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http://purl.uniprot.org/citations/16274229http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16274229http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16274229http://www.w3.org/2000/01/rdf-schema#comment"Malonate semialdehyde decarboxylase (MSAD) from Pseudomonas pavonaceae 170 is a tautomerase superfamily member that converts malonate semialdehyde to acetaldehyde by a mechanism utilizing Pro-1 and Arg-75. Pro-1 and Arg-75 have also been implicated in the hydratase activity of MSAD in which 2-oxo-3-pentynoate is processed to acetopyruvate. Crystal structures of MSAD (1.8 A resolution), the P1A mutant of MSAD (2.7 A resolution), and MSAD inactivated by 3-chloropropiolate (1.6 A resolution), a mechanism-based inhibitor activated by the hydratase activity of MSAD, have been determined. A comparison of the P1A-MSAD and MSAD structures reveals little geometric alteration, indicating that Pro-1 plays an important catalytic role but not a critical structural role. The structures of wild-type MSAD and MSAD covalently modified at Pro-1 by 3-oxopropanoate, the adduct resulting from the incubation of MSAD and 3-chloropropiolate, implicate Asp-37 as the residue that activates a water molecule for attack at C-3 of 3-chloropropiolate to initiate a Michael addition of water. The interactions of Arg-73 and Arg-75 with the C-1 carboxylate group of the adduct suggest these residues polarize the alpha,beta-unsaturated acid and facilitate the addition of water. On the basis of these structures, a mechanism for the inactivation of MSAD by 3-chloropropiolate can be formulated along with mechanisms for the decarboxylase and hydratase activities. The results also provide additional evidence supporting the hypothesis that MSAD and trans-3-chloroacrylic acid dehalogenase, a tautomerase superfamily member preceding MSAD in the trans-1,3-dichloropropene degradation pathway, diverged from a common ancestor but retained the key elements for the conjugate addition of water."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.org/dc/terms/identifier"doi:10.1021/bi051383m"xsd:string
http://purl.uniprot.org/citations/16274229http://purl.org/dc/terms/identifier"doi:10.1021/bi051383m"xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Hackert M.L."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Hackert M.L."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Johnson W.H. Jr."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Whitman C.P."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Whitman C.P."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Almrud J.J."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Almrud J.J."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Poelarends G.J."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Poelarends G.J."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Johnson W.H."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Serrano H."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/author"Serrano H."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/pages"14818-14827"xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/pages"14818-14827"xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/title"Crystal structures of the wild-type, P1A mutant, and inactivated malonate semialdehyde decarboxylase: a structural basis for the decarboxylase and hydratase activities."xsd:string
http://purl.uniprot.org/citations/16274229http://purl.uniprot.org/core/title"Crystal structures of the wild-type, P1A mutant, and inactivated malonate semialdehyde decarboxylase: a structural basis for the decarboxylase and hydratase activities."xsd:string
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