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MetaCyc Reaction: 3.1.1.5

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.1.1.5

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655 : multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1 Inferred from experiment : tesA
Saccharomyces cerevisiae : Neuropathy Target Esterase : NTE1
phospholipase B/lyso-phospholipase : PLB1
phospholipase B/lyso-phospholipase : PLB2
phospholipase B : PLB3

Reaction Locations: periplasmic space (sensu Gram-negative Bacteria)

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.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: lysophospholipase

Enzyme Commission Synonyms: lecithinase B, lysolecithinase, phospholipase B, lysophosphatidase, lecitholipase, phosphatidase B, lysophosphatidylcholine hydrolase, lysophospholipase A1, lysophopholipase L2, lysophospholipase transacylase, neuropathy target esterase, NTE, NTE-LysoPLA, NTE-lysophospholipase

Taxonomic Range: Fungi , Metazoa , Bacteria

Standard Gibbs Free Energy (ΔrG in kcal/mol): 192.38416 Inferred by computational analysis [Latendresse13]

Citations: [vanTienhoven02, vandenBosch81, vandenBosch73, Shapiro53, Dawson58, Quistad03, Lush98, Winrow03]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reaction of [a medium-chain acyl-CoA + H2O → a medium-chain carboxylate + coenzyme A + H+] (3.1.2.19):
i2: lauroyl-CoA + H2O → laurate + coenzyme A + H+ (3.1.2.2)

Instance reaction of [an acyl-CoA + H2O → a carboxylate + coenzyme A + H+] (3.1.2.20):
i1: a 2,3,4-saturated fatty acyl CoA + H2O → a 2,3,4-saturated fatty acid + coenzyme A + H+ (3.1.2.2)

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):
i3: icosanoyl-CoA + H2O → arachidate + coenzyme A + H+ (3.1.2.2)

i4: palmitoyl-CoA + H2O → palmitate + coenzyme A + H+ (3.1.2.2)

i5: stearoyl-CoA + H2O → stearate + coenzyme A + H+ (3.1.2.2)

i6: myristoyl-CoA + H2O → myristate + coenzyme A + H+ (3.1.2.2)

i7: decanoyl-CoA + H2O → decanoate + coenzyme A + H+ (3.1.2.2)

Unification Links: KEGG:R07291 , Rhea:15177

Relationship Links: BRENDA:EC:3.1.1.5 , ENZYME:EC:3.1.1.5 , IUBMB-ExplorEnz:EC:3.1.1.5 , UniProt:RELATED-TO:O07427 , UniProt:RELATED-TO:O42970 , UniProt:RELATED-TO:P07000 , UniProt:RELATED-TO:P0ADA1 , UniProt:RELATED-TO:P39457 , UniProt:RELATED-TO:P53541 , UniProt:RELATED-TO:P78854 , UniProt:RELATED-TO:Q7M3V3 , UniProt:RELATED-TO:Q9P327 , UniProt:RELATED-TO:Q03674


References

Dawson58: Dawson RM (1958). "Studies on the hydrolysis of lecithin by a Penicillium notatum phospholipase B preparation." Biochem J 70(4);559-70. PMID: 13607409

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lush98: Lush MJ, Li Y, Read DJ, Willis AC, Glynn P (1998). "Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man." Biochem J 332 ( Pt 1);1-4. PMID: 9576844

Quistad03: Quistad GB, Barlow C, Winrow CJ, Sparks SE, Casida JE (2003). "Evidence that mouse brain neuropathy target esterase is a lysophospholipase." Proc Natl Acad Sci U S A 100(13);7983-7. PMID: 12805562

Shapiro53: Shapiro B (1953). "Purification and properties of a lysolecithinase from pancreas." Biochem J 53(4);663-6. PMID: 13032127

vandenBosch73: van den Bosch H, Aarsman AJ, de Jong JG, van Deenem LL (1973). "Studies on lysophospholipases. I. Purification and some properties of a lysophospholipase from beef pancreas." Biochim Biophys Acta 296(1);94-104. PMID: 4693514

vandenBosch81: van den Bosch H, Vianen GM, van Heusden GP (1981). "Lysophospholipase--transacylase from rat lung." Methods Enzymol 71 Pt C;513-21. PMID: 7278668

vanTienhoven02: van Tienhoven M, Atkins J, Li Y, Glynn P (2002). "Human neuropathy target esterase catalyzes hydrolysis of membrane lipids." J Biol Chem 277(23);20942-8. PMID: 11927584

Winrow03: Winrow CJ, Hemming ML, Allen DM, Quistad GB, Casida JE, Barlow C (2003). "Loss of neuropathy target esterase in mice links organophosphate exposure to hyperactivity." Nat Genet 33(4);477-85. PMID: 12640454


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 19.0 on Mon Aug 31, 2015, BIOCYC14B.