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Mechanism of the dehydrogenase reaction of DmpFG and analysis of inter-subunit channeling efficiency and thermodynamic parameters in the overall reaction

Date

Authors

Smith, Natalie E

Tie, Wan Jun

Flematti, Gavin

Stubbs, Keith A

Corry, Ben

Attwood, Paul V

Vrielink, Alice

Publisher

Pergamon-Elsevier Ltd

Abstract

The bifunctional, microbial enzyme DmpFG is comprised of two subunits: the aldolase, DmpG, and the dehydrogenase, DmpF. DmpFG is of interest due to its ability to channel substrates between the two spatially distinct active sites. While the aldolase is we

Keywords

Keywords: acetaldehyde; acetyl coenzyme A; DmpFG enzyme; fructose bisphosphate aldolase; microbial enzyme; oxidoreductase; reduced nicotinamide adenine dinucleotide; unclassified drug; article; catalysis; energy; entropy; enzyme activity; enzyme inhibition; oxidati Allosteric interaction; Enzyme activity; Substrate channeling; Thermodynamic activation parameters

URI

http://hdl.handle.net/1885/77652

Collections

ANU Research Publications

Source

The International Journal of Biochemistry and Cell Biology

Type

Journal article

DOI

10.1016/j.biocel.2013.05.028

Restricted until

2037-12-31

Downloads

File

Description

01_Smith_Mechanism_of_the_dehydrogenase_2013.pdf (1.12 MB)

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