In many different species, lactate dehydrogenase (LDH) constitutes a major checkpoint of
anaerobic glycolysis, by catalyzing the reduction of pyruvate into lactate. This enzyme has …

Malate dehydrogenase (MDH)(EC 1.1. 1.37) catalyzes the conversion of oxaloacetate and
malate. This reaction is important in cellular metabolism, and it is coupled with easily …

The crystal structures of a deglycosylated form of the egg-white glycoprotein avidin and of its
complex with biotin have been determined to 2.6 and 3.0 A, respectively. The structures …

Lactate dehydrogenase (LDH) interconverts pyruvate and lactate with concomitant
interconversion of NADH and NAD+. Although crystal structures of a variety of LDH have …

The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the
archaebacterium Haloarcula marismortui was determined by x-ray crystallography …

7α-Hydroxysteroid dehydrogenase (7α-HSDH; 1 EC 1.1. 1.159) is an NAD+-dependent
oxidoreductase belonging to the short-chain dehydrogenase/reductase (SDR) 1 family. It …

The x-ray structure of a short-chain dehydrogenase, the bacterial holo 3 alpha, 20 beta-
hydroxysteroid dehydrogenase (EC 1.1. 1.53), is described at 2.6 A resolution. This enzyme …

Although the molecular mechanism by which chloroquine exerts its effects on the malarial
parasitePlasmodium falciparum remains unclear, the drug has previously been found to …

Lactate dehydrogenase (LDH) catalyzes the conversion of pyruvate to lactate with
concomitant oxidation of NADH during the last step in anaerobic glycolysis. In the present …

Publisher Summary This chapter discusses structure and stability of hyperstable proteins. It
compares selected proteins from a hyperthermophilic micro-organism with corresponding …