Title : The beta-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity.

Pub. Date : 2003 Oct

PMID : 16120349






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate. magnesium ion FKBP prolyl isomerase 1B Homo sapiens
2 The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate. Fluorine FKBP prolyl isomerase 1B Homo sapiens
3 The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate. aminomethylenediphosphate FKBP prolyl isomerase 1B Homo sapiens
4 The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate. imidodiphosphonic acid FKBP prolyl isomerase 1B Homo sapiens