Partial Purification and Characterization of an Aspartate Racemase from Streptococcus faecalis
Year: 1972
Type: article
Abstract: An aspartate racemase has been purified approximately 60-fold from the supernatant fraction of Streptococcus faecalis (ATCC 9790), a gram-positive organism whose peptidoglycan is cross-linked by d-isoasparagine residues. This partially purified preparation racemizes l-alanine about half as rapidly as it racemizes l-aspartate. With l-glutamate as substrate, it exhibits no racemase activity. In the presence of dithiothreitol, the aspartate racemase is remarkably thermostable at pH 6 and pH 8 to 9, but it is thermolabile at pH 7.5. Other properties of the enzyme are described.
Source: Journal of Biological Chemistry
Institution: Harvard University
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1489182117