Isoenzymatic forms alfa2, alfa-beta, and beta2 of bovine seminal ribonuclease are generated by the transformation of beta-type into alfa-type subunit through deamidation of a single amide group. The residue involved in this selective deamidation has been identified as Asn67 . Deamidation occurs by formation of a cyclic imide intermediate involving the Gly at position 68. Opening of the cyclic imide may occur on either side of the nitrogen, generating both the normal alfa-aspartyl and an isoaspartyl residue at position 67. The alfa-carboxyl of the isoaspartyl residue is effectively methylated by bovine brain protein carboxylmethyltransferase.

Selective Deamidation and Enzymatic Methylation of Seminal Ribonuclease / DI DONATO, Alberto; Galletti, P.; D'Alessio, Giuseppe. - In: BIOCHEMISTRY. - ISSN 0006-2960. - STAMPA. - 25:(1986), pp. 8361-8368.

Selective Deamidation and Enzymatic Methylation of Seminal Ribonuclease

DI DONATO, ALBERTO;D'ALESSIO, GIUSEPPE
1986

Abstract

Isoenzymatic forms alfa2, alfa-beta, and beta2 of bovine seminal ribonuclease are generated by the transformation of beta-type into alfa-type subunit through deamidation of a single amide group. The residue involved in this selective deamidation has been identified as Asn67 . Deamidation occurs by formation of a cyclic imide intermediate involving the Gly at position 68. Opening of the cyclic imide may occur on either side of the nitrogen, generating both the normal alfa-aspartyl and an isoaspartyl residue at position 67. The alfa-carboxyl of the isoaspartyl residue is effectively methylated by bovine brain protein carboxylmethyltransferase.
1986
Selective Deamidation and Enzymatic Methylation of Seminal Ribonuclease / DI DONATO, Alberto; Galletti, P.; D'Alessio, Giuseppe. - In: BIOCHEMISTRY. - ISSN 0006-2960. - STAMPA. - 25:(1986), pp. 8361-8368.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/456008
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