All Outputs (45)

Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: Ketimine and pyridoxamine phosphate forms (2002)
Journal Article
Yennawar, N. H., Conway, M. E., Yennawar, H. P., Farber, G. K., & Hutson, S. M. (2002). Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: Ketimine and pyridoxamine phosphate forms. Biochemistry, 41(39), 11592-11601. https://doi.org/10.1021/bi020221c

The three-dimensional structures of the isoleucine ketimine and the pyridoxamine phosphate forms of human mitochondrial branched chain aminotransferase (hBCATm) have been determined crystallographically at 1.9 Å resolution. The hBCATm-catalyzed trans... Read More about Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: Ketimine and pyridoxamine phosphate forms.

A continuous 96-well plate spectrophotometric assay for branched-chain amino acid aminotransferases (2002)
Journal Article
Cooper, A. J. L., Conway, M., & Hutson, S. M. (2002). A continuous 96-well plate spectrophotometric assay for branched-chain amino acid aminotransferases. Analytical Biochemistry, 308(1), 100-105. https://doi.org/10.1016/S0003-2697%2802%2900243-9

A new, continuous 96-well plate spectrophotometric assay for the branched-chain amino acid aminotransferases is described. Transamination of L-leucine with α-ketoglutarate results in formation of α-ketoisocaproate, which is reductively aminated back... Read More about A continuous 96-well plate spectrophotometric assay for branched-chain amino acid aminotransferases.

Identification of a peroxide-sensitive redox switch at the CXXC motif in the human mitochondrial branched chain aminotransferase (2002)
Journal Article
Conway, M. E., Yennawar, N., Wallin, R., Poole, L. B., & Hutson, S. M. (2002). Identification of a peroxide-sensitive redox switch at the CXXC motif in the human mitochondrial branched chain aminotransferase. Biochemistry, 41(29), 9070-9078. https://doi.org/10.1021/bi020200i

The human mitochondrial branched chain aminotransferase isoenzyme (hBCATm) must be stored in a reducing environment to remain active. Oxidation or labeling of hBCATm with sulfhydryl reagents results in enzyme inhibition. In this study, we investigate... Read More about Identification of a peroxide-sensitive redox switch at the CXXC motif in the human mitochondrial branched chain aminotransferase.

Role of specific aminotransferases in de novo glutamate synthesis and redox shuttling in the retina (2001)
Journal Article
LaNoue, K., Berkich, D., Conway, M. E., Barber, A., Hu, L., Taylor, C., & Hutson, S. M. (2001). Role of specific aminotransferases in de novo glutamate synthesis and redox shuttling in the retina. Journal of Neuroscience Research, 66(5), 914-922

In this study aminotransferase inhibitors were used to determine the relative importance of different aminotransferases in providing nitrogen for de novo glutamate synthesis in the retina. Aminooxyacetate, which inhibits all aminotransferases, blocke... Read More about Role of specific aminotransferases in de novo glutamate synthesis and redox shuttling in the retina.

The structure of human mitochondrial branched-chain aminotransferase (2001)
Journal Article
Farber, G., Hutson, S., Yennawar, N., Conway, M., Dunbar, J., Hutson, S. M., & Farber, J. (2001). The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallographica Section D: Biological Crystallography, 57(4), 506-515. https://doi.org/10.1107/S0907444901001925

X-ray crystal structures of three forms of human mitochondrial branched-chain aminotransferase were solved by molecular-replacement methods. In two of the forms the enzyme is in its active form, with the pyridoxal 5′-phosphate (PLP) cofactor covalent... Read More about The structure of human mitochondrial branched-chain aminotransferase.