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Literature summary for 2.5.1.B21 extracted from

  • Deng, H.; O'Hagan, D.
    The fluorinase, the chlorinase and the duf-62 enzymes (2008), Curr. Opin. Chem. Biol., 12, 582-592.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + H2O Pyrococcus horikoshii the enzyme is most active at pH 8.5, so perhaps it has a regulatory role in influencing the cellular pH in the host organism. Many, but not all of the duf-62 containing organisms are extremophiles adenosine + L-methionine + H+
-
?

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58212
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + H2O the enzyme is most active at pH 8.5, so perhaps it has a regulatory role in influencing the cellular pH in the host organism. Many, but not all of the duf-62 containing organisms are extremophiles Pyrococcus horikoshii adenosine + L-methionine + H+
-
?
S-adenosyl-L-methionine + H2O mechanistic hypothesis for SAM hydroxide adenosyltransferase Pyrococcus horikoshii adenosine + L-methionine + H+
-
?

Synonyms

Synonyms Comment Organism
duf-62
-
Pyrococcus horikoshii
SAM hydroxide adenosyltransferase
-
Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Pyrococcus horikoshii