Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1990.tb15443.x/fullpdf
Reference53 articles.
1. Nucleotide sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from the mesophilic methanogenic archaebacteria Methanobacterium bryantii and Methanobacterium formicicum. Comparison with the respective gene structure of the closely related extreme thermophile Methanothermus fervidus
2. Isolation and nucleotide sequence of a cDNA clone encoding rat mitochondrial malate dehydrogenase
3. Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity.
4. The three-dimensional structure of porcine heart mitochondrial malate dehydrogenase at 3.0-A resolution.
5. Structure of porcine heart cytoplasmic malate dehydrogenase: combining x-ray diffraction and chemical sequence data in structural studies
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