- search hit 1 of 1
Coenzyme binding at different ionization states of cytoplasmic and mitochondrial malate dehydrogenase
- pH-titrations with NADH show two ionizable groups in mitochondrial and cytoplasmic malate dehydrogenase, the first with a pKa in the range 6.8 -8.3 for the mitochondrial and 6.4-7.8 for the cytoplasmic enzyme, the second with a lower limit at 10.2 resp. 11. Comparison with bis-(dihydronicotinamide)-dinucleotide and dihydronicotina-mide-ribosyl-P2-ribose-pyrophosphate instead of NADH indicates that the second alkaline ionization is caused by a residue placed near the adenine binding site of the active centre of the two isoenzymes. Binding studies with NADH and NAD+ give evidence for the participation of a group in the mitochondrial enzyme with pKa 6.8, deprotonation of which is necessary for detectable association of NAD+. In contrast the fixation of NAD+ to the cytoplasmic enzyme is independent of pH.
Author: | Klaus Schwerdtfeger, Christoph Woenckhaus, David M. Parker, John J. Holbrook |
---|---|
URN: | urn:nbn:de:hebis:30:3-719371 |
DOI: | https://doi.org/10.1515/znc-1982-5-632 |
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: | English |
Date of Publication (online): | 2014/06/02 |
Year of first Publication: | 1982 |
Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
Release Date: | 2024/02/05 |
Tag: | Coenzyme Binding; Ionization State; Malate Dehydrogenases |
Volume: | 37.1982 |
Issue: | 5-6 |
Page Number: | 3 |
First Page: | 547 |
Last Page: | 549 |
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): | Creative Commons - Namensnennung-Nicht kommerziell-Keine Bearbeitung 3.0 |