EC Number   |
General Information |
Reference |
|---|
    2.6.1.42 | evolution |
branched-chain amino acid aminotransferases (BCATs) belong to fold-type IV class of PLP enzymes and are referred to as alpha-aminotransferases. Sequence alignment reveals two motifs (V/I)xLDxR and PFG(K/H)YL characteristic of BCATs from species of the related genera Vulcanisaeta, Pyrobaculum and Thermoproteus that might be responsible for the unique substrate recognition profile of the enzyme |
-, 759134 |
| 2.6.1.42 | evolution |
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis |
-, 758768 |
| 2.6.1.42 | evolution |
the enzyme belongs to the PLP fold type IV transaminases |
-, 759531 |
| 2.6.1.42 | evolution |
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases |
-, 758848 |
| 2.6.1.42 | evolution |
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G |
-, 759127 |
| 2.6.1.42 | evolution |
the enzyme belongs to the PLP-dependent fold-type IV branched-chain amino acid aminotransferases (BCATs) from archaea, docking study and identification of subfamily-specific positions, overview |
-, 758697 |
| 2.6.1.42 | malfunction |
because deletion of BAT1 only slightly affects cell growth in the absence of externally supplied BCAAs (isoleucine, leucine, valine) and deletion of BAT2 has no effect, mitochondrial carriers must exist to transport branched-chain 2-oxo acids and amino acids from the mitochondria to the cytosol. In contrast, strains with both BAT1 and BAT2 deleted are auxotrophic for BCAAs |
-, 759717 |
| 2.6.1.42 | malfunction |
deletion of BAT1 alone increases isobutanol production by 14.2fold compared to wild-type strains in media lacking valine, interactions between valine and the regulatory protein Ilv6p affect isobutanol production. Compartmentalizing the five-gene isobutanol biosynthetic pathway in mitochondria of BAT1 deletion strains results in an additional 2.1-fold increase in isobutanol production in the absence of valine. While valine inhibits isobutanol production, it boosts 2-methyl-1-butanol production. Because deletion of BAT1 only slightly affects cell growth in the absence of externally supplied BCAAs (isoleucine, leucine, valine) and deletion of BAT2 has no effect, mitochondrial carriers must exist to transport branched-chain 2-oxo acids and amino acids from the mitochondria to the cytosol. In contrast, strains with both BAT1 and BAT2 deleted are auxotrophic for BCAAs. Bat1 overexpression phenotype, overview |
-, 759717 |
| 2.6.1.42 | malfunction |
isozymes CsBCAT2 and CsBCAT3 restore the growth of a bat1DELTA/bat2DELTA double knockout Saccharomyces cerevisiae strain, and isozymes CsBCAT3 and CsBCAT7, that show different substrate preferences, act in a reverse reaction. The transgenic approach demonstrates that the overexpression of the three CsBCATs results in early flowering phenotypes, which are associated with the upregulation of FLOWERING LOCUS T (FT) and SUPPRESSOR OF OVEREXPRESSION OF CONSTANS1 (SOC1) in a manner in which they are dependent on GIGANTEA (GI)/CONSTANS (CO) and SHORT VEGETATIVE PHASE (SVP)/FLOWERING LOCUS C (FLC) modules. The overexpressed CsBCAT isozymes with BCAT enzymatic activities affect the flowering time in transgenic Arabidopsis thaliana |
759947 |
| 2.6.1.42 | malfunction |
knockdown of BCAT1 represses the growth rate and colony formation capacity of breast cancer cells, opposing results are observed when BCAT1 is overexpressed. BCAT1 can promote mitochondrial biogenesis, ATP production and repress mitochondrial ROS in breast cancer cells by regulating the expression of related genes. BCAA catabolism is activated in human breast cancer, and abolishment of BCAA catabolism by knocking down BCAT1 inhibits breast cancer cell growth by repressing mTOR-mediated mitochondrial biogenesis and function. BCAT1 overexpression is unable to affect the mRNA levels of the genes involved in mitochondrial biogenesis (PGC1alpha, NRF-1, Tfam, and beta-F1-ATPase) and oxidative stress (SOD1, SOD2, catalase, and Gpx1) |
758728 |
