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Article

Deamidation of asparagine residues in a recombinant serine hydroxymethyltransferase.

Archives of biochemistry and biophysics - 15 Dec 1999

di Salvo M L, Delle Fratte S, Maras B, Bossa F, Wright H T, Schirch V

Abstract excerpt

Serine hydroxymethyltransferase purified from rabbit liver cytosol has at least two Asn residues (Asn(5) and Asn(220)) that are 67 and 30% deamidated, respectively. Asn(5) is deamidated equally to Asp and isoAsp, while Asn(220) is deamidated only to isoAsp. To determine the effect of these Asn deamidations on enzyme activity and stability a recombinant rabbit liver cytosolic serine hydroxymethyltransferase was...

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Source

Identifiers

PMID: 10600164
DOI: 10.1006/abbi.1999.1512

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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