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Protein Science (2006), 15:1387-1396. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Characterization of E. coli tetrameric aldehyde dehydrogenases with atypical properties compared to other aldehyde dehydrogenases

José Salud Rodríguez-Zavala1, Abdellah Allali-Hassani2 and Henry Weiner2

1 Departamento de Bioquímica, Instituto Nacional de Cardiología, Tlalpan, México D.F. 14080, México
2 Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907-2063, USA

(RECEIVED December 14, 2005; FINAL REVISION March 3, 2006; ACCEPTED March 6, 2006)

Aldehyde dehydrogenases are general detoxifying enzymes, but there are also isoenzymes that are involved in specific metabolic pathways in different organisms. Two of these enzymes are Escherichia coli lactaldehyde (ALD) and phenylacetaldehyde dehydrogenases (PAD), which participate in the metabolism of fucose and phenylalanine, respectively. These isozymes share some properties with the better characterized mammalian enzymes but have kinetic properties that are unique. It was possible to thread the sequences into the known ones for the mammalian isozymes to better understand some structural differences. Both isozymes were homotetramers, but PAD used both NAD+ and NADP+ but with a clear preference for NAD, while ALD used only NAD+. The rate-limiting step for PAD was hydride transfer as indicated by the primary isotopic effect and the absence of a pre-steady-state burst, something not previously found for tetrameric enzymes from other organisms where the rate-limiting step is related to both deacylation and coenzyme dissociation. In contrast, ALD had a pre-steady-state burst indicating that the rate-limiting step was located after the NADH formation, but the rate-limiting step was a combination of deacylation and coenzyme dissociation. Both enzymes possessed esterase activity that was stimulated by NADH; NAD+ stimulated the esterase activity of PAD but not of ALD. Finding enzymes that structurally are similar to the well-characterized mammalian enzymes but have a different rate-limiting step might serve as models to allow us to determine what regulates the rate-limiting step.

Keywords: aldehyde dehydrogenase; ALDH; phenylacetaldehyde dehydrogenase; lactaldehyde dehydrogenase; pre-steady-state burst; esterase activity


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J. S. Rodriguez-Zavala
Enhancement of coenzyme binding by a single point mutation at the coenzyme binding domain of E. coli lactaldehyde dehydrogenase
Protein Sci., March 1, 2008; 17(3): 563 - 570.
[Abstract] [Full Text] [PDF]


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