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1.97.1.4: [formate-C-acetyltransferase]-activating enzyme

This is an abbreviated version!
For detailed information about [formate-C-acetyltransferase]-activating enzyme, go to the full flat file.

Word Map on EC 1.97.1.4

Reaction

S-adenosyl-L-methionine
+
dihydroflavodoxin
+
[formate C-acetyltransferase]-glycine
=
5'-deoxyadenosine
+
L-methionine
+
flavodoxin semiquinone
+
[formate C-acetyltransferase]-glycin-2-yl radical
+
H+

Synonyms

PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving), Activase, pyruvate formate-lyase, Formate acetyltransferase activase, Pyruvate formate-lyase activase, Pyruvate formate-lyase activating enzyme, PFL-AE, Formate-lyase-activating enzyme, PFL activase, PFL-activating enzyme, PFL, pyruvate formate lyase activating enzyme, PFL activating enzyme, pyruvate formate-lyase-activating enzyme, PflA

ECTree

     1 Oxidoreductases
         1.97 Other oxidoreductases
             1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses
                1.97.1.4 [formate-C-acetyltransferase]-activating enzyme

Metals Ions

Metals Ions on EC 1.97.1.4 - [formate-C-acetyltransferase]-activating enzyme

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cobalt
-
Co(II) and Cu(II) can be reconstituted into the protein with similar stoichiometry
copper
-
Co(II) and Cu(II) can be reconstituted into the protein with similar stoichiometry
K+
the presence and identity of the bound monovalent cation, requiring a K+ ion bound in the active site for optimal activity
Na+
Na+ as the most likely ion present in the solved enzyme structures, and pulsed electron nuclear double resonance (ENDOR) demonstrates that the same cation site is occupied by 23Na in the solution state of the as isolated enzyme
[4Fe-4S] cluster
additional information
enzyme PFL-AE binds a catalytically essential monovalent cation at its active site. PFL-AE is thus a type I M+-activated enzyme whose M+ controls reactivity by interactions with the cosubstrate, SAM, which is bound to the catalytic iron-sulfur cluster. PFL-AE in the absence of any simple monovalent cations has little or no activity, and among monocations, going down Group 1 of the periodic table from Li+ to Cs+, PFL-AE activity sharply maximizes at K+ and NH4+. Cation binding site structure, e.g. with Mg2+, Cs+, Ca2+, Tl+, Li+, Zn2+, K+, NH4+, and Na+, overview. Modeling of different cations bound to the cation binding site of the enzyme, negative Fo-Fc electron density appears when the site is modeled as potassium or calcium, more extensive positive Fo-Fc electron density is present in the site when modeled with water than when modeled with sodium or magnesium. Residue D104 is important for cation binding