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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Enzyme: thioesterase II



Gene: tesB Accession Numbers: EG10995 (EcoCyc), b0452, ECK0446

Regulation Summary Diagram: ?

Subunit composition of thioesterase II = [TesB]4

Summary:
Thioesterase II (TesB) is one of a number of thioesterases present in E. coli. The enzyme has relatively broad substrate specificity, cleaving medium- and long-chain acyl-CoA substrates; the best tested substrate was 3,5-tetradecadienoyl-CoA [Nie08a]. Thioesterase II is one of the thioesterases supporting growth on oleate or conjugated linoleic acid as the sole source of carbon [Nie08a].

A crystal structure of the enzyme has been solved at 1.9 Å resolution. The D204 residue was predicted to be in the active site; its importance was confirmed by kinetic analysis of mutants [Li00a].

Strains either lacking or overproducing tesB have no obvious defect [Narasimhan86, Naggert91]. Overproduction of TesB relieves inhibition of fatty acid synthesis by long-chain acyl-ACP molecules that accumulate upon glycerol starvation [Jiang94].

Locations: cytosol

Map Position: [473,525 <- 474,385] (10.21 centisomes)
Length: 861 bp / 286 aa

Molecular Weight of Polypeptide: 31.966 kD (from nucleotide sequence), 32.1 kD (experimental) [Naggert91 ]

Molecular Weight of Multimer: 123.0 kD (experimental) [Naggert91]

pI: 6.58

Unification Links: ASAP:ABE-0001566 , CGSC:17581 , EchoBASE:EB0988 , EcoGene:EG10995 , EcoliWiki:b0452 , OU-Microarray:b0452 , PortEco:tesB , PR:PRO_000024049 , Pride:P0AGG2 , Protein Model Portal:P0AGG2 , RefSeq:NP_414986 , RegulonDB:EG10995 , SMR:P0AGG2 , String:511145.b0452 , Swiss-Model:P0AGG2 , UniProt:P0AGG2

Relationship Links: InterPro:IN-FAMILY:IPR003703 , InterPro:IN-FAMILY:IPR025652 , Panther:IN-FAMILY:PTHR11066 , PDB:Structure:1C8U , Pfam:IN-FAMILY:PF02551

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009062 - fatty acid catabolic process Inferred from experiment [Nie08a]
GO:0006637 - acyl-CoA metabolic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0047617 - acyl-CoA hydrolase activity Inferred from experiment Inferred by computational analysis [GOA01a, Naggert91, Narasimhan86]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ishihama08]

MultiFun Terms: metabolism

Essentiality data for tesB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 07-Oct-2009 by Keseler I , SRI International


Enzymatic reaction of: acyl-CoA thioesterase (thioesterase II)

Synonyms: long-chain fatty acyl thioesterase

EC Number: 3.1.2.20

an acyl-CoA + H2O <=> a carboxylate + coenzyme A + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is irreversible in the direction shown.

Alternative Substrates [Comment 5]:

Summary:
The enzyme was first purified to homogeneity from E. coli B (and there named fatty acyl thioesterase I) [Bonner72]. Km values have been measured for a number of substrates and range between 6 µM for 3,5-dodecadienoyl-CoA and 13 µM for tetradecanoyl-CoA [Nie08a].

Acyl-ACP substrates are hydrolyzed at a much lower rate than acyl-CoA substrates of the same chain length [Spencer78].

Thioesterase II is not inhibited by iodoacetate [Naggert91] or diisopropyl fluorophosphate [Spencer78].

Inhibitors (Unknown Mechanism): diethylpyrocarbonate [Naggert91] , iodoacetamide [Naggert91] , methylene blue [Bonner72]


Enzymatic reaction of: (S)-3-hydroxybutanoyl-CoA thioesterase (thioesterase II)

(S)-3-hydroxybutanoyl-CoA + H2O <=> (S)-3-hydroxybutanoate + coenzyme A + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from MetaCyc 08-Sep-2014 by Caspi R , SRI International


Enzymatic reaction of: (R)-3-hydroxybutanoyl-CoA thioesterase (thioesterase II)

(R)-3-hydroxybutanoyl-CoA + H2O <=> (R)-3-hydroxybutanoate + coenzyme A + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

Credits:
Imported from MetaCyc 08-Sep-2014 by Caspi R , SRI International


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[UniProt08]
UniProt: Removed;
Chain 2 -> 286
[UniProt09]
UniProt: Acyl-CoA thioesterase 2;
Active-Site 58
[UniProt10]
Active-Site 204
[UniProt08]


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b0452 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10995; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bonner72: Bonner WM, Bloch K (1972). "Purification and properties of fatty acyl thioesterase I from Escherichia coli." J Biol Chem 1972;247(10);3123-33. PMID: 4554913

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Jiang94: Jiang P, Cronan JE (1994). "Inhibition of fatty acid synthesis in Escherichia coli in the absence of phospholipid synthesis and release of inhibition by thioesterase action." J Bacteriol 176(10);2814-21. PMID: 7910602

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Li00a: Li J, Derewenda U, Dauter Z, Smith S, Derewenda ZS (2000). "Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme." Nat Struct Biol 7(7);555-9. PMID: 10876240

Naggert91: Naggert J, Narasimhan ML, DeVeaux L, Cho H, Randhawa ZI, Cronan JE, Green BN, Smith S (1991). "Cloning, sequencing, and characterization of Escherichia coli thioesterase II." J Biol Chem 1991;266(17);11044-50. PMID: 1645722

Narasimhan86: Narasimhan ML, Lampi JL, Cronan JE (1986). "Genetic and biochemical characterization of an Escherichia coli K-12 mutant deficient in acyl-coenzyme A thioesterase II." J Bacteriol 1986;165(3);911-7. PMID: 2869026

Nie08a: Nie L, Ren Y, Janakiraman A, Smith S, Schulz H (2008). "A novel paradigm of fatty acid beta-oxidation exemplified by the thioesterase-dependent partial degradation of conjugated linoleic acid that fully supports growth of Escherichia coli." Biochemistry 47(36);9618-26. PMID: 18702504

Spencer78: Spencer AK, Greenspan AD, Cronan JE (1978). "Thioesterases I and II of Escherichia coli. Hydrolysis of native acyl-acyl carrier protein thioesters." J Biol Chem 253(17);5922-6. PMID: 355247

Tseng09: Tseng HC, Martin CH, Nielsen DR, Prather KL (2009). "Metabolic engineering of Escherichia coli for enhanced production of (R)- and (S)-3-hydroxybutyrate." Appl Environ Microbiol 75(10);3137-45. PMID: 19304817

UniProt08: UniProt Consortium (2008). "UniProt version 14.6 released on 2008-12-16." Database.

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc11.