ISSN:
1573-4986
Keywords:
sulfatides
;
sulfotransferase
;
pyridoxal 5′-phosphate
;
protein modification
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract In the course of characterization of glycolipid sulfotransferase from human renal cancer cells, the manner of inhibition of sulfotransferase activity with pyridoxal 5′-phosphate was investigated. Incubation of a partially purified sulfotransferase preparation with pyridoxal 5′-phosphate followed by reduction with NaBH4 resulted in an irreversible inactivation of the enzyme. When adenosine 3′-phosphate 5′-phosphosulfate was co-incubated with pyridoxal 5′-phosphate, the enzyme was protected against this inactivation. Furthermore, pyridoxal 5′-phosphate was found to behave as a competitive inhibitor with respect to adenosine 3′-phosphate 5′-phosphosulfate with aK i value of 287 µm. These results suggest that pyridoxal 5′-phosphate modified a lysine residue in the adenosine 3′-phosphate 5′-phosphosulfate-recognizing site of the sulfotransferase.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00731236
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