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1bf6
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bf6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bf6 RCSB], [http://www.ebi.ac.uk/pdbsum/1bf6 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bf6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bf6 RCSB], [http://www.ebi.ac.uk/pdbsum/1bf6 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PHP_ECOLI PHP_ECOLI]] Its real enzymatic activity is not yet known. It was tested for general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities with the following substrates: P-nitrophenyl acetate, L-alanine nitroanilide, P-nitrophenyl sulfate, bis(P-nitrophenyl) phosphate, paraoxon, and P-nitrophenyl phosphate. No enzymatic activity was detected with any of these nonspecific substrates. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 07:52, 25 December 2014
PHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLI
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