Literature summary for 3.1.3.1 extracted from

Kojima, M.; Ayabe, K.; Ueda, H.
Importance of terminal residues on circularly permutated Escherichia coli alkaline phosphatase with high specific activity (2005), J. Biosci. Bioeng., 100, 197-202.

Search for more literature for 3.1.3.1

Cloned(Commentary)

Cloned (Comment)	Organism
circularly permutated alkaline phosphatase, expression in Escherichia coli	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	alkaline phosphatase is subject to circular permutation with its novel termini at the loops near the active site, and the original termini are linked by a flexible linker. While a permutant with the termini at original residues 407 and 408 is not active, a permutant with termini at residues 90 and 94 shows significant activity. Also the addition of a randomized residue at position 91 and 93 as well as outer peptide epitopes yields several mutants with specific activity comparable to the wild-type enzyme with similar outer peptides	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P00634	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant circularly permutated alkaline phosphatase	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
p-nitrophenyl phosphate + H2O	-	Escherichia coli	p-nitrophenol + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
PHOA	-	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Escherichia coli

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Release 2023.1 (January 2023)