α‐Aminophosphonous acids: the substrates of ATP—PP_i exchange reaction, catalysed by aminoacyl‐tRNA synthetases

Interaction of tyrosine phenol‐lyase with phosphoroorganic analogues of substrate amino acids

“…Phosphororganic analogues of amino acids ( I , R = Alk, X = H, OH) are known to display high biological activities [1–7], thus investigation of their interaction with the enzymes involved in amino‐acid transformations is useful for understanding the enzymatic mechanisms and creating new probes for studies in this field.…”

“…It may be concluded that differences in structure and chemical properties between (HO) 2 (O)P and HOOC groups are very important for the factors controlling the substrate specificities of the respective enzymes. For the groups (HO)(O)PH and HOOC, the differences are less pronounced, and aminophosphinic acids ( I , R = Alk, X = H) are considered to be closer analogues of natural amino acids [4,5]. For example, the phosphinic analogue of methionine ( I , R = CH 3 S CH 2 CH 2 , X = H) is a much better competitive inhibitor of enzymic aminoacylation of tRNA and it is a substrate of the ATP–PP i exchange reaction, the first stage of this process [4].…”

“…For the groups (HO)(O)PH and HOOC, the differences are less pronounced, and aminophosphinic acids ( I , R = Alk, X = H) are considered to be closer analogues of natural amino acids [4,5]. For example, the phosphinic analogue of methionine ( I , R = CH 3 S CH 2 CH 2 , X = H) is a much better competitive inhibitor of enzymic aminoacylation of tRNA and it is a substrate of the ATP–PP i exchange reaction, the first stage of this process [4]. The phosphinic analogues of aspartic ( I , R = HOOCCH 2 , X = H) and glutamic ( I , R = HOOCCH 2 CH 2 , X = H) acids are good substrates of transformation of aldimine form to ketamino form of aspartate aminotransferase [6].…”

Interaction of tyrosine phenol-lyase with phosphoroorganic analogues of substrate amino acids

“…It may be concluded that differences in structure and chemical properties between (HO) 2 (O)P and HOOC groups are very important for the factors controlling the substrate specificities of the respective enzymes. For the groups (HO)(O)PH and HOOC, the differences are less pronounced, and aminophosphinic acids (I, R Alk, X H) are considered to be closer analogues of natural amino acids [4,5]. For example, the phosphinic analogue of methionine (I, R CH 3 SCH 2 CH 2 , X H) is a much better competitive inhibitor of enzymic aminoacylation of tRNA and it is a substrate of the ATP±PP i exchange reaction, the first stage of this process [4].…”

“…For the groups (HO)(O)PH and HOOC, the differences are less pronounced, and aminophosphinic acids (I, R Alk, X H) are considered to be closer analogues of natural amino acids [4,5]. For example, the phosphinic analogue of methionine (I, R CH 3 SCH 2 CH 2 , X H) is a much better competitive inhibitor of enzymic aminoacylation of tRNA and it is a substrate of the ATP±PP i exchange reaction, the first stage of this process [4]. The phosphinic analogues of aspartic (I, R HOOCCH 2 , X H) and glutamic (I, R HOOCCH 2 CH 2 , X H) acids are good substrates of transformation of aldimine form to ketamino form of aspartate aminotransferase [6].…”