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B6db references: 26872794

type Journal Article
authors Boyko KM, Stekhanova TN, Nikolaeva AY, Mardanov AV, Rakitin AL, Ravin NV, Bezsudnova EY, Popov VO
title First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for L-amino acids and R-amines
journal Extremophiles
Activity tuzn1299
Family tuzn1299
sel selected
ui 26872794
year (2016)
volume 20
number 2
pages 215-25
keywords 3D structure; Archaea; Branched-chain amino acid aminotransferase; Selectivity; Thermostability
abstract 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 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.
last changed 2017/12/22 08:39

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