C-terminal truncation of spinach chloroplast NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase prevents inactivation and reaggregation

DC FieldValueLanguage
dc.contributor.authorScheibe, R
dc.contributor.authorBaalmann, E
dc.contributor.authorBackhausen, JE
dc.contributor.authorRak, C
dc.contributor.authorVetter, S
dc.date.accessioned2021-12-23T15:59:35Z-
dc.date.available2021-12-23T15:59:35Z-
dc.date.issued1996
dc.identifier.issn01674838
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/4010-
dc.description.abstractChloroplast NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase (NAD(P)-GAPDH; EC 1.2.1.13) consists of two types of subunits: GapA and GapB, which are rather similar! except that GapB carries an unique C-terminal sequence extension. Here, we report evidence that this sequence extension might be responsible for aggregation and dark inactivation of the enzyme in vivo. Recently, it had been demonstrated that upon limited proteolysis of the purified 600 kDa enzyme, using the Staphylococcus aureus V8 endoproteinase (Zapponi et al. (1993) Biol. Chem. Hoppe-Seyler 374, 395-402), the C-terminus of GapB can be removed, giving rise to the 150 kDa form. Based on these findings, we analyzed the changed catalytic properties of the enzyme after proteolysis and its ability to reaggregate. The time-course of proteolysis is paralleled by a strong increase in enzyme activity and the appearence of the tetrameric enzyme form, the increase of apparent activity preceding disaggregation. The proteolyzed enzyme is characterized by its increased affinity towards the substrate 1,3-bisphosphoglycerate and thus resembles the fully activated intact enzyme. In contrast to the effector-mediated activation of the intact enzyme, both proteolytic activation and the resulting disaggregation of the high-molecular-weight form cannot be reversed, even by incubation with NAD.
dc.language.isoen
dc.publisherELSEVIER SCIENCE BV
dc.relation.ispartofBIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
dc.subject(S-aureus endoproteinase V8)
dc.subject(spinach)
dc.subjectACTIVATION
dc.subjectaggregation
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.subjectCHENOPODIUM-RUBRUM
dc.subjectchloroplast
dc.subjectINVITRO
dc.subjectINVIVO REGULATION
dc.subjectISOZYMES
dc.subjectLIGHT
dc.subjectlight activation
dc.subjectLIMITED PROTEOLYSIS
dc.subjectNAD(P)-GAPDH
dc.subjectNADP
dc.subjectSEQUENCE
dc.subjectSUBUNIT STRUCTURE
dc.titleC-terminal truncation of spinach chloroplast NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase prevents inactivation and reaggregation
dc.typejournal article
dc.identifier.doi10.1016/0167-4838(96)00074-X
dc.identifier.isiISI:A1996VG78700013
dc.description.volume1296
dc.description.issue2
dc.description.startpage228
dc.description.endpage234
dc.publisher.placePO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
dcterms.isPartOf.abbreviationBiochim. Biophys. Acta-Protein Struct. Molec. Enzym.
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0002-6140-6181-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidScRe288-
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