YEAST PYRUVATE-KINASE - ESSENTIAL LYSINE RESIDUES IN THE ACTIVE-SITE

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dc.contributor.authorIMARAI, M
dc.contributor.authorHINRICHSEN, P
dc.contributor.authorBAZAES, S
dc.contributor.authorWILKENS, M
dc.contributor.authorEYZAGUIRRE, J
dc.date.accessioned2025-01-23T19:25:09Z
dc.date.available2025-01-23T19:25:09Z
dc.date.issued1988
dc.description.abstractYeast pyruvate kinase was purified to near homogeneity and subjected to chemical modification by trinitrobenzenesulfonate and by P1, P2-bis (5'' pyridoxal) diphosphate. Labeled peptides were isolated and their amino acid composition was determined. The results suggest that yeast pyruvate kinase has an essential lysine residue, and that this residue is in a location equivalent to an essential lysine described in the muscle enzyme. Protection experiments indicate that this lysine is located at the nucleotide binding site.
dc.fuente.origenWOS
dc.identifier.issn0020-711X
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99444
dc.identifier.wosidWOS:A1988Q195800018
dc.issue.numero9
dc.language.isoen
dc.pagina.final+
dc.pagina.inicio1001
dc.revistaInternational journal of biochemistry
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleYEAST PYRUVATE-KINASE - ESSENTIAL LYSINE RESIDUES IN THE ACTIVE-SITE
dc.typeartículo
dc.volumen20
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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