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
- 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. ..
- 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%. ..
- 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. ..
- 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
- Bonner W, Bloch K. Purification and properties of fatty acyl thioesterase I from Escherichia coli. J Biol Chem. 1972;247:3123-33 pubmed
- 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...
- 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. ..
- 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. ..
- 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. ..
- 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...
- 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. ..