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
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1.97.1.4
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glycyl
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5\'-deoxyadenosyl
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iron-sulfur
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organometallic
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adomet
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oxygen-sensitive
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homolytic
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endor
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adenosylmethionine
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5'-deoxyadenosine
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h-atom
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sulfonium
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knappe
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deoxyadenosyl
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medicine
- 1.97.1.4
-
glycyl
-
5\'-deoxyadenosyl
-
iron-sulfur
-
organometallic
- adomet
-
oxygen-sensitive
-
homolytic
-
endor
- adenosylmethionine
- 5'-deoxyadenosine
-
h-atom
-
sulfonium
-
knappe
-
deoxyadenosyl
- medicine
Reaction
Synonyms
Activase, pyruvate formate-lyase, Formate acetyltransferase activase, Formate-lyase-activating enzyme, PFL, PFL activase, PFL activating enzyme, PFL-activating enzyme, PFL-AE, PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving), PflA, pyruvate formate lyase activating enzyme, Pyruvate formate-lyase activase, Pyruvate formate-lyase activating enzyme, pyruvate formate-lyase-activating enzyme
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Cofactor
Cofactor on EC 1.97.1.4 - [formate-C-acetyltransferase]-activating enzyme
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[4Fe-4S]-center
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an increase in pre-edge intensity is due to additional contributions from sulfide and thiolate of the Fe4S4 cluster into the C-S sigma* orbital. There is a backbonding interaction between the Fe4S4 cluster and C-S sigma* orbitals of S-adenosyl-L-methionine in this inner sphere complex. This backbonding is enhanced in the reduced form and this configurational interaction between the donor and acceptor orbitals facilitates the electron transfer from the cluster to S-adenosyl-L-methionine, that otherwise has a large outer sphere electron transfer barrier. The energy of the reductive cleavage of the C-S bond is sensitive to the dielectric of the protein in the immediate vicinity of the site as a high dielectric stabilizes the more charge separated reactant increasing the reaction barrier
additional information
reduced flavodoxin serves as an electron donor and SAM as a cosubstrate for PFL-AE to generate a 5'-deoxyadenosyl radical, which is responsible for PFL activation
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S-adenosyl-L-methionine
pyruvate formate-lyase activating enzyme is a radical SAM enzyme. Conserved cysteines coordinate three irons of a [4Fe-4S] cluster, while SAM coordinates the fourth iron through its amino and carboxylate moieties