Title : Multiple magnesium ions in the ribonuclease P reaction mechanism.

Pub. Date : 1993 May 25

PMID : 8499432






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The 2"-OH at the site of substrate cleavage may act as a ligand for a catalytically important Mg2+: deoxyribose substitution reduces the apparent number of Mg2+ bound from three to two and increases the apparent dissociation constant for Mg2+ from the micromolar to the millimolar range. Deoxyribose mucin 7, secreted Homo sapiens
2 The 2"-OH at the site of substrate cleavage may act as a ligand for a catalytically important Mg2+: deoxyribose substitution reduces the apparent number of Mg2+ bound from three to two and increases the apparent dissociation constant for Mg2+ from the micromolar to the millimolar range. Deoxyribose mucin 7, secreted Homo sapiens
3 The 2"-OH at the site of substrate cleavage may act as a ligand for a catalytically important Mg2+: deoxyribose substitution reduces the apparent number of Mg2+ bound from three to two and increases the apparent dissociation constant for Mg2+ from the micromolar to the millimolar range. Deoxyribose mucin 7, secreted Homo sapiens