| pubmed-article:16332250 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16332250 | lifeskim:mentions | umls-concept:C0004595 | lld:lifeskim |
| pubmed-article:16332250 | lifeskim:mentions | umls-concept:C1417216 | lld:lifeskim |
| pubmed-article:16332250 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:16332250 | lifeskim:mentions | umls-concept:C0598002 | lld:lifeskim |
| pubmed-article:16332250 | lifeskim:mentions | umls-concept:C0913811 | lld:lifeskim |
| pubmed-article:16332250 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:16332250 | pubmed:dateCreated | 2006-3-10 | lld:pubmed |
| pubmed-article:16332250 | pubmed:abstractText | Homotetrameric MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis catalyses the NAD-dependent oxidation of MMSA (methylmalonate semialdehyde) and MSA (malonate semialdehyde) into PPCoA (propionyl-CoA) and acetyl-CoA respectively via a two-step mechanism. In the present study, a detailed mechanistic characterization of the MSDH-catalysed reaction has been carried out. The results suggest that NAD binding elicits a structural imprinting of the apoenzyme, which explains the marked lag-phase observed in the activity assay. The enzyme also exhibits a half-of-the-sites reactivity, with two subunits being active per tetramer. This result correlates well with the presence of two populations of catalytic Cys302 in both the apo- and holo-enzymes. Binding of NAD causes a decrease in reactivity of the two Cys302 residues belonging to the two active subunits and a pKapp shift from approx. 8.8 to 8.0. A study of the rate of acylation as a function of pH revealed a decrease in the pKapp of the two active Cys302 residues to approx. 5.5. Taken to-gether, these results support a sequential Cys302 activation process with a pKapp shift from approx. 8.8 in the apo-form to 8.0 in the binary complex and finally to approx. 5.5 in the ternary complex. The rate-limiting step is associated with the b-decarboxylation process which occurs on the thioacylenzyme intermediate after NADH release and before transthioesterification. These data also indicate that bicarbonate, the formation of which is enzyme-catalysed, is the end-product of the reaction. | lld:pubmed |
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| pubmed-article:16332250 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16332250 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16332250 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16332250 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:16332250 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:16332250 | pubmed:author | pubmed-author:BranlantGuyG | lld:pubmed |
| pubmed-article:16332250 | pubmed:author | pubmed-author:TalfournierFr... | lld:pubmed |
| pubmed-article:16332250 | pubmed:author | pubmed-author:Stines-Chaume... | lld:pubmed |
| pubmed-article:16332250 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:16332250 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:16332250 | pubmed:volume | 395 | lld:pubmed |
| pubmed-article:16332250 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16332250 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16332250 | pubmed:pagination | 107-15 | lld:pubmed |
| pubmed-article:16332250 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16332250 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16332250 | pubmed:articleTitle | Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis. | lld:pubmed |
| pubmed-article:16332250 | pubmed:affiliation | Maturation des ARN et Enzymologie Moléculaire, UMR 7567 CNRS-UHP, Université Henri Poincaré Nancy I, 54506 Vandoeuvre-lès-Nancy Cedex, France. | lld:pubmed |
| pubmed-article:16332250 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16332250 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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