Dehydrogenase activities in red blood cells of rabbits made anemic with phenyihydrazinc were assayed. These assays were continued at the time of reticulocytosis and followed through the course of in vivo maturation of the reticulocytes to a younger erythrocyte population. Isocitric, glucose-6-phosphate, and 6-phosphogluconic dehydrogenases were more active in the reticulocytes. Isocitric and gl...

Parts of the primary structure of the NAD-specific glutamate dehydrogenase [L-glutamate:NAD oxidoreductase (deaminating), EC 1.4.1.2] from Neurospora crassa are presented. Segments of the sequence representing 886 unique amino-acid residues have been determined; the largest contains 267 residues. There are only short regions of possible homology between this enzyme and the glutamate dehydrogena...

The primary structure of about half of the protein chain of yeast alcohol dehydrogenase has been determined and compared with the amino-acid sequences of other dehydrogenases. The enzyme is found to be distantly related to horse-liver alcohol dehydrogenase, although these two proteins have different quaternary structures and subunit sizes. Some regions show no significant similarities, but long...

How is retinoic acid produced? In vertebrates, vitamin A, in the form of retinyl esters, is stored mainly in the liver as well as in the lungs, kidneys and bone marrow. Retinol, bound to the retinolbinding protein (RBP), enters the circulatory system in order to reach cells that require retinoic acid. The retinol–RBP complex enters the cells through the RBP receptor (STRA6). Within the cells, r...

Ketoacyl reductases (KRs), hydroxyacyl dehydratases (HDs) and enoyl reductases (ERs) are part of the fatty acid and polyketide synthesis cycles. Their reverse reactions, catalyzed by acyl dehydrogenases (equivalent to ERs), enoyl hydratases (equivalent to HDs) and hydroxyacyl dehydrogenases (equivalent to KRs), are part of fatty acid degradation by β-oxidation. These enzymes have been classifie...