Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase

Acta Biochimica et Biophysica Sinica

Volumn 44, Issue 2, 2012, Pages 172-176

  Coles, Steven J ^a   Hancock, John T ^b   Conway, Myra E ^b  

^a CARDIFF UNIVERSITY   (United Kingdom)

^b UNIVERSITY OF THE WEST OF ENGLAND   (United Kingdom)

Author keywords

branched chain aminotransferase; glutathione; Nernst equation; redox potential

Indexed keywords

AMINOTRANSFERASE; BCAT1 PROTEIN, HUMAN; BCAT2 PROTEIN, HUMAN; GLUTATHIONE; GLUTATHIONE DISULFIDE; PLACENTA PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; CHEMISTRY; COMPARATIVE STUDY; CYTOSOL; ENZYMOLOGY; GENETICS; HUMAN; IN VITRO STUDY; METABOLISM; MITOCHONDRION; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PROTEIN MOTIF;

AMINO ACID MOTIFS; CYTOSOL; GLUTATHIONE; GLUTATHIONE DISULFIDE; HUMANS; MITOCHONDRIA; OXIDATION-REDUCTION; OXIDATIVE STRESS; PREGNANCY PROTEINS; RECOMBINANT PROTEINS; TRANSAMINASES;

EID: 84856442668     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gmr103     Document Type: Article

References (22)

1. Hutson S. Structure and function of branched chain aminotransferases. Prog Nucleic Acid Res Mol Biol 2001, 70: 175-206.
2. Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM and Hutson SM. Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. J Biol Chem 2005, 280: 37246-37256.
3. Coles SJ, Easton P, Sharrod H, Hutson SM, Hancock J, Patel VB and Conway ME. S-Nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation. Biochemistry 2009, 48: 645-656.
4. Conway ME, Coles SJ, Islam MM and Hutson SM. Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins. Biochemistry 2008, 47: 5465-5479.
5. Schafer FQ and Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 2001, 30: 1191-1212.
6. Maher P. The effects of stress and aging on glutathione metabolism. Ageing Res Rev 2005, 4: 288-314.
7. Choi C, Zhao C, Dimitrov I, Douglas D, Coupland NJ, Kalra S and Hawesa H, et al. Measurement of glutathione in human brain at 3T usingan improved double quantum filter in vivo. J Magn Reson 2009, 198: 160-166.
8. Trabesinger AH, Weber OM, Duc CO and Boesiger P. Detection of glutathione in the human brain in vivo by means of double quantum coherence filtering. Magn Reson Med 1999, 42: 283-289.
9. Rost J and Rapoport S. Reduction-potential of glutathione. Nature 1964, 201: 185.
10. Davoodi J, Drown PM, Bledsoe RK, Wallin R, Reinhart GD and Hutson SM. Overexpression and characterization of the human mitochondrial and cytosolic branched-chain aminotransferases. J Biol Chem 1998, 273: 4982-4989.
11. Simonian NA and Coyle JT. Oxidative stress in neurodegenerative diseases. Annu Rev Pharmacol Toxicol 1996, 36: 83-106.
12. Conway ME, Yennawar N, Wallin R, Poole LB and Hutson SM. Identification of a peroxide-sensitive redox switch at the CXXC motif in the human mitochondrial branched chain aminotransferase. Biochemistry 2002, 41: 9070-9078.
13. Watson WH, Pohl J, Montfort WR, Stuchlik O, Reed MS, Powis G and Jones DP. Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif. J Biol Chem 2003, 278: 33408-33415.
14. Holmgren A and Fagerstedt M. The in vivo distribution of oxidized and reduced thioredoxin in Escherichia coli. J Biol Chem 1982, 257: 6926-6930.
15. Chivers PT, Prehoda KE and Raines RT. The CXXC motif: A rheostat in the active site. Biochemistry 1997, 36: 4061-4066.
16. Carvalho AT, Fernandes PA and Ramos MJ. Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA. J Comput Chem 2006, 27: 966-975.
17. Yennawar NH, Islam MM, Conway M, Wallin R and Hutson SM. Human mitochondrial branched chain aminotransferase isozyme: Structural role of the CXXC center in catalysis. J Biol Chem 2006, 281: 39660-39671.
18. Dyson HJ, Jeng MF, Tennant LL, Slaby I, Lindell M, Cui DS and Kuprin S, et al. Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp 26 and Lys 57. Biochemistry 1997, 36: 2622-2636.
19. Islam MM, Wallin R, Wynn RM, Conway M, Fujii H, Mobley JA and Chuang DT, et al. A novel branched-chain amino acid metabolon. Protein-protein interactions in a supramolecular complex. J Biol Chem 2007, 282: 11893-11903.
20. Islam MM, Nautiyal M, Wynn RM, Mobley JA, Chuang DT and Hutson SM. Branched-chain amino acid metabolon: Interaction of glutamate dehydrogenase with the mitochondrial branched-chain aminotransferase (BCATm). J Biol Chem 2010, 285: 265-276.
21. Sagemark J, Elgan TH, Burglin TR, Johansson C, Holmgren A and Berndt KD. Redox properties and evolution of human glutaredoxins. Proteins 2007, 68: 879-892.
22. Beer SM, Taylor ER, Brown SE, Dahm CC, Costa NJ, Runswick MJ and Murphy MP. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant defense. J Biol Chem 2004, 279: 47939-47951.