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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: thioesterase II

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

Species: Escherichia coli K-12 substr. MG1655

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 [Nie08]. Thioesterase II is one of the thioesterases supporting growth on oleate or conjugated linoleic acid as the sole source of carbon [Nie08].

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 [Li00c].

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]

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: ?

Instance reaction of [an acyl-CoA + H2O → a carboxylate + coenzyme A + H+] (3.1.2.20):
i1: propanoyl-CoA + H2O → propanoate + coenzyme A + H+ (3.1.2.18)

Instance reactions of [a 2,3,4-saturated fatty acyl CoA + H2O → a 2,3,4-saturated fatty acid + coenzyme A + H+] (3.1.2.2):
i2: decanoyl-CoA + H2O → decanoate + coenzyme A + H+ (3.1.2.2)

i3: lauroyl-CoA + H2O → laurate + coenzyme A + H+ (3.1.2.2)

i4: arachidoyl-CoA + H2O → arachidate + coenzyme A + H+ (3.1.2.2)

i5: palmitoyl-CoA + H2O → palmitate + coenzyme A + H+ (3.1.2.2)

i6: stearoyl-CoA + H2O → stearate + coenzyme A + H+ (3.1.2.2)

i7: myristoyl-CoA + H2O → myristate + coenzyme A + H+ (3.1.2.2)

GO Terms:

Biological Process: GO:0009062 - fatty acid catabolic process Inferred from experiment [Nie08]
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

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , 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 1]:

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

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 [Nie08].

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.

In Pathways: photosynthetic 3-hydroxybutyrate biosynthesis (engineered) , (R)- and (S)-3-hydroxybutyrate biosynthesis

Credits:
Imported from MetaCyc 08-Sep-2014 by Caspi R , SRI International
Imported from EcoCyc 16-Sep-2014 by Paley S , 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.

In Pathways: photosynthetic 3-hydroxybutyrate biosynthesis (engineered) , (R)- and (S)-3-hydroxybutyrate biosynthesis

Credits:
Imported from MetaCyc 08-Sep-2014 by Caspi R , SRI International
Imported from EcoCyc 16-Sep-2014 by Paley S , 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]

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


References

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

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

Li00c: 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

Nie08: 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."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, BIOCYC14B.