Betaine aldehyde dehydrogenase (BADH) catalyses the irreversible oxidation of betaine aldehyde to glycine betaine with the concomitant reduction of NAD(P)+ to NADP(H). In Pseudomonas aeruginosa this reaction is a compulsory step in the assimilation of carbon and nitrogen when bacteria are growing in choline or choline precursors. The kinetic mechanisms of the NAD+- and NADP+-dependent reactions were examined by steady-state kinetic methods and by dinucleotide binding experiments. The double-reciprocal patterns obtained for initial velocity with NAD(P)+ and for product and dead-end inhibition establish that both mechanisms are steady-state random. However, quantitative analysis of the inhibitions, and comparison with binding data, suggest a preferred route of addition of substrates and release of products in which NAD(P)+ binds first and NAD(P)H leaves last, particularly in the NADP+-dependent reaction. Abortive binding of the dinucleotides, or their analogue ADP, in the betaine aldehyde site was inferred from total substrate inhibition by the dinucleotides, and parabolic inhibition by NADH and ADP. A weak partial uncompetitive substrate inhibition by the aldehyde was observed only in the NADP+-dependent reaction. The kinetics of P. aeruginosa BADH is very similar to that of glucose-6-phosphate dehydrogenase, suggesting that both enzymes fulfil a similar amphibolic metabolic role when the bacteria grow in choline and when they grow in glucose.
Skip Nav Destination
Follow us on Twitter @Biochem_Journal
Article navigation
December 2000
-
Cover Image
Cover Image
- PDF Icon PDF LinkTable of Contents
Research Article|
December 08 2000
Steady-state kinetic mechanism of the NADP+- and NAD+-dependent reactions catalysed by betaine aldehyde dehydrogenase from Pseudomonas aeruginosa
Roberto VELASCO-GARCÍA;
Roberto VELASCO-GARCÍA
*Laboratorio de Osmorregulación, ENEP Iztacala, Universidad Nacional Autónoma de México, Avenida de los Barrios s/n, Tlalnepantla, Estado de México, C. P. 54090, México
Search for other works by this author on:
Lilian GONZÁLEZ-SEGURA;
Lilian GONZÁLEZ-SEGURA
†Departamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, D. F. 04510, México
Search for other works by this author on:
Rosario A. MUÑOZ-CLARES
Rosario A. MUÑOZ-CLARES
1
†Departamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, D. F. 04510, México
1To whom correspondence should be addressed (e-mail [email protected]).
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
February 22 2000
Revision Received:
September 08 2000
Accepted:
October 05 2000
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 2000
2000
Biochem J (2000) 352 (3): 675–683.
Article history
Received:
February 22 2000
Revision Received:
September 08 2000
Accepted:
October 05 2000
Citation
Roberto VELASCO-GARCÍA, Lilian GONZÁLEZ-SEGURA, Rosario A. MUÑOZ-CLARES; Steady-state kinetic mechanism of the NADP+- and NAD+-dependent reactions catalysed by betaine aldehyde dehydrogenase from Pseudomonas aeruginosa. Biochem J 15 December 2000; 352 (3): 675–683. doi: https://doi.org/10.1042/bj3520675
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionGet Access To This Article
Cited By
Follow us on Twitter @Biochem_Journal
Open Access for all
We offer compliant routes for all authors from 2025. With library support, there will be no author nor reader charges in 5 journals. Check here |
![]() View past webinars > |