Literature summary for 3.1.3.48 extracted from

Temel, D.B.; Dutta, K.; Alphonse, S.; Nourikyan, J.; Grangeasse, C.; Ghose, R.
Regulatory interactions between a bacterial tyrosine kinase and its cognate phosphatase (2013), J. Biol. Chem., 288, 15212-15228 .

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AAB2	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
[Wzb]-tyrosine phosphate + H2O	Wzb i.e. bacterial tyrosine kinase	Escherichia coli	[Wzb]-tyrosine + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
low molecular weight protein-tyrosine-phosphatase	-	Escherichia coli
Wzb	-	Escherichia coli

General Information

General Information	Comment	Organism
metabolism	regulatory interaction of tyrosine kinase Wzc, and its opposing tyrosine phosphatase, Wzb. The phosphatase Wzb utilizes a surface distal to the catalytic elements of the kinase, Wzc, to dock onto its catalytic domain WzcCD. WzcCD binds in a fashion largely independent of the C-terminal tyrosine cluster near the Wzb catalytic site, inducing allosteric changes therein. YC dephosphorylation is proximity-mediated and reliant on the elevated concentration of phosphorylated YC near the Wzb active site resulting from WzcCD docking	Escherichia coli

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Release 2023.1 (January 2023)