All Outputs (31)

Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins (2008)
Journal Article
Conway, M. E., Coles, S. J., Islam, M. M., & Hutson, S. M. (2008). Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins. Biochemistry, 47(19), 5465-5479. https://doi.org/10.1021/bi800303h

Redox regulation of proteins through oxidation and S-thiolation are important regulatory processes, acting in both a protective and adaptive role in the cell. In the current study, we investigated the sensitivity of the neuronal human cytosolic branc... Read More about Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins.

A novel branched-chain amino acid metabolon: Protein-protein interactions in a supramolecular complex (2007)
Journal Article
Islam, M. M., Wallin, R., Wynn, R. M., Conway, M., Fujii, H., Mobley, J. A., …Hutson, S. M. (2007). A novel branched-chain amino acid metabolon: Protein-protein interactions in a supramolecular complex. Journal of Biological Chemistry, 282(16), 11893-11903. https://doi.org/10.1074/jbc.M700198200

The catabolic pathways of branched-chain amino acids have two common steps. The first step is deamination catalyzed by the vitamin B6-dependent branched-chain aminotransferase isozymes (BCATs) to produce branched-chain α-keto acids (BCKAs). The secon... Read More about A novel branched-chain amino acid metabolon: Protein-protein interactions in a supramolecular complex.

Human mitochondrial branched chain aminotransferase isozyme: Structural role of the CXXC center in catalysis (2006)
Journal Article
Conway, M., Islam, M. M., Yennawar, N. H., Islam, M. M., Conway, M. E., Wallin, R., & Hutson, S. M. (2006). Human mitochondrial branched chain aminotransferase isozyme: Structural role of the CXXC center in catalysis. Journal of Biological Chemistry, 281(51), 39660-39671. https://doi.org/10.1074/jbc.M607552200

Mammalian branched chain aminotransferases (BCATs) have a unique CXXC center. Kinetic and structural studies of three CXXC center mutants (C315A, C318A, and C315A/C318A) of human mitochondrial (hBCATm) isozyme and the oxidized hBCATm enzyme (hBCATm-O... Read More about Human mitochondrial branched chain aminotransferase isozyme: Structural role of the CXXC center in catalysis.

Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin (2005)
Journal Article
Yennawar, N., Goto, M., Miyahara, I., Hirotsu, K., Conway, M., Islam, M. M., & Hutson, S. M. (2005). Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. Journal of Biological Chemistry, 280(44), 37246-37256. https://doi.org/10.1074/jbc.M506486200

This study presents the first three-dimensional structures of human cytosolic branched-chain aminotransferase (hBCATc) isozyme complexed with the neuroactive drug gabapentin, the hBCATc Michaelis complex with the substrate analog, 4-methylvalerate, a... Read More about Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin.

Roles for cysteine residues in the regulatory CXXC motif of human mitochondrial branched chain aminotransferase enzyme (2004)
Journal Article
Conway, M. E., Poole, L. B., & Hutson, S. M. (2004). Roles for cysteine residues in the regulatory CXXC motif of human mitochondrial branched chain aminotransferase enzyme. Biochemistry, 43(23), 7356-7364. https://doi.org/10.1021/bi0498050

The redox-active dithiol/disulfide C315-Xaa-Xaa-C318 center has been implicated in the regulation of the human mitochondrial branched chain aminotransferase isozyme (hBCATm) [Conway, M. E., Yennawar, N., Wallin, R., Poole, L. B., and Hutson, S. M. (2... Read More about Roles for cysteine residues in the regulatory CXXC motif of human mitochondrial branched chain aminotransferase enzyme.

Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate β-lyases, but turnover leads to inactivation (2003)
Journal Article
Cooper, A. J. L., Bruschi, S. A., Conway, M., & Hutson, S. M. (2003). Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate β-lyases, but turnover leads to inactivation. Biochemical Pharmacology, 65(2), 181-192. https://doi.org/10.1016/S0006-2952%2802%2901513-7

The mitochondrial and cytosolic branched-chain aminotransferases (BCATm and BCATc) are homodimers in the fold type IV class of pyridoxal 5′-phosphate-containing enzymes that also contains D-amino acid aminotransferase and 4-amino-4-deoxychorismate ly... Read More about Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate β-lyases, but turnover leads to inactivation.

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.