Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ruzicka, F.J.; Frey, P.A.
    Glutamate 2,3-aminomutase: a new member of the radical SAM superfamily of enzymes (2007), Biochim. Biophys. Acta, 1774, 286-296.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.3.9 gene eam, DNA and amio acid sequence determination and analysis, functional expression in Escherichia coli BL21 (DE3) CodonPlus RILP cells Clostridioides difficile

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.4.3.9 O2 glutamate-specific 2,3-aminomutases is sensitive to molecular oxygen which oxidizes the [4Fe-4S]1+ cluster required for catalysis to [4Fe–4S]2+ Clostridioides difficile

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.3.9 Fe2+ required, iron-sulfide cluster [4Fe-4S], the iron-sulfur cluster in glutamate 2,3-aminomutase is labile duirng purification Clostridioides difficile

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.3.9 beta-glutamate Clostridioides difficile
-
3-aminopentanedioate
-
?
5.4.3.9 L-glutamate Clostridioides difficile
-
3-aminopentanedioate
-
?

Organism

EC Number Organism UniProt Comment Textmining
5.4.3.9 Clostridioides difficile
-
gene eam
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.3.9 recombinant enzyme from Escherichia coli by ammonium sulfate fractuionation, hydrophobic interaction chromatography, anion exchange chromatography, another step of ammonium sulfate fractionation, centrifugation, and gel filtration Clostridioides difficile

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.3.9 beta-glutamate
-
Clostridioides difficile 3-aminopentanedioate
-
?
5.4.3.9 L-glutamate
-
Clostridioides difficile 3-aminopentanedioate
-
?
5.4.3.9 additional information no activity with L-lysine by the recombinant enzyme Clostridioides difficile ?
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.4.3.9 37
-
assay at Clostridioides difficile

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4.3.9 8
-
assay at Clostridioides difficile

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.3.9 pyridoxal 5'-phosphate enzyme-bound, one molecule per subunit Clostridioides difficile

General Information

EC Number General Information Comment Organism
5.4.3.9 evolution glutamate 2,3-aminomutase is a member of the radical SAM superfamily of enzymes. The highly active glutamate 2,3-aminomutase that is homologous with lysine 2,3-aminomutase Clostridioides difficile