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Distinct structure and activity recoveries reveal differences in metal binding between mammalian and Escherichia coli alkaline phosphatases

Distinct structure and activity recoveries reveal differences in metal binding between mammalian and Escherichia coli alkaline phosphatases

Biochemical Journal 392(Pt 2): 407-415

ISSN/ISBN: 0264-6021

PMID: 16086666

DOI: 10.1042/bj20050509

The amino acids involved in the coordination of two Zn2+ ions and one Mg2+ ion in the active site are well conserved from EAP (Escherichia coli alkaline phosphatase) to BIAP (bovine intestinal alkaline phosphatase), whereas most of their surrounding residues are different. To verify the consequences of this heterology oil their specific activities, we compared file activity and structure recoveries of the metal-free forms (apo) of EAP and of BIAP.

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Accession: 011967956

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