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Literature summary for 3.1.3.16 extracted from

  • Rajagopalan, K.; Dworkin, J.
    Identification and biochemical characterization of a novel protein phosphatase 2C-like Ser/Thr phosphatase in Escherichia coli (2018), J. Bacteriol., 200, e00225-18 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.16

Cloned(Commentary)

Cloned (Comment) Organism
gene pphC or yegK, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain C43 (DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
D46N site-directed mutagenesis, catalytically inactive mutant Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
5,5'-methylene disalicylic acid 13% inhibition at 0.1 mM Escherichia coli
Aurin tricarboxylic acid 48% inhibition at 0.1 mM Escherichia coli
EDTA 62% inhibition at 2 mM Escherichia coli
additional information no inhibition by sanguinarine chloride at 0.05 mM. Poor inhibition by orthovanadate at 0.005-0.05 mM Escherichia coli
okadaic acid 12% inhibition at 0.001 mM Escherichia coli
Sodium fluoride 30% inhibition at 100 mM, 18% at 10 mM Escherichia coli
Sodium phosphate 87% inhibition at 5 mM, 96% at 10 mM Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ slightly activating Escherichia coli
Mn2+ highly activating, PphC (YegK) is a Mn2+-dependent PP2C-like phosphatase, best at 1-2 mM Escherichia coli
additional information no effect by Ca2+, Zn2+, or Ni2+ Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[YegI kinase]-serine/threonine phosphate + H2O Escherichia coli dephosphorylation of autophosphorylated Escherichia coli YegI. Gene yegI encodes the partner kinase YegI of PphC [YegI kinase]-serine/threonine + phosphate
-
 ?
[YegI kinase]-serine/threonine phosphate + H2O Escherichia coli MG1655 dephosphorylation of autophosphorylated Escherichia coli YegI. Gene yegI encodes the partner kinase YegI of PphC [YegI kinase]-serine/threonine + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P76395
-
-
Escherichia coli MG1655 P76395
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain C43 (DE3) by nickel affinity chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PphC displays low preference for pSer/pThr/pTyr peptides, the minimal activity against phosphopeptides is in contrast to the ability of PphC to dephosphorylate the pSer-containing protein substrate beta-casein. PphC may require additional residues for substrate recognition and/or binding that are not present in the phosphopeptides Escherichia coli ?
-
 ?
additional information PphC displays low preference for pSer/pThr/pTyr peptides, the minimal activity against phosphopeptides is in contrast to the ability of PphC to dephosphorylate the pSer-containing protein substrate beta-casein. PphC may require additional residues for substrate recognition and/or binding that are not present in the phosphopeptides Escherichia coli MG1655 ?
-
 ?
[YegI kinase]-serine/threonine phosphate + H2O dephosphorylation of autophosphorylated Escherichia coli YegI. Gene yegI encodes the partner kinase YegI of PphC Escherichia coli [YegI kinase]-serine/threonine + phosphate
-
 ?
[YegI kinase]-serine/threonine phosphate + H2O dephosphorylation of autophosphorylated Escherichia coli YegI. Gene yegI encodes the partner kinase YegI of PphC Escherichia coli MG1655 [YegI kinase]-serine/threonine + phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 25000, recombinant His6-tagged enzyme, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
phosphatase 2C-like Ser/Thr phosphatase
-
 Escherichia coli
PP2C-like phosphatase
-
 Escherichia coli
PphC
-
 Escherichia coli
YegK
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30 37 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8 assay at Escherichia coli

General Information

General Information Comment Organism
evolution enzyme PphC belongs to the eukaryote-like Ser/Thr phosphatases (eSTPs) in Escherichia coli, that have extensive sequence and structural homology to eukaryotic Ser/Thr protein phosphatase 2C (PP2C) phosphatases. But YegK is an atypical PP2C-like phosphatase. Unlike other bacterial PP2C homologues, YegK contains only six of the eight absolutely conserved residues that are involved in metal binding, coordination, and catalysis, instead of eleven. In particular, the amino acid sequence alignment clearly shows that YegK lacks the conserved glycine residue in motif VI and the aspartic acid residue in motif VIII Escherichia coli
physiological function the Escherichia coli eSTP acts to dephosphorylate another Ser/Thr kinase that is encoded in the same operon. Regulatory reversible protein phosphorylation is a conserved mechanism of signaling in all biological systems Escherichia coli