Literature summary for 3.1.3.1 extracted from

Dealwis, C.G.; Chen, L.; Brennan, C.; Mandecki, W.; Abad-Zapatero, C.
3-D structure of the D153G mutant of Escherichia coli alkaline phosphatase: an enzyme with weaker magnesium binding and increased catalytic activity (1995), Protein Eng., 8, 865-871.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D153G	the mutant has 5fold higher catalytic activity but no change in Km at pH 8.0 in 50 mM Tris-HCl. The mutation also affects Mg2+ binding, resulting in an enzyme with lower metal affinity. The mutation also affects the position of the water ligands of Mg2+ and the loop Gln152-Thr155 is shifted by 0.3 A away from the active site. The weaker Mg2+ binding of the mutant compared with the wild type is caused by an altered coordination sphere in the proximity of the Mg2+ ion and also by the loss of an electrostatic interaction, Mg2+/COO-Asp153, in the mutant	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)