LOGIN TO YOUR ACCOUNT

Username
Password
Remember Me
Or use your Academic/Social account:

CREATE AN ACCOUNT

Or use your Academic/Social account:

Congratulations!

You have just completed your registration at OpenAire.

Before you can login to the site, you will need to activate your account. An e-mail will be sent to you with the proper instructions.

Important!

Please note that this site is currently undergoing Beta testing.
Any new content you create is not guaranteed to be present to the final version of the site upon release.

Thank you for your patience,
OpenAire Dev Team.

Close This Message

CREATE AN ACCOUNT

Name:
Username:
Password:
Verify Password:
E-mail:
Verify E-mail:
*All Fields Are Required.
Please Verify You Are Human:
fbtwitterlinkedinvimeoflicker grey 14rssslideshare1
Conway, M. E.; Hutson, S. (2015)
Publisher: Springer
Languages: English
Types: Part of book or chapter of book
Subjects:
Key Points\ud • The branched chain aminotransferases (BCAT) 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. \ud • Structurally the BCAT proteins are homodimers, where the active site between each isoform is largely conserved. \ud • The cytosolic and mitochondrial isoforms show cell and tissue specific expression where the aminotransferase proteins play an integrated role in shuttling metabolites between cells and tissues.\ud • These anaplerotic shuttles interface with core metabolic pathways and protein complexes such as the branched-chain α-keto acid dehydrogenase complex and glutamate dehydrogenase, respectively, indicating a role in the regeneration of key metabolites such as the primary neurotransmitter glutamate. \ud • Leucine is a nutrient signal and involved in mTOR signalling, which controls the synthesis of cellular protein levels.\ud • Moreover, the BCAT proteins have a unique redox active CXXC motif regulated through changes in the redox environment, likely to play a key role in this signalling mechanism. \ud • Site-directed mutagenesis studies have identified that the N-terminal cysteine acts as the ‘redox sensor’ and the C-terminal cysteine as its resolving partner, which permits reversible regulation.\ud • Oxidation, S-nitrosation and S-glutathionylation are important redox regulators of BCAT activity and are reversibly controlled through the glutaredoxin/glutathione system.\ud • Biochemical and X-ray crystallography studies of the redox-active mutant proteins describe the importance of the N-terminal cysteine in the orientation of the substrate and its interaction with key residues of the interdomain loop.

Share - Bookmark

Cite this article