黑曲霉（米曲霉）最适pH 6.0酸性磷酸酶和菜豆紫色酸性磷酸酶活性位点基序的保守性。
Conservation of the active site motif in Aspergillus niger (ficuum) pH 6.0 optimum acid phosphatase and kidney bean purple acid phosphatase.
作者信息
Mullaney E J, Ullah A H
机构信息
Southern Regional Research Center, ARS, USDA, New Orleans, Louisiana 70124, USA.
出版信息
Biochem Biophys Res Commun. 1998 Feb 13;243(2):471-3. doi: 10.1006/bbrc.1998.8116.
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.
尽管总序列同源性程度较低，但黑曲霉（米曲霉）和菜豆紫色酸性磷酸酶在活性位点保留了所有必需氨基酸。黑曲霉真菌酸性磷酸酶（Apase6）活性位点的序列基序与菜豆金属磷酸酯酶（KBPAP）具有高度同源性，且不存在RHG-XRXP序列基序，这表明Apase6是一种金属磷酸酯酶，而非组氨酸酸性磷酸酶。
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