Interactions between alpha-amino acids and cobalt(II) bovine-carbonic anhydrase.
The results of a study on the interaction between cobalt(II) bovine carbonic anhydrase and the alpha-amino acids L(+) and D(-)alanine, glycine and betaine are reported. L(+)alanine and glycine have been found to have larger affinity for the enzyme than D(-)alanine whereas no sizable affinity is shown by betaine. The electronic spectra indicate that these systems are similar to that containing the acetate ion. Utilizing the inhibition properties of L(+)alanine at various pH an analysis of the species involved in the inhibition reaction is presented.
D000409:Alanine / Q000494:pharmacology*; D000818:Animals; D002256:Carbonic Anhydrases / Q000378:metabolism*; D002417:Cattle; D003035:Cobalt / Q000494:pharmacology*; D005998:Glycine / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D008954:Models, Biological; D011485:Protein Binding; D013053:Spectrophotometry
D003035:Cobalt; D002256:Carbonic Anhydrases; D000409:Alanine; D005998:Glycine