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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

Reference

Reference on EC 1.97.1.4 - [formate-C-acetyltransferase]-activating enzyme

Please use the Reference Search for a specific query.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johnson, M.K.; Staples, C.R.; Duin, E.C.; Lafferty, M.E.; Duderstadt, R.E.
Novel roles for Fe-S clusters in stabilizing or generating radical intermediates
Pure Appl. Chem.
70
939-946
1998
Escherichia coli
-
Manually annotated by BRENDA team
Weidner, G.; Sawers, G.
Molecular characterization of the genes encoding pyruvate formate-lyase and its activating enzyme of Clostridium pasteurianum
J. Bacteriol.
178
2440-2444
1996
Clostridium pasteurianum
Manually annotated by BRENDA team
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
J. Biol. Chem.
273
4897-4903
1998
Escherichia coli
Manually annotated by BRENDA team
Frey, M.; Rothe, M.; Wagner, A.F.V.; Knappe, J.
Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom
J. Biol. Chem.
269
12432-12437
1994
Escherichia coli
Manually annotated by BRENDA team
Wong, K.K.; Murray, B.W.; Lewisch, S.A.; Baxter, M.K.; Ridky, T.W.; Ulissi-DeMario, L.; Kozarich, J.W.
Molecular properties of pyruvate formate-lyase activating enzyme
Biochemistry
32
14102-14110
1993
Escherichia coli
Manually annotated by BRENDA team
Wagner, A.F.V.; Demand, J.; Schilling, G.; Pils, T.; Knappe, J.
A dehydroalanyl residue can capture the 5'-deoxyadenosyl radical generated from S-adenosylmethionine by pyruvate formate-lyase-activating enzyme
Biochem. Biophys. Res. Commun.
254
306-310
1999
Escherichia coli
Manually annotated by BRENDA team
Conradt, H.; Hohmann-Berger, M.; Hohmann, H.P.; Blaschkowski, H.P.; Knappe, J.
Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: isolation and structural properties
Arch. Biochem. Biophys.
228
133-142
1984
Escherichia coli
Manually annotated by BRENDA team
Rödel, W.; Plaga, W.; Frank, W.; Knappe, J.
Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide sequences
Eur. J. Biochem.
177
153-158
1988
Escherichia coli
Manually annotated by BRENDA team
Sawers, G.; Watson, G.
A glycyl radical solution: oxygen-dependent interconversion of pyruvate formate-lyase
Mol. Microbiol.
29
945-954
1998
Escherichia coli
Manually annotated by BRENDA team
Hesslinger, C.; Fairhurst, S.A.; Sawers, G.
Novel keto acid formate-lyase and propionate kinase enzynes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate
Mol. Microbiol.
27
477-492
1998
Escherichia coli
Manually annotated by BRENDA team
Asanuma, N.; Hino, T.
Molecular characterization and expression of pyruvate formate-lyase-activating enzyme in a ruminal bacterium, Streptococcus bovis
Appl. Environ. Microbiol.
68
3352-3357
2002
Streptococcus equinus (Q93UQ7), Streptococcus equinus
Manually annotated by BRENDA team
Broderick, J.B.; Henshaw, T.F.; Cheek, J.; Wojtuszewski, K.; Smith, S.R.; Trojan, M.R.; McGhan, R.M.; Kopf, A.; Kibbey, M.; Broderick, W.E.
Pyruvate formate-lyase-activating enzyme: Strictly anaerobic isolation yields active enzyme containing a [3Fe-4S]+ cluster
Biochem. Biophys. Res. Commun.
269
451-456
2000
Escherichia coli
Manually annotated by BRENDA team
Krebs, C.; Broderick, W.E.; Henshaw, T.F.; Broderick, J.B.; Huynh, B.H.
Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a moessbauer spectroscopic study
J. Am. Chem. Soc.
124
912-913
2002
Escherichia coli
Manually annotated by BRENDA team
Gelius-Dietrich, G.; Henze, K.
Pyruvate formate lyase (PFL) and PFL activating enzyme in the chytrid fungus Neocallimastix frontalis: a free-radical enzyme system conserved across divergent eukaryotic lineages
J. Eukaryot. Microbiol.
51
456-463
2004
Neocallimastix frontalis (Q6RFH6), Neocallimastix frontalis
Manually annotated by BRENDA team
Takahashi-Abbe, S.; Abe, K.; Takahashi, N.
Biochemical and functional properties of a pyruvate formate-lyase (PFL)-activating system in Streptococcus mutans
Oral Microbiol. Immunol.
18
293-297
2003
Streptococcus mutans
Manually annotated by BRENDA team
Sparling, R.; Islam, R.; Cicek, N.; Carere, C.; Chow, H.; Levin, D.B.
Formate synthesis by Clostridium thermocellum during anaerobic fermentation
Can. J. Microbiol.
52
681-688
2006
Acetivibrio thermocellus, Acetivibrio thermocellus 27405
Manually annotated by BRENDA team
Atteia, A.; van Lis, R.; Gelius-Dietrich, G.; Adrait, A.; Garin, J.; Joyard, J.; Rolland, N.; Martin, W.
Pyruvate formate-lyase and a novel route of eukaryotic ATP synthesis in Chlamydomonas mitochondria
J. Biol. Chem.
281
9909-9918
2006
Chlamydomonas reinhardtii
Manually annotated by BRENDA team
Peng, Y.; Veneziano, S.E.; Gillispie, G.D.; Broderick, J.B.
Pyruvate formate-lyase, evidence for an open conformation favored in the presence of its activating enzyme
J. Biol. Chem.
285
27224-27231
2010
Escherichia coli, Escherichia coli (P0A9N4)
Manually annotated by BRENDA team
Crain, A.V.; Broderick, J.B.
Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme
Biochim. Biophys. Acta
1834
2512-2519
2013
Escherichia coli
Manually annotated by BRENDA team
Dey, A.; Peng, Y.; Broderick, W.E.; Hedman, B.; Hodgson, K.O.; Broderick, J.B.; Solomon, E.I.
S K-edge XAS and DFT calculations on SAM dependent pyruvate formate-lyase activating enzyme: nature of interaction between the Fe4S4 cluster and SAM and its role in reactivity
J. Am. Chem. Soc.
133
18656-18662
2011
Escherichia coli
Manually annotated by BRENDA team
Crain, A.V.; Broderick, J.B.
Pyruvate formate-lyase and its activation by pyruvate formate-lyase activating enzyme
J. Biol. Chem.
289
5723-5729
2013
Escherichia coli
Manually annotated by BRENDA team
Zhang, Y.; Dai, Z.; Krivoruchko, A.; Chen, Y.; Siewers, V.; Nielsen, J.
Functional pyruvate formate lyase pathway expressed with two different electron donors in Saccharomyces cerevisiae at aerobic growth
FEMS Yeast Res.
15
fov024
2015
Escherichia coli (P0A9N4)
Manually annotated by BRENDA team
Shisler, K.A.; Hutcheson, R.U.; Horitani, M.; Duschene, K.S.; Crain, A.V.; Byer, A.S.; Shepard, E.M.; Rasmussen, A.; Yang, J.; Broderick, W.E.; Vey, J.L.; Drennan, C.L.; Hoffman, B.M.; Broderick, J.B.
Monovalent cation activation of the radical SAM enzyme pyruvate formate-lyase activating enzyme
J. Am. Chem. Soc.
139
11803-11813
2017
Escherichia coli (P0A9N4)
Manually annotated by BRENDA team
Crain, A.; Broderick, J.
Pyruvate formate-lyase and its activation by pyruvate formate-lyase activating enzyme
J. Biol. Chem.
289
5723-5729
2014
Escherichia coli (P0A9N4)
Manually annotated by BRENDA team
Al-Bayati, F.A.; Kahya, H.F.; Damianou, A.; Shafeeq, S.; Kuipers, O.P.; Andrew, P.W.; Yesilkaya, H.
Pneumococcal galactose catabolism is controlled by multiple regulators acting on pyruvate formate lyase
Sci. Rep.
7
43587
2017
Streptococcus pneumoniae (A0A0H2ZPG2), Streptococcus pneumoniae
Manually annotated by BRENDA team