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Gene Review

cpo  -  non-heme chloroperoxidase

Pseudomonas protegens Pf-5

 
 
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Disease relevance of PFL_3458

 

High impact information on PFL_3458

  • Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively than distant mutations [5].
  • Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3bromo-2-methylpropanoate and ethyl 3phenylbutyrate [6].
  • Directed evolution combined with saturation mutagenesis identified six different point mutations that each moderately increases the enantioselectivity of an esterase from Pseudomonas fluorescens (PFE) towards either of two chiral synthons [6].
  • The second domain was also not required for esterase activity and appeared to be an atypically large linker comprising multiple tandem repeats of a 13-residue motif [7].
  • Esterase EstF1 was encoded by a 999-bp open reading frame (ORF) and exhibited significant amino acid sequence identity with members of the serine hydrolase family [2].
 

Chemical compound and disease context of PFL_3458

 

Biological context of PFL_3458

  • Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones [2].
  • The 1.6kb insert revealed one complete open reading frame, predicted to encode an esterase (320 aa, 34.1kDa) with a pI of 9.86 [3].
  • The results of the experiments for identifying substrate specificity and the inhibitor studies suggest that this enzyme is a carboxylesterase (EC 3.1.1.1) and a serine residue is present at the active site of the esterase, as in the esterases of animal tissues [13].
  • From these studies it is concluded that esterase is not involved in the accumulation of FFA by hydrolysing short chain fatty acid esters; that the highly lipolytic phenotype of LS107d2 is due solely to a single secreted lipase; and that the main FFA accumulated in milk cultures of LS107d2 are C4, C16, C18 and C18: 1 [14].
 

Associations of PFL_3458 with chemical compounds

  • All lipases and the esterase of P. fluorescens GK13 but none of the PHA depolymerases tested hydrolyzed triolein, thereby confirming a functional difference between lipases and PHA depolymerases [15].
  • However, esterase activity was not induced by growing of P. fluorescens DSM 50106 in the presence of several cyclic ketones [2].
  • Directed evolution of an esterase for the stereoselective resolution of a key intermediate in the synthesis of epothilones [16].
  • Among tested p-NP esters, caproate was the most preferential substrate of this esterase [3].
  • The Pro ester was an effective substrate for porcine esterase and was hydrolysed at a rate 20 times greater than the Lau and Dec esters [17].
 

Other interactions of PFL_3458

 

Analytical, diagnostic and therapeutic context of PFL_3458

References

  1. A modular esterase from Pseudomonas fluorescens subsp. cellulosa contains a non-catalytic cellulose-binding domain. Ferreira, L.M., Wood, T.M., Williamson, G., Faulds, C., Hazlewood, G.P., Black, G.W., Gilbert, H.J. Biochem. J. (1993) [Pubmed]
  2. Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones. Khalameyzer, V., Fischer, I., Bornscheuer, U.T., Altenbuchner, J. Appl. Environ. Microbiol. (1999) [Pubmed]
  3. A novel esterase from Ralstonia sp. M1: Gene cloning, sequencing, high-level expression and characterization. Quyen, D.T., Dao, T.T., Thanh Nguyen, S.L. Protein Expr. Purif. (2007) [Pubmed]
  4. Cloning of a gene encoding cinnamoyl ester hydrolase from the ruminal bacterium Butyrivibrio fibrisolvens E14 by a novel method. Dalrymple, B.P., Swadling, Y., Cybinski, D.H., Xue, G.P. FEMS Microbiol. Lett. (1996) [Pubmed]
  5. Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively than distant mutations. Park, S., Morley, K.L., Horsman, G.P., Holmquist, M., Hult, K., Kazlauskas, R.J. Chem. Biol. (2005) [Pubmed]
  6. Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3bromo-2-methylpropanoate and ethyl 3phenylbutyrate. Horsman, G.P., Liu, A.M., Henke, E., Bornscheuer, U.T., Kazlauskas, R.J. Chemistry (Weinheim an der Bergstrasse, Germany) (2003) [Pubmed]
  7. A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces equi acts synergistically with xylanase and is part of a multiprotein cellulose-binding cellulase-hemicellulase complex. Fillingham, I.J., Kroon, P.A., Williamson, G., Gilbert, H.J., Hazlewood, G.P. Biochem. J. (1999) [Pubmed]
  8. An Aspergillus niger esterase (ferulic acid esterase III) and a recombinant Pseudomonas fluorescens subsp. cellulosa esterase (Xy1D) release a 5-5' ferulic dehydrodimer (diferulic acid) from barley and wheat cell walls. Bartolomé, B., Faulds, C.B., Kroon, P.A., Waldron, K., Gilbert, H.J., Hazlewood, G., Williamson, G. Appl. Environ. Microbiol. (1997) [Pubmed]
  9. A systematic approach for yielding a potential pool of enzymes: practical case for chiral resolution of (R,S)-ketoprofen ethyl ester. Kim, J.Y., Choi, G.S., Jung, I.S., Ryu, Y.W., Kim, G.J. Protein Eng. (2003) [Pubmed]
  10. A bacterial esterase is homologous with non-haem haloperoxidases and displays brominating activity. Pelletier, I., Altenbuchner, J. Microbiology (Reading, Engl.) (1995) [Pubmed]
  11. Directed evolution of an esterase from Pseudomonas fluorescens. Random mutagenesis by error-prone PCR or a mutator strain and identification of mutants showing enhanced enantioselectivity by a resorufin-based fluorescence assay. Henke, E., Bornscheuer, U.T. Biol. Chem. (1999) [Pubmed]
  12. Nondenaturing protein electrotransfer of the esterase activity of lipolytic preparations. Brahimi-Horn, M.C., Guglielmino, M.L., Gaal, A.M., Sparrow, L.G. Anal. Biochem. (1991) [Pubmed]
  13. Characterization of Pseudomonas fluorescens carboxylesterase: cloning and expression of the esterase gene in Escherichia coli. Hong, K.H., Jang, W.H., Choi, K.D., Yoo, O.J. Agric. Biol. Chem. (1991) [Pubmed]
  14. Degradation of triglycerides by a pseudomonad isolated from milk: the roles of lipase and esterase studied using recombinant strains over-producing, or specifically deficient in these enzymes. McKay, D.B., Dieckelmann, M., Beacham, I.R. J. Appl. Bacteriol. (1995) [Pubmed]
  15. Substrate specificities of bacterial polyhydroxyalkanoate depolymerases and lipases: bacterial lipases hydrolyze poly(omega-hydroxyalkanoates). Jaeger, K.E., Steinbüchel, A., Jendrossek, D. Appl. Environ. Microbiol. (1995) [Pubmed]
  16. Directed evolution of an esterase for the stereoselective resolution of a key intermediate in the synthesis of epothilones. Bornscheuer, U.T., Altenbuchner, J., Meyer, H.H. Biotechnol. Bioeng. (1998) [Pubmed]
  17. The detection of lipase activity in bacteria using novel chromogenic substrates. Miles, R.J., Siu, E.L., Carrington, C., Richardson, A.C., Smith, B.V., Price, R.G. FEMS Microbiol. Lett. (1992) [Pubmed]
  18. Cloning of Pseudomonas fluorescens carboxylesterase gene and characterization of its product expressed in Escherichia coli. Kim, Y.S., Lee, H.B., Choi, K.D., Park, S., Yoo, O.J. Biosci. Biotechnol. Biochem. (1994) [Pubmed]
  19. Esterase EstA6 from Pseudomonas sp. CR-611 is a novel member in the utmost conserved cluster of family VI bacterial lipolytic enzymes. Prim, N., Bofill, C., Pastor, F.I., Diaz, P. Biochimie (2006) [Pubmed]
 
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