tesA

Summary

Gene Symbol: tesA
Description: acyl-CoA thioesterase 1 and protease I and lysophospholipase L1
Alias: ECK0488, JW0483, apeA, pldC
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Nishijima M, Nakaike S, Tamori Y, Nojima S. Detergent-resistant phospholipase A of Escherichia coli K-12. Purification and properties. Eur J Biochem. 1977;73:115-24 pubmed
    ..However, it differs from the latter in its positional specificity and susceptibility to sodium dodecylsulfate. Possible explanation of the difference of positional specificity of the two preparations is also described. ..
  2. Lee L, Lee Y, Leu R, Shaw J. Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1. Biochem J. 2006;397:69-76 pubmed
    ..The role of Asn73 is proposed to be involved in a loop75-80 switch-move motion, which is essential for the accommodation of substrates with longer acyl-chain lengths. ..
  3. Lee L, Liaw Y, Lee Y, Shaw J. Enhanced preference for pi-bond containing substrates is correlated to Pro110 in the substrate-binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L(1). Biochim Biophys Acta. 2007;1774:959-67 pubmed
    ..Some of the interactions between the enzyme protein and the substrate may be contributed by an attractive force between the Pro110 C-H donor and the substrate pi-acceptor. ..
  4. Cho H, Cronan J. Defective export of a periplasmic enzyme disrupts regulation of fatty acid synthesis. J Biol Chem. 1995;270:4216-9 pubmed
    Escherichia coli thioesterase I (TesA) encoded by the tesA gene is located in the cellular periplasm. The tesA gene was modified by deletion of the leader sequence such that the mature enzyme was instead localized to the cellular cytosol...
  5. Cho H, Cronan J. Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme. J Biol Chem. 1993;268:9238-45 pubmed
    The structural gene for Escherichia coli thioesterase I (called tesA) has been cloned by use of sequence data obtained from the purified protein. The tesA gene was mapped at 530 kilobase pair of the E. coli physical map (minute 11.6 of E...
  6. Lo Y, Lin S, Shaw J, Liaw Y. Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network. J Mol Biol. 2003;330:539-51 pubmed
    ..We have defined these consensus sequence blocks providing a basis for the sub-classification of SGNH-hydrolases. ..
  7. Ichihara S, Matsubara Y, Kato C, Akasaka K, Mizushima S. Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of proteinase and proteinase-defective Escherichia coli mutants. J Bacteriol. 1993;175:1032-7 pubmed
    ..8 min, the gene order being dnaZ-adk-ush-Kmr-purE, which is consistent with the map position of apeA, the gene encoding protease I in Salmonella typhimurium. Therefore, the gene was named apeA...
  8. Karasawa K, Yokoyama K, Setaka M, Nojima S. The Escherichia coli pldC gene encoding lysophospholipase L(1) is identical to the apeA and tesA genes encoding protease I and thioesterase I, respectively. J Biochem. 1999;126:445-8 pubmed
    ..A search involving a data bank showed that the nucleotide sequence of the pldC gene was identical to those of the apeA and tesA genes encoding protease I and thioesterase I, respectively...
  9. Lee L, Chou Y, Chen H, Lee Y, Shaw J. Functional role of a non-active site residue Trp(23) on the enzyme activity of Escherichia coli thioesterase I/protease I/lysophospholipase L(1). Biochim Biophys Acta. 2009;1794:1467-73 pubmed publisher
    ..The protein is dubbed as TAP according to the chronological order of gene discovery (TesA/ApeA/PldC)...

More Information

Publications20

  1. Tyukhtenko S, Litvinchuk A, Chang C, Lo Y, Lee S, Shaw J, et al. Sequential structural changes of Escherichia coli thioesterase/protease I in the serial formation of Michaelis and tetrahedral complexes with diethyl p-nitrophenyl phosphate. Biochemistry. 2003;42:8289-97 pubmed
    ..The present study also demonstrates the important catalytic roles of conserved residues in the SGNH family of proteins. ..
  2. Lo Y, Lee Y, Shaw J, Liaw Y. Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2000;56:756-7 pubmed
    ..85 (7), c = 171.5 (1) A. The crystals diffract to beyond 2.4 A resolution. There is one molecule of molecular weight 20.5 kDa in the asymmetric unit, with a solvent content of 55%. ..
  3. Lee Y, Chen J, Shaw J. The thioesterase I of Escherichia coli has arylesterase activity and shows stereospecificity for protease substrates. Biochem Biophys Res Commun. 1997;231:452-6 pubmed
    ..171 s-1 microM-1). It was concluded that the thioesterase I of E. coli had arylesterase activity and it possessed stereospecificity for protease substrates. ..
  4. Barnes E, Wakil S. Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmityl thioesterase. J Biol Chem. 1968;243:2955-62 pubmed
  5. Bonner W, Bloch K. Purification and properties of fatty acyl thioesterase I from Escherichia coli. J Biol Chem. 1972;247:3123-33 pubmed
  6. Cho H, Cronan J. "Protease I" of Escherichia coli functions as a thioesterase in vivo. J Bacteriol. 1994;176:1793-5 pubmed
    ..However, the gene encoding protease I has the same DNA sequence and genomic location as tesA, a gene that encodes E. coli thioesterase I...
  7. Lo Y, Lin S, Shaw J, Liaw Y. Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement. Biochemistry. 2005;44:1971-9 pubmed
    ..This result strengthens our hypothesis that the switch loop movement is induced by hydrophobic interactions. ..
  8. Wu W, Tyukhtenko S, Huang T. Direct NMR resonance assignments of the active site histidine residue in Escherichia coli thioesterase I/protease I/lysophospholipase L1. Magn Reson Chem. 2006;44:1037-40 pubmed
    ..The sensitivity of detection for the short-lived N(delta1)-H proton was enhanced substantially by improved water suppression, in particular, the suppression of radiation damping via pulsed field gradients. ..
  9. Nie L, Ren Y, Schulz H. Identification and characterization of Escherichia coli thioesterase III that functions in fatty acid beta-oxidation. Biochemistry. 2008;47:7744-51 pubmed publisher
    ..Thioesterase III is proposed to hydrolyze metabolites of beta-oxidation that are resistant to further degradation and that would inhibit the flux through the pathway if they were allowed to accumulate. ..
  10. Karasawa K, Kudo I, Kobayashi T, Homma H, Chiba N, Mizushima H, et al. Lysophospholipase L1 from Escherichia coli K-12 overproducer. J Biochem. 1991;109:288-93 pubmed
    ..The gene responsible for overproduction of lysophospholipase L1 activity was designated as pldC (phospholipid degradation C). Its restriction enzyme map was also different from that of cloned pldB...
  11. Pacaud M, Sibilli S, Bras G. Protease I from Escherichia coli. Some physicochemical properties and substrate specificity. Eur J Biochem. 1976;69:141-51 pubmed
    ..From a detailed study of peptides bonds hydrolyzed, it was concluded that protease I has a stringent requirement for both residues forming the scissile bond, and appears to possess an extended hydrophobic binding site. ..