2.6.1.B16	evolution	along with the structure-based classifications, a more practical system groups TAs into two groups according based on the relative position of the amino group being transferred: alpha-transaminases (alpha-TAs) and omega-transaminases (omega-TAs). While the former exclusively transfers amino groups at alpha-position relative to the carbonyl functionality (e.g. alpha-amino acids, alpha-ketoacids), the latter are able to transfer amino groups from substrates bearing it at two or more positions away from the carbonyl moiety (e.g.omega-amino acids). Depending on the selectivity, enantiopure R- and S-amines can be synthetized. This feature is derived from the two naturally occurring fold-types of transaminases, being those belonging to fold-type I known as (S)-ATAs whilst those from fold-type IV are known as (R)-ATAs. Phylogenetic analysis	-, 759132	
2.6.1.B16	evolution	the ATA enzyme from Ruegeria sp. TM1040 (Rsp-ATA, PDB ID 3FCR) belongs to the ATAs of fold class I	759050	
2.6.1.B16	evolution	the enzyme belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family	758672	
2.6.1.B16	evolution	the enzyme has a high sequence identity to a fold type I class III transaminase from Pseudomonas fluorescens	758672	
2.6.1.B16	evolution	there are two types of TAs, alpha-transaminases, which convert alpha-amino and alpha-keto acids, and omega-transaminases (omegaTAs), which also accept amino and keto acids in which the amino or keto group is in a non-alpha position relative to the carboxyl group, called omega-amino or omega-keto acids, respectively	758577	
2.6.1.B16	additional information	four mutants of the amine transaminase from Halomonas elongata are generated by an in silico-based design and recombinantly produced in Escherichia coli, purified, and applied to the amination of mono-substituted aromatic carbonyl-derivatives. While benzaldehyde derivatives are excellent substrates, only NO2-acetophenones are transformed into the (S)-amine with a high enantioselectivity. The different behaviour of wild-type and mutated transaminases is assessed by in silico substrate binding mode studies, overview	759888	
2.6.1.B16	additional information	homology structure modelling of ATA_SLM16 using the crystal structure of the (S)-omega-TA from chromobacterium violaceum (PDB ID 4BA5) as template	-, 759132	
2.6.1.B16	additional information	quantum chemical study of dual-substrate recognition in omega-transaminase. The reaction mechanism for the half-transamination of L-alanine to pyruvate in (S)-selective Chromobacterium violaceum omega-transaminase is investigated using density functional theory calculations. The role of a flexible arginine residue, Arg416, in the dual-substrate recognition is revealed using two different active site models, one including this residue and one lacking it. Molecular docking and molecular dynamics simulations, active site modeling, overview. The amino acids that make up the binding site are Phe22, Leu59, Trp60, Phe88', Tyr153, Ile262, and Thr321', as well as Gly230 and Ala231 and the backbone between them	758577	
2.6.1.B16	additional information	sequence-structure-function relationship	758672	
2.6.1.B16	additional information	structure-function analysis, molecular dynamics simulations, and molecular modeling of substrate recognition. Residue W56 is the only residue in direct contact with alanine's carboxylate. Residue R162, pointing towards the substrate from the active site's entrance is binding the carboxylate indirectly via two water molecules	758672	
2.6.1.B16	physiological function	amine-transaminases (ATAs) are enzymes that catalyze the reversible transfer of an amino group between primary amines and carbonyl compounds	-, 759132	
2.6.1.B16	physiological function	transaminases (TAs) catalyze the reversible interchange of amino and keto groups, by the use of the coenzyme pyridoxal-5'-phosphate (PLP)	758577	
2.6.1.B16	physiological function	transaminases play a central role in the biocatalytic preparation of enantiopure amines and amino acids, challenging reactions to achieve by conventional synthesis	759320