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Mechanism of glyceraldehyde‐3‐phosphate transfer from aldolase to glyceraldehyde‐3‐phosphate dehydrogenase

Kvassman, Jan LU ; Pettersson, Gösta LU and Ryde-Pettersson, Ulf LU (1988) In European Journal of Biochemistry 172(2). p.427-431
Abstract

The catalytic interaction of glyceraldehyde‐3‐phosphate dehydrogenase with glyceraldehydes‐3‐phosphate has been examined by transient‐state kinetic methods. The results confirm previous reports that the apparent Km for oxidative phosphorylation of glyceraldehydes‐3‐phosphate decreases at least 50‐fold when the substrate is generated in a coupled reaction system through the action of aldolase on fructose 1,6‐bisphosphate, but lend no support to the proposal that glyceraldehydes 3‐phosphate is directly transferred between the two enzymes without prior release to the reaction medium. A theoretical analysis is presented which shows that the kinetic behaviour of the coupled two‐enzyme system is compatible in all respects tested... (More)

The catalytic interaction of glyceraldehyde‐3‐phosphate dehydrogenase with glyceraldehydes‐3‐phosphate has been examined by transient‐state kinetic methods. The results confirm previous reports that the apparent Km for oxidative phosphorylation of glyceraldehydes‐3‐phosphate decreases at least 50‐fold when the substrate is generated in a coupled reaction system through the action of aldolase on fructose 1,6‐bisphosphate, but lend no support to the proposal that glyceraldehydes 3‐phosphate is directly transferred between the two enzymes without prior release to the reaction medium. A theoretical analysis is presented which shows that the kinetic behaviour of the coupled two‐enzyme system is compatible in all respects tested with a free‐diffusion mechanism for the transfer of glyceraldehydes 3‐phosphate from the producing enzyme to the consuming one. Copyright © 1988, Wiley Blackwell. All rights reserved

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
European Journal of Biochemistry
volume
172
issue
2
pages
5 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:0023974881
ISSN
0014-2956
DOI
10.1111/j.1432-1033.1988.tb13905.x
language
English
LU publication?
yes
id
b5453fe0-b6ac-4cfd-8f25-40aaabeae13b
date added to LUP
2017-02-04 11:26:44
date last changed
2017-07-30 05:21:05
@article{b5453fe0-b6ac-4cfd-8f25-40aaabeae13b,
  abstract     = {<p>The catalytic interaction of glyceraldehyde‐3‐phosphate dehydrogenase with glyceraldehydes‐3‐phosphate has been examined by transient‐state kinetic methods. The results confirm previous reports that the apparent K<sub>m</sub> for oxidative phosphorylation of glyceraldehydes‐3‐phosphate decreases at least 50‐fold when the substrate is generated in a coupled reaction system through the action of aldolase on fructose 1,6‐bisphosphate, but lend no support to the proposal that glyceraldehydes 3‐phosphate is directly transferred between the two enzymes without prior release to the reaction medium. A theoretical analysis is presented which shows that the kinetic behaviour of the coupled two‐enzyme system is compatible in all respects tested with a free‐diffusion mechanism for the transfer of glyceraldehydes 3‐phosphate from the producing enzyme to the consuming one. Copyright © 1988, Wiley Blackwell. All rights reserved</p>},
  author       = {Kvassman, Jan and Pettersson, Gösta and Ryde-Pettersson, Ulf},
  issn         = {0014-2956},
  language     = {eng},
  number       = {2},
  pages        = {427--431},
  publisher    = {Wiley-Blackwell},
  series       = {European Journal of Biochemistry},
  title        = {Mechanism of glyceraldehyde‐3‐phosphate transfer from aldolase to glyceraldehyde‐3‐phosphate dehydrogenase},
  url          = {http://dx.doi.org/10.1111/j.1432-1033.1988.tb13905.x},
  volume       = {172},
  year         = {1988},
}