[Effect of chemical modification and carboxylate anions on transamination of phenylalanine and alanine in the active center of chicken cytosol aspartate transaminase].
Photooxidation of a histidine residue in aspartate transaminase leads to proportionate loss of the enzyme activity in reactions with L-aspartate and L-phenylalanine. Modification of two arginine residues by 1,2-cyclohexanedione strongly inhibits transamination of aspartate but, in contrast, slightly increases the rate of phenylalanine transamination. A stimulatory effect of a number of aromatic and aliphatic monocarboxylate anions on the rate of alanine transamination in the active site was observed. Indolylbutyrate was the most effective compound among those tested. Indolylbutyrate and indolylacetate act as competitive inhibitors in the case of transamination of phenylalanine or aspartate. The results were interpreted as indicating the presence in the active center of transaminase of a hydrophobic subsite participating in the binding of aromatic aminoacids.
D000409:Alanine / Q000378:metabolism*; D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism* / Q000528:radiation effects; D001665:Binding Sites; D002264:Carboxylic Acids; D055598:Chemical Phenomena; D002621:Chemistry; D002645:Chickens; D003512:Cyclohexanones; D007700:Kinetics; D008027:Light; D010649:Phenylalanine / Q000378:metabolism*; D013379:Substrate Specificity
D002264:Carboxylic Acids; D003512:Cyclohexanones; D010649:Phenylalanine; D001219:Aspartate Aminotransferases; D000409:Alanine
Vliianie khimicheskoĭ modifikatsii i karboksilat-anionov na transaminirovanie fenilalanina i alanina v aktivnom tsentre tsitozol'noĭ aspartat-transaminazy kur.