All Outputs (39)

Distribution of the branched chain aminotransferase proteins in the human brain and their role in glutamate regulation (2012)
Journal Article

The branched chain aminotransferase enzymes (BCAT) serve as nitrogen donors for the production of 30% of de novo glutamate synthesis in rat brain. Despite the importance of this major metabolite and excitatory neurotransmitter, the distribution of BC... Read More about Distribution of the branched chain aminotransferase proteins in the human brain and their role in glutamate regulation.

Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase (2012)
Journal Article

The human branched-chain aminotransferase (hBCAT) isoenzymes are CXXC motif redox sensitive homodimers central to glutamate metabolism in the central nervous system. These proteins respond differently to oxidation by H 2O 2, NO, and S-glutathionylati... Read More about Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase.

Aminotransferases (2011)
Book Chapter

The aminotransferases are PLP dependent proteins which catalyze the transfer of an amino group from the donor amino acid to α-ketoglutarate, forming glutamate and the respective keto acids. Several key aminotransferase proteins have been identified a... Read More about Aminotransferases.

S-nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and s-thiolation (2009)
Journal Article

Specific proteins with reactive thiol(ate) groups are susceptible to nitric oxide (NO) modification, which can result in S-nitrosation, S-thiolation, or disulfide bond formation. In the present study the effect of NO modification on the functionality... Read More about S-nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and s-thiolation.

S-Nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation (2009)
Journal Article

Specific proteins with reactive thiol(ate) groups are susceptible to nitric oxide (NO) modification, which can result in S-nitrosation, S-thiolation, or disulfide bond formation. In the present study the effect of NO modification on the functionality... Read More about S-Nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation.

Redox regulation and trapping sulfenic acid in the peroxide-sensitive human mitochondrial branched chain aminotransferase (2009)
Book Chapter

The human branched chain aminotransferase enzymes are key regulators of glutamate metabolism in the brain and are among a growing number of redox-sensitive proteins. Studies that use thiol-specific reagents and electrospray ionization mass spectromet... Read More about Redox regulation and trapping sulfenic acid in the peroxide-sensitive human mitochondrial branched chain aminotransferase.

Redox regulation and trapping sulphenic acid in the peroxide sensitive human mitochondrial branched chain aminotransferase (2008)
Journal Article

The human branched chain aminotransferase enzymes are key regulators of glutamate metabolism in the brain and are among a growing number of redox-sensitive proteins. Studies that use thiol-specific reagents and electrospray ionization mass spectromet... Read More about Redox regulation and trapping sulphenic acid in the peroxide sensitive human mitochondrial branched chain aminotransferase.

Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins (2008)
Journal Article

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

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

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

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

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

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

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

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

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

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

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.

Human mitochondrial branched chain aminotransferase: Structural basis for substrate specificity and role of redox active cysteines
Presentation / Conference Contribution

Crystal structures of the fold type IV pyridoxal phosphate (PLP)-dependent human mitochondrial branched chain aminotransferase (hBCATm) reaction intermediates have provided a structural explanation for the kinetically determined substrate specificity... Read More about Human mitochondrial branched chain aminotransferase: Structural basis for substrate specificity and role of redox active cysteines.