Literature summary for 3.1.3.1 extracted from

Helland, R.; Larsen, R.L.; Asgeirsson, B.
The 1.4 A crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase (2009), Biochim. Biophys. Acta, 1794, 297-308.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the enzyme at 1.4 A resolution is reported and compared to alkaline phosphatases from other species. The surface does not have the high negative charge density as observed in shrimp alkaline phosphatase, but a positively charged patch is observed around the active site that may be favourable for substrate binding. The dimer interface has a similar number of non-covalent interactions and the crown-domain is the largest observed in known alkaline phosphatases. The catalytic serines are refined with multiple conformations in both monomers. One of the ligands to the catalytic zinc ion in binding site M1 is directly connected to the crown-domain and is closest to the dimmer interface. Subtle movements in metal ligands may help in the release of the product and/or facilitate prior dephosphorylation of the covalent intermediate	Vibrio sp.

Crystallization (Comment)

Organism

crystal structure of the enzyme at 1.4 A resolution is reported and compared to alkaline phosphatases from other species. The surface does not have the high negative charge density as observed in shrimp alkaline phosphatase, but a positively charged patch is observed around the active site that may be favourable for substrate binding. The dimer interface has a similar number of non-covalent interactions and the crown-domain is the largest observed in known alkaline phosphatases. The catalytic serines are refined with multiple conformations in both monomers. One of the ligands to the catalytic zinc ion in binding site M1 is directly connected to the crown-domain and is closest to the dimmer interface. Subtle movements in metal ligands may help in the release of the product and/or facilitate prior dephosphorylation of the covalent intermediate

Vibrio sp.

Organism

Organism	UniProt	Comment	Textmining
Vibrio sp.	-	-	-

Subunits

Subunits	Comment	Organism
dimer	crystal structure	Vibrio sp.

Synonyms

Synonyms	Comment	Organism
alkaline phosphatase	-	Vibrio sp.

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Release 2023.1 (January 2023)