Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.3.16 extracted from

  • Qadota, H.; McGaha, L.A.; Mercer, K.B.; Stark, T.J.; Ferrara, T.M.; Benian, G.M.
    A novel protein phosphatase is a binding partner for the protein kinase domains of UNC-89 (obscurin) in Caenorhabditis elegans (2008), Mol. Biol. Cell, 19, 2424-2432.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.16

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Saccharomyces cerevisiae and Escherichia coli Caenorhabditis elegans

Inhibitors

Inhibitors Comment Organism Structure
AlF4-
-
 Caenorhabditis elegans
BeF3-
-
 Caenorhabditis elegans
additional information SCPL-1 is not inhibited by the typical phosphatase inhibitors NaF, BeCl2, AlCl3, and Na3VO4 Caenorhabditis elegans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ SCPL-1 is dependent on Mg2+ Caenorhabditis elegans

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
 Caenorhabditis elegans
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
 Caenorhabditis elegans 4-nitrophenol + phosphate
-
 ?
UNC-89 + H2O the protein kinase 2 region of UNC-89 specifically interacts with SCPL-1 Caenorhabditis elegans ?
-
 ?

Synonyms

Synonyms Comment Organism
SCPL-1
-
 Caenorhabditis elegans
SCPL-1a isozyme Caenorhabditis elegans
SCPL-1b isozyme Caenorhabditis elegans
small CTD phosphatase-like-1 the protein contains a C-terminal domain phosphatase type domain Caenorhabditis elegans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 around pH 5.0 Caenorhabditis elegans