Literature summary for 2.3.1.54 extracted from

Becker, A.; Fritz-Wolf, K.; Kabsch, W.; Knappe, J.; Schultz, S.; Wagner, A.F.V.
Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase (1999), Nat. Struct. Biol., 6, 969-975.

Search for more literature for 2.3.1.54

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant pfl in Escherichia coli RM221	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
space group P4(3)2(1)2 a = b = 159 A, c = 160 A	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
85000	-	2 * 85000, homodimer, SDS-PAGE	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
pyruvate + CoA	Escherichia coli	-	acetyl-CoA + formate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Escherichia coli	P09373	PFL wild-type, structure factor amplitude and model coordinate, Protein Data Bank accession code	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pyruvate + CoA	-	Escherichia coli	acetyl-CoA + formate	-	?
pyruvate + CoA	-	Escherichia coli	acetyl-CoA + formate	-	r

Subunits

Subunits	Comment	Organism
dimer	2 * 85000, homodimer, SDS-PAGE	Escherichia coli

Synonyms

Synonyms	Comment	Organism
PFL	-	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)