Abstract
Aspergillus niger (ficuum)and the kidney bean purple acid phosphatases retained all the essential amino acids in the active site despite a low degree of total sequence homology. This high degree of homology in the sequence motif ofA. nigerfungal acid phosphatase (Apase6) active site with Kidney bean metallo phosphoesterase (KBPAP) and the absence of the RHGXRXP sequence motif indicates Apase6 to be a metallo-phosphoesterase rather than a histidine acid phosphatase.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Published version (
Free)
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and biophysical research communications
Paper Title
Journal
Date
