Ecdysteroid-phosphate phosphatase

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Ecdysteroid-phosphate Phosphatase is the first structure of a steroid phosphate phosphotase containing alpha beta folds common to members of the two histidine (2H)-Phosphatase superfamily with strong homology to the Suppressor of T-cell receptor signaling-1 (Sts-1 PGM) protein. The putative EPPase PGM active site contains signature residues shared by 2H-phosphatase enzymes, including a conserved histidine (His80) that acts as a nucleophile during catalysis. The physiological substrate ecdysone 22-phosphate was modeled in a hydrophobic cavity close to the phosphate-binding site. EPPase PGM shows limited substrate specificity with an ability to hydrolyze steroid phosphates, the phospho-tyrosine (pTyr) substrate analogue para-nitrophenylphosphate ( pNPP) and pTyr-containing peptides and proteins. It has been shown that new protein tyrosine phosphatase (PTP) activity for EPPase. Also, EPPase and its closest homologues can be grouped into a distinct subfamily in the large 2H-Phosphatase superfamily of proteins.

Image

Concerning the sequence for EPPase, the following link will display where in the sequence alpha and beta strands can be found. http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=3C7T Archived 2011-06-15 at the Wayback Machine

Studies of EPPase

In some studies, the genes for EPPase were obtained from a silk moth while a strain of Escherichia coli served as the host for production of this receptor. A plasmid served as the vector for which this gene was implanted into the E.coli strain.

Structure

The structure of EPPase was obtained by x-ray diffraction and the following link provides another picture of the structure. https://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?uid=70358

References

Chen, Y.; Carpino, N.; Nassar, N. "Protein Data Bank (PDB) "Crystal structure of the ecdysone phosphate phosphatase, EPPase, from Bombix mori in complex with tungstate"".

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4:
Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease
and ribonuclease)

3.1.11-16:
Exonuclease

Exodeoxyribonuclease	RecBCD
Exoribonuclease	Oligonucleotidase

3.1.21-31:
Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme;see {{Restriction enzyme}} UvrABC endonuclease
Endoribonuclease	RNase III Drosha: Microprocessor complex Dicer: RNA-induced silencing complex RNase H 1 2A 2B 2C RNase P RNase A RNase Z RNase E 1 2 3 4/5 RNase T1
either deoxy- or ribo-	Nuclease S1 Mung bean nuclease Serratia marcescens nuclease Micrococcal nuclease

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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