Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase

Thumbnail Image

Date

1999

Authors

Lappaenen, Veli-Matti
Merckel, Michael
Ollis, David
Wong, Kenny
Kozarich, John
Goldman, Adrian

Journal Title

Journal ISSN

Volume Title

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

Description

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

Citation

URI

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

Collections

ANU Research Publications

Source

Structure

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

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)

DSpace software copyright © 2002-2026 LYRASIS