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.
(Less)
- author
- Kvassman, Jan
LU
; Pettersson, Gösta
LU
and Ryde-Pettersson, Ulf
LU
- organization
- publishing date
- 1988
- 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
-
- pmid:3350006
- 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
- 2025-01-07 06:05:06
@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.</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 = {{https://lup.lub.lu.se/search/files/24720444/gapdh.pdf}},
doi = {{10.1111/j.1432-1033.1988.tb13905.x}},
volume = {{172}},
year = {{1988}},
}