Modifizierung von Glycerinaldehyd-3-phosphat-Dehydrogenase aus Kaninchen-Skelettmuskel mit dem Coenzymanalogen [3-(3-Bromacetylpyridinio)-propyl]-adenosin-pyrophosphat

Modification of glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle by [3-(3-Bromoacetylpyridinio)-propyl]-adenosine pyrophosphate

  • The NAD analogue [3-(3-acetylpyridinio)-propyl] adenosine pyrophosphate forms enzymically inactive complexes with glyceraldehyde-3-phosphate dehydrogenase from yeast and rabbit skeletal muscle. In the latter enzyme four mol of the analogue are bound with equal affinity inhibiting the enzyme in a competitive way: KI = 0.3 mM as compared to the dissociation constant KD=O.6 mм. The brominated derivative [3- (3-bromoacetylpyridinio) -propyl] adenosine pyrophosphate is co­valently bound to both enzymes causing irreversible loss of enzymic activity. Complete inactivation of the enzyme from muscle requires two moles of the analogue per mol of tetramer. The remaining two sites are still able to bind two mol of NAD+ without regain of enzymic activity. In the case of the yeast enzyme four mol of the analogue are bound. Inactivation of the rabbit muscle enzyme is accompanied by the disappearance of two out of four highly reactive sulfhydryl groups; in the yeast enzyme the four active site cysteine residues are still able to react with DTNB1 the reactivity being diminished significantly. Hybrid formation between the native enzymes from yeast and skeletal muscle is not affected by the modification of the enzyme. Similarly the sedimentation properties of the covalently modi­fied enzyme are indistinguishable from those of the native molecule. This indicates that both the native and the irreversibly inhibited enzyme are identical regarding their quaternary structure.

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Metadaten
Author:Gerhard Dietz, Christoph Woenckhaus, Rainer JaenickeGND, Inge Schuster
URN:urn:nbn:de:hebis:30:3-720347
DOI:https://doi.org/10.1515/znc-1977-1-214
ISSN:0939-5075
ISSN:1865-7125
Parent Title (German):Zeitschrift für Naturforschung, C
Publisher:Verlag der Zeitschrift für Naturforschung
Place of publication:Tübingen
Document Type:Article
Language:German
Date of Publication (online):2014/06/02
Year of first Publication:1977
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2024/02/05
Tag:Affinity Labeling; Glyceraldehyde-3-phosphate Dehydrogenase; Hybrid Formation
Volume:32.1977
Issue:1-2
Page Number:10
First Page:85
Last Page:92
Institutes:Medizin
Biochemie, Chemie und Pharmazie / Biochemie und Chemie
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - Namensnennung-Nicht kommerziell-Keine Bearbeitung 3.0