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Literature summary extracted from

  • Deng, H.; Botting, C.H.; Hamilton, J.T.; Russell, R.J.; O'Hagan, D.
    S-adenosyl-L-methionine:hydroxide adenosyltransferase: a SAM enzyme (2008), Angew. Chem. Int. Ed. Engl., 47, 5357-5361.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.B21 expression in Escherichia coli Pyrococcus horikoshii

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.B21 S-adenosyl-L-homocysteine
-
 Pyrococcus horikoshii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.B21 0.0392
-
 S-adenosyl-L-methionine pH 8.5, 37°C Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.B21 Pyrococcus horikoshii O58212 strain OT3
-
2.5.1.B21 Pyrococcus horikoshii OT-3 O58212 strain OT3
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.B21
-
 Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.B21 5'-deoxy-5'-chloroadenosine + H2O adenosine is generated from 5'-deoxy-5'-chloroadenosine with much lower efficiency than from S-adenosyl-L-methionine Pyrococcus horikoshii adenosine + ?
-
 ?
2.5.1.B21 5'-deoxy-5'-chloroadenosine + H2O adenosine is generated from 5'-deoxy-5'-chloroadenosine with much lower efficiency than from S-adenosyl-L-methionine Pyrococcus horikoshii OT-3 adenosine + ?
-
 ?
2.5.1.B21 S-adenosyl-L-methionine + H2O conversion of S-adenosyl-L-methionine into adenosine by the attack of a hydroxide ion from water at C5’ of S-adenosyl-L-methionine. No new products are detected by HPLC or NMR spectroscopy after the incubation of the enzyme with S-adenosyl-L-methionine and F-, Cl-, or NH4+ ions at high mM concentrations. In all cases adenosine is generated in a manner consistent with normal enzymatic turnover, with water providing the nucleophil Pyrococcus horikoshii adenosine + L-methionine + H+
-
 ?
2.5.1.B21 S-adenosyl-L-methionine + H2O conversion of S-adenosyl-L-methionine into adenosine by the attack of a hydroxide ion from water at C5’ of S-adenosyl-L-methionine. No new products are detected by HPLC or NMR spectroscopy after the incubation of the enzyme with S-adenosyl-L-methionine and F-, Cl-, or NH4+ ions at high mM concentrations. In all cases adenosine is generated in a manner consistent with normal enzymatic turnover, with water providing the nucleophil Pyrococcus horikoshii OT-3 adenosine + L-methionine + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.B21 duf62 gene name. duf: domain of unknown function. Found in extremophiles Pyrococcus horikoshii
2.5.1.B21 SAM hydroxide adenosyltransferase
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.B21 37
-
 assay at Pyrococcus horikoshii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.5.1.B21 80
-
 the enzyme retains full activity after being heated at 80°C for 30 min and then cooled to 37°C Pyrococcus horikoshii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.B21 0.14
-
 S-adenosyl-L-methionine pH 8.5, 37°C Pyrococcus horikoshii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.B21 8.5
-
-
 Pyrococcus horikoshii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.5.1.B21 5 10 the enzyme is inactive below pH 5 and above pH 10 Pyrococcus horikoshii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.5.1.B21 0.0036
-
 S-adenosyl-L-homocysteine pH 8.5, 37°C Pyrococcus horikoshii