Structural highlights
Publication Abstract from PubMed
The gene TUZN1299 from the genome of the hyperthermophilic archaeon Thermoproteus uzoniensis encoding a new 32.8 kDa branched-chain amino acid aminotransferase (BCAT) was expressed in Escherichia coli. The recombinant protein TUZN1299 was purified to homogeneity in the PLP-bound form. TUZN1299 was active towards branched-chain amino acids (L-Val, L-Leu, L-Ile) and showed low but detectable activity toward (R)-alpha-methylbenzylamine. The enzyme exhibits high-temperature optimum, thermal stability, and tolerance to organic solvents. The structure of an archaeal BCAT called TUZN1299 was solved for the first time (at 2.0 A resolution). TUZN1299 has a typical BCAT type IV fold, and the organization of its active site is similar to that of bacterial BCATs. However, there are some differences in the amino acid composition of the active site.
First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for L-amino acids and R-amines.,Boyko KM, Stekhanova TN, Nikolaeva AY, Mardanov AV, Rakitin AL, Ravin NV, Bezsudnova EY, Popov VO Extremophiles. 2016 Mar;20(2):215-25. doi: 10.1007/s00792-016-0816-z. Epub 2016, Feb 12. PMID:26872794[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boyko KM, Stekhanova TN, Nikolaeva AY, Mardanov AV, Rakitin AL, Ravin NV, Bezsudnova EY, Popov VO. First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for L-amino acids and R-amines. Extremophiles. 2016 Mar;20(2):215-25. doi: 10.1007/s00792-016-0816-z. Epub 2016, Feb 12. PMID:26872794 doi:http://dx.doi.org/10.1007/s00792-016-0816-z
