Publications by authors named "Peter E Peterson"

3 Publications

  • Page 1 of 1

A perspective on errors, bias, and interpretation in the forensic sciences and direction for continuing advancement.

J Forensic Sci 2009 Jul 26;54(4):798-809. Epub 2009 May 26.

FBI Laboratory, 2501 Investigation Parkway, Quantico, VA 22135, USA.

The forensic sciences are under review more so than ever before. Such review is necessary and healthy and should be a continuous process. It identifies areas for improvement in quality practices and services. The issues surrounding error, i.e., measurement error, human error, contextual bias, and confirmatory bias, and interpretation are discussed. Infrastructure is already in place to support reliability. However, more definition and clarity of terms and interpretation would facilitate communication and understanding. Material improvement across the disciplines should be sought through national programs in education and training, focused on science, the scientific method, statistics, and ethics. To provide direction for advancing the forensic sciences a list of recommendations ranging from further documentation to new research and validation to education and to accreditation is provided for consideration. The list is a starting point for discussion that could foster further thought and input in developing an overarching strategic plan for enhancing the forensic sciences.
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http://dx.doi.org/10.1111/j.1556-4029.2009.01081.xDOI Listing
July 2009

Kinetic and crystallographic analysis of active site mutants of Escherichia coli gamma-aminobutyrate aminotransferase.

Biochemistry 2005 Mar;44(8):2982-92

Department of Chemistry, University of California-Davis, Davis, California 95616, USA.

The E. coli isozyme of gamma-aminobutyrate aminotransferase (GABA-AT) is a tetrameric pyridoxal phosphate-dependent enzyme that catalyzes transamination between primary amines and alpha-keto acids. The roles of the active site residues V241, E211, and I50 in the GABA-AT mechanism have been probed by site-directed mutagenesis. The beta-branched side chain of V241 facilitates formation of external aldimine intermediates with primary amine substrates, while E211 provides charge compensation of R398 selectively in the primary amine half-reaction and I50 forms a hydrophobic lid at the top of the substrate binding site. The structures of the I50Q, V241A, and E211S mutants were solved by X-ray crystallography to resolutions of 2.1, 2.5, and 2.52 A, respectively. The structure of GABA-AT is similar in overall fold and active site structure to that of dialkylglycine decarboxylase, which catalyzes both transamination and decarboxylation half-reactions in its normal catalytic cycle. Therefore, an attempt was made to convert GABA-AT into a decarboxylation-dependent aminotransferase similar to dialkylglycine decarboxylase by systematic mutation of E. coli GABA-AT active site residues. Two of the twelve mutants presented, E211S/I50G/C77K and E211S/I50H/V80D, have approximately 10-fold higher decarboxylation activities than the wild-type enzyme, and the E211S/I50H/V80D has formally changed the reaction specificity to that of a decarboxylase.
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http://dx.doi.org/10.1021/bi048657aDOI Listing
March 2005

Crystal structures of unbound and aminooxyacetate-bound Escherichia coli gamma-aminobutyrate aminotransferase.

Biochemistry 2004 Aug;43(34):10896-905

Department of Chemistry, University of California, Davis, California 95616, USA.

The X-ray crystal structures of Escherichia coli gamma-aminobutyrate aminotransferase unbound and bound to the inhibitor aminooxyacetate are reported. The enzyme crystallizes from ammonium sulfate solutions in the P3(2)21 space group with a tetramer in the asymmetric unit. Diffraction data were collected to 2.4 A resolution for the unliganded enzyme and 1.9 A resolution for the aminooxyacetate complex. The overall structure of the enzyme is similar to those of other aminotransferase subgroup II enzymes. The ability of gamma-aminobutyrate aminotransferase to act on primary amine substrates (gamma-aminobutyrate) in the first half-reaction and alpha-amino acids in the second is proposed to be enabled by the presence of Glu211, whose side chain carboxylate alternates between interactions with Arg398 in the primary amine half-reaction and an alternative binding site in the alpha-amino acid half-reaction, in which Arg398 binds the substrate alpha-carboxylate. The specificity for a carboxylate group on the substrate side chain is due primarily to the presence of Arg141, but also requires substantial local main chain rearrangements relative to the structurally homologous enzyme dialkylglycine decarboxylase, which is specific for small alkyl side chains. No iron-sulfur cluster is found in the bacterial enzyme as was found in the pig enzyme [Storici, P., De Biase, D., Bossa, F., Bruno, S., Mozzarelli, A., Peneff, C., Silverman, R. B., and Schirmer, T. (2004) J. Biol. Chem. 279, 363-73.]. The binding of aminooxyacetate causes remarkably small changes in the active site structure, and no large domain movements are observed. Active site structure comparisons with pig gamma-aminobutyrate aminotransferase and dialkylglycine decarboxylase are discussed.
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http://dx.doi.org/10.1021/bi049218eDOI Listing
August 2004