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Properties of Dipeptidyl Arylamidase I of the Pituitary

CHLORIDE AND SULFHYDRYL ACTIVATION OF SERYLTYROSYL-{beta}-NAPHTHYLAMIDE HYDROLYSIS

J. Ken McDonald 1, Stanley Ellis 1, and Thomas J. Reilly 1

From the 1 From the Environmental Biology Division, Ames Research Center, National Aeronautics and Space Administration, Moffett Field, California

Extracts of bovine anterior pituitary tissue were found to contain enzymes which cleaved dipeptides from ß-naphthylamide derivatives between pH 3 and 7. The pH optimum for the release of Ser-Tyr from Ser-Tyr-ß-naphthylamide was pH 4, whereas at neutrality this substrate was hydrolyzed stepwise from the NH2 terminus. The enzyme catalyzing the dipeptidyl cleavage of Ser-Tyr-ß-naphthylamide, referred to as "dipeptidyl arylamidase I," showed an absolute requirement for Cl- and contained —SH groups which were essential for activity.

By fractionation with (NH4)2SO4, a separate enzyme was demonstrated which cleaved Lys-Ala from Lys-Ala-ß-naphthylamide. This enzyme, referred to as "dipeptidyl arylamidase II," required neither Cl- nor —SH for activity.

On the basis of chloride requirements, the pituitary enzyme hydrolyzing Ser-Tyr-ß-naphthylamide at pH 4 may have been responsible for the observed cleavage of Ser-Tyr from the NH2-terminal decapeptide of adrenocorticotropic hormone at pH 4.

The Ser-Tyr arylamidase was distinguished from the pituitary enzyme, which cleaves Ser-Met from Ser-Met-Glu, and from the glucagon-degrading enzyme, which has similar Cl- and —SH requirements.

Submitted on September 27, 1965


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