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. 1998 Feb 13;243(2):471-3.
doi: 10.1006/bbrc.1998.8116.

Conservation of the active site motif in Aspergillus niger (ficuum) pH 6.0 optimum acid phosphatase and kidney bean purple acid phosphatase

E J Mullaney  1 , A H Ullah
Affiliations

Conservation of the active site motif in Aspergillus niger (ficuum) pH 6.0 optimum acid phosphatase and kidney bean purple acid phosphatase

E J Mullaney et al. Biochem Biophys Res Commun. .

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 of A. niger fungal acid phosphatase (Apase6) active site with Kidney bean metallo phosphoesterase (KBPAP) and the absence of the RHG-XRXP sequence motif indicates Apase6 to be a metallophosphoesterase rather than a histidine acid phosphatase.

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