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

BRENDA support

Literature summary extracted from

  • Kulzer, R.; Pils, T.; Kappl, R.; Huttermann, J.; Knappe, J.
    Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form (1998), J. Biol. Chem., 273, 4897-4903.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.97.1.4 C102S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent Escherichia coli
1.97.1.4 C12S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent Escherichia coli
1.97.1.4 C29S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent Escherichia coli
1.97.1.4 C33S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent Escherichia coli
1.97.1.4 C36S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent Escherichia coli
1.97.1.4 C94S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.97.1.4 Iron contains an iron-sulfur cluster, most probably of the [4Fe-4S]type Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.97.1.4 28000
-
 gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.54 pyruvate + CoA Escherichia coli key enzyme of the glucose fermentation route in anaerobically growing cells acetyl-CoA + formate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.97.1.4 Escherichia coli
-
-
-
2.3.1.54 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.97.1.4 S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
-
 Escherichia coli 5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
-
 ?
2.3.1.54 pyruvate + CoA
-
 Escherichia coli acetyl-CoA + formate
-
 ?
2.3.1.54 pyruvate + CoA key enzyme of the glucose fermentation route in anaerobically growing cells Escherichia coli acetyl-CoA + formate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.54 PFL
-
 Escherichia coli