Crystalline d-Serine Dehydrase

Crystalline D-serine dehydrase.

Purification and properties of D-serine dehydrase from Escherichia coli.

A procedure is described for obtaining crystalline o-serine dehydrase from a mutant of Escherichia coli which produces this enzyme constitutively. The enzyme appears pure by ultracentrifugal and electrophoretic criteria. In sucrose gradients, serine dehydrase sediments to the same position as horseradish peroxidase, indicating a molecular weight of about 40,000. This corresponds closely to its ...

D-serine Dehydrase of Neurospora* by Charles Yanofsky

In a previous publication from this laboratory (l), it was mentioned that cell-free extracts of Neurospora mycelium form considerable amounts of pyruvate and ammonia from m-serine. It was also reported that pyridoxal phosphate stimulates the activity of this system. Results similar to these have recently been obtained by Reissig (2). On further examination of the Neurospora system, it has been ...

D-serine Dehydrase of Neurospora* by Charles Yanofsky

In a previous publication from this laboratory (l), it was mentioned that cell-free extracts of Neurospora mycelium form considerable amounts of pyruvate and ammonia from m-serine. It was also reported that pyridoxal phosphate stimulates the activity of this system. Results similar to these have recently been obtained by Reissig (2). On further examination of the Neurospora system, it has been ...

DEAMINATION OF SERINE II. D-SERINE DEHYDRASE, A VITAMIN Bs ENZYME FROM ESCHERICHIA COLP

Non-enzymatic deamination of serine and cysteine is catalyzed by pyridoxal and certain metal salts at 100” (2). This finding suggested that pyridoxal phosphate might be involved in the enzymatic deamination of these amino acids. Vitamin B, has already been implicated in the desulfhydration of cysteine by rat liver (3) and of cysteine and homocysteine by bacteria (4). Several similarities of cys...