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dc.contributor.authorLima, Santiago
dc.date.accessioned2014-03-04T03:21:21Z
dc.date.available2014-03-04T03:21:21Z
dc.date.issued2008-05
dc.identifier.otherlima_santiago_200805_phd
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/lima_santiago_200805_phd
dc.identifier.urihttp://hdl.handle.net/10724/24677
dc.description.abstractPyridoxal-5’-phosphate (PLP) dependent enzymes are a large and catalytically diversegroup of proteins primarily involved in the metabolism of amino acids, amino acid derived compounds, and amino sugars. In this work, three PLP-dependent enzymes, Homo sapiens kynureninase, Pseudomonas dacunhae L-aspartate-2-decarboxylase, and Pyrococcus furiosustryptophan synthase -subunit 2homolog are studied using a variety of biophysical methods. Thenovel crystal structures for these enzymes are presented, along with the structure of a kynureninase-inhibitor complex, and the analysis of a number of mutants generated to study specific structure activity relationships in them. The results of these analyses reveal the interactions that contribute to substrate specificity in kynureninase, a novel oligomerization scheme and catalytically important residues in aspartate-2-decarboxylase, and the elucidation of the kinetic properties of the P. furiosus tryptophan synthase 2-subunit homolog.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectpyridoxal-5'-phosphate
dc.subjectkynureninase
dc.subjectL-kynurenine hydrolase
dc.subject3-hydroxykynurenine
dc.subject2HZP
dc.subjectL-aspartate-beta-decarboxylase
dc.subjectaspartate-4-decarboxylase
dc.subjecttryptophan synthase beta subunit homolog
dc.subjecttrpb2
dc.subjecttryptophan synthase
dc.titleStructure activity relationships in pyridoxal-5'-phosphate dependent enzymes
dc.typeDissertation
dc.description.degreePhD
dc.description.departmentBiochemistry and Molecular Biology
dc.description.majorBiochemistry and Molecular Biology
dc.description.advisorRobert S. Phillips
dc.description.committeeRobert S. Phillips
dc.description.committeeBi-Cheng Wang
dc.description.committeeCory Momany
dc.description.committeeMichael W. W. Adams


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