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Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase

Date

Authors

Lappaenen, Veli-Matti

Merckel, Michael

Ollis, David

Wong, Kenny

Kozarich, John

Goldman, Adrian

Publisher

Cell Press

Abstract

Background: Pyruvate formate lyase (PFL) catalyses a key step in Escherichia coli anaerobic glycolysis by converting pyruvate and CoA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate, involving an essential Cα

Keywords

Keywords: bacterial enzyme; lyase; ribonucleotide reductase; article; binding site; catalysis; enzyme analysis; enzyme binding; enzyme mechanism; enzyme structure; escherichia coli; nonhuman; priority journal; structure analysis; Acetyltransferases; Amino Acid Sequ Enzyme mechanism; Pyruvate formate lyase; Ribonucleotide reductase; Structure; X-ray crystallography

URI

http://hdl.handle.net/1885/93797

Collections

ANU Research Publications

Source

Structure

Type

Journal article

DOI

10.1016/S0969-2126(99)80098-7

Restricted until

2037-12-31

Downloads

File

Description

01_Lappaenen_Pyruvate_formate_lyase_is_1999.pdf (309.86 KB)

02_Lappaenen_Pyruvate_formate_lyase_is_1999.pdf (309.86 KB)

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