کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2580641 1561635 2013 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Catalytic properties of a bacterial acylating acetaldehyde dehydrogenase: Evidence for several active oligomeric states and coenzyme A activation upon binding
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم محیط زیست بهداشت، سم شناسی و جهش زایی
پیش نمایش صفحه اول مقاله
Catalytic properties of a bacterial acylating acetaldehyde dehydrogenase: Evidence for several active oligomeric states and coenzyme A activation upon binding
چکیده انگلیسی

Until the last decade, two unrelated aldehyde dehydrogenase (ALDH) superfamilies, i.e. the phosphorylating and non-phosphorylating superfamilies, were known to catalyze the oxidation of aldehydes to activated or non-activated acids. However, a third one was discovered by the crystal structure of a bifunctional enzyme 4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase (DmpFG) from Pseudomonas sp. strain CF600 (Manjasetty et al., Proc. Natl. Acad. Sci. USA 100 (2003) 6992–6997). Indeed, DmpF exhibits a non-phosphorylating CoA-dependent ALDH activity, but is structurally related to the phosphorylating superfamily. In this study, we undertook the characterization of the catalytic and structural properties of MhpEF from Escherichia coli, an ortholog of DmpFG in which MhpF converts acetaldehyde, produced by the cleavage of 4-hydroxy-2-ketovalerate by MhpE, into acetyl-CoA. The kinetic data obtained under steady-state and pre-steady-state conditions show that the aldehyde dehydrogenase, MhpF, is active as a monomer, a unique feature relative to the phosphorylating and non-phosphorylating ALDH superfamilies. Our results also reveal that the catalytic properties of MhpF are not dependent on its oligomeric state, supporting the hypothesis of a structurally and catalytically independent entity. Moreover, the transthioesterification is shown to be rate-limiting and, when compared with a chemical model, its catalytic efficiency is increased 104-fold. Therefore, CoA binding to MhpF increases its reactivity and optimizes its positioning relative to the thioacylenzyme intermediate, thus enabling the formation of an efficient deacylation complex.


► The catalytic properties of an acylating aldehyde dehydrogenase are investigated.
► The monomeric form of this aldehyde dehydrogenase is shown to be fully active.
► The rate-limiting step of the reaction is associated with the transthioesterification.
► The catalytic efficiency of the transthioesterification relies on CoA binding mode.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Chemico-Biological Interactions - Volume 202, Issues 1–3, 25 February 2013, Pages 70–77
نویسندگان
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