.4.31 adenosine + H2O low activity Methanocaldococcus jannaschii inosine + NH3
-
 ?
3.5.4.31 adenosine + H2O low activity Methanocaldococcus jannaschii DSM 2661 inosine + NH3
-
 ?
3.5.4.31 S-methyl-5'-thioadenosine + H2O
-
 Methanocaldococcus jannaschii S-methyl-5'-thioinosine + NH3
-
 ?
3.5.4.31 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
-
 ?
3.5.4.31 S-methyl-5'-thioadenosine + H2O
-
 Methanocaldococcus jannaschii DSM 2661 S-methyl-5'-thioinosine + NH3
-
 ?
3.5.4.31 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
-
 ?
3.5.4.41 5'-deoxyadenosine + H2O 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 5'-deoxyinosine + NH3
-
 ?
3.5.4.41 5'-deoxyadenosine + 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 5'-deoxyinosine + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.4.4 tetramer 4 * 57500 Methanocaldococcus jannaschii
3.5.4.28 tetramer 4 * 57500 Methanocaldococcus jannaschii
3.5.4.31 tetramer 4 * 57500 Methanocaldococcus jannaschii
3.5.4.41 tetramer 4 * 57500 Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
3.5.4.4 MJ1541 locus name Methanocaldococcus jannaschii
3.5.4.28 MJ1541 locus name Methanocaldococcus jannaschii
3.5.4.31 DadD
-
 Methanocaldococcus jannaschii
3.5.4.31 MJ1541
-
 Methanocaldococcus jannaschii
3.5.4.31 MJ1541 locus name Methanocaldococcus jannaschii
3.5.4.31 MtaD
-
 Methanocaldococcus jannaschii
3.5.4.41 DadD
-
 Methanocaldococcus jannaschii
3.5.4.41 MJ1541 locus name Methanocaldococcus jannaschii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.4.31 60
-
-
 Methanocaldococcus jannaschii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.4.4 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
3.5.4.4 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
3.5.4.4 70
-
 10 min, mutant enzyme loses 66% of its activity Methanocaldococcus jannaschii
3.5.4.28 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
3.5.4.28 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
3.5.4.28 70
-
 10 min, mutant enzyme loses 66% of its activity Methanocaldococcus jannaschii
3.5.4.31 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
3.5.4.31 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
3.5.4.31 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
3.5.4.31 70
-
 10 min, mutant enzyme loses 66% of its activity Methanocaldococcus jannaschii
3.5.4.41 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
3.5.4.41 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
3.5.4.41 70
-
 10 min, mutant enzyme loses 66% of its activity Methanocaldococcus jannaschii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.4.4 110
-
 adenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
3.5.4.4 110
-
 adenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.4 140
-
 adenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.28 2.1
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii
3.5.4.28 2.7
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.28 58.2
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.28 1300
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
3.5.4.31 1.39
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii
3.5.4.31 1.39
-
 S-methyl-5'-thioadenosine mutant enzyme Y136R/E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 110
-
 adenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 110
-
 adenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 140
-
 adenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 160
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
3.5.4.31 160
-
 S-methyl-5'-thioadenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 200
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.31 200
-
 S-methyl-5'-thioadenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 220
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.31 220
-
 S-methyl-5'-thioadenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.41 1.12
-
 5'-deoxyadenosine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii
3.5.4.41 21
-
 5'-deoxyadenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.41 330
-
 5'-deoxyadenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.41 120000
-
 5'-deoxyadenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.4.31 9
-
-
 Methanocaldococcus jannaschii

General Information

EC Number General Information Comment Organism
3.5.4.4 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
3.5.4.28 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
3.5.4.31 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
3.5.4.41 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.4.4 750
-
 adenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
3.5.4.4 750
-
 adenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.4 2900
-
 adenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.28 5.3
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii
3.5.4.28 21
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.28 230
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.28 4400
-
 S-adenosyl-L-homocysteine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
3.5.4.31 19
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii
3.5.4.31 19
-
 S-methyl-5'-thioadenosine mutant enzyme Y136R/E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 750
-
 adenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 750
-
 adenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 1100
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii
3.5.4.31 1100
-
 S-methyl-5'-thioadenosine wild type enzyme, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 2900
-
 adenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 4200
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.31 4200
-
 S-methyl-5'-thioadenosine mutant enzyme E150R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.31 11000
-
 S-methyl-5'-thioadenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.31 11000
-
 S-methyl-5'-thioadenosine mutant enzyme Y136R, at pH 9.0 and 60°C Methanocaldococcus jannaschii
3.5.4.41 31
-
 5'-deoxyadenosine pH and temperature not specified in the publication, mutant enzyme Y136R/E150R Methanocaldococcus jannaschii
3.5.4.41 17000
-
 5'-deoxyadenosine pH and temperature not specified in the publication, mutant enzyme Y136R Methanocaldococcus jannaschii
3.5.4.41 98000
-
 5'-deoxyadenosine pH and temperature not specified in the publication, mutant enzyme E150R Methanocaldococcus jannaschii
3.5.4.41 9100000
-
 5'-deoxyadenosine pH and temperature not specified in the publication, wild-type enzyme Methanocaldococcus jannaschii