Lizofosfolipaza

Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Lizofosfolipaza
Lizofosfolipaza
Identifikatori
EC broj	3.1.1.5
CAS broj	9001-85-8
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
PMC
Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Lizofosfolipaza (EC 3.1.1.5, lecitinaza B, lizolecitinaza, fosfolipaza B, lizofosfatidaza, lecitolipaza, fosfatidaza B, lizofosfatidilholinska hidrolaza, lizofosfolipaza A1, lizofofolipaza L2, lizofosfolipaza transacilaza, neuropatična ciljna esteraza, NTE, NTE-LysoPLA, NTE-lizofosfolipaza) je enzim sa sistematskim imenom 2-lisofosfatidilholin acilhidrolaza.^[1]^[2]^[3]^[4]^[5]^[6]^[7]^[8]^[9]^[10]^[11] Ovaj enzim katalizuje sledeću hemijsku reakciju

2-lizofosfatidilholin + H₂O

\rightleftharpoons

glicerofosfoholin + karboksilat

Reference уреди

^ Abe, M., Ohno, K. and Sato, R. (1974). „Possible identity of lysolecithin acyl-hydrolase with lysolecithin-lysolecithin acyl-transferase in rat-lung soluble fraction”. Biochim. Biophys. Acta. 369: 361—370.
^ Contardi, A. & Ercoli, A. (1933). „The enzymic cleavage of lecithin and lysolecithin”. Biochem. Z. 261: 275—302.
^ Dawson, R.M.C. (1958). „Studies on the hydrolysis of lecithin by Penicillium notatum phospholipase B preparation”. Biochem. J. 70: 559—570. PMID 13607409.
^ Fairbairn, D. (1948). „The preparation and properties of a lysophospholipase from Penicillium notatum”. J. Biol. Chem. 173: 705—714.
^ Shapiro, B. (1953). „Purification and properties of a lysolecithinase from pancreas”. Biochem. J. 53: 663—666. PMID 13032127.
^ van den Bosch, H., Aarsman, A.J., De Jong, J.G.N. and van Deenen, L.L.M. (1973). „Studies on lysophospholipases. I. Purification and some properties of a lysophospholipase from beef pancreas”. Biochim. Biophys. Acta. 296: 94—104. PMID 4693514.
^ van den Bosch, H., Vianen, G.M. and van Heusden, G.P.H. (1981). „Lysophospholipase-transacylase from rat lung”. Methods Enzymol. 71: 513—521. PMID 7278668.
^ van Tienhoven, M., Atkins, J., Li, Y. and Glynn, P. (2002). „Human neuropathy target esterase catalyzes hydrolysis of membrane lipids”. J. Biol. Chem. 277: 20942—20948. PMID 11927584.
^ Quistad, G.B., Barlow, C., Winrow, C.J., Sparks, S.E. and Casida, J.E. (2003). „Evidence that mouse brain neuropathy target esterase is a lysophospholipase”. Proc. Natl. Acad. Sci. USA. 100: 7983—7987. PMID 12805562.
^ Lush, M.J., Li, Y., Read, D.J., Willis, A.C. and 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: 1—4. PMID 9576844.
^ Winrow, C.J., Hemming, M.L., Allen, D.M., Quistad, G.B., Casida, J.E. and Barlow, C. (2003). „Loss of neuropathy target esterase in mice links organophosphate exposure to hyperactivity”. Nat. Genet. 33: 477—485. PMID 12640454.

Literatura уреди

Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Spoljašnje veze уреди

Lysophospholipase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Abe, M., Ohno, K. and Sato, R. (1974). „Possible identity of lysolecithin acyl-hydrolase with lysolecithin-lysolecithin acyl-transferase in rat-lung soluble fraction”. Biochim. Biophys. Acta. 369: 361—370.

[2] Contardi, A. & Ercoli, A. (1933). „The enzymic cleavage of lecithin and lysolecithin”. Biochem. Z. 261: 275—302.

[3] Dawson, R.M.C. (1958). „Studies on the hydrolysis of lecithin by Penicillium notatum phospholipase B preparation”. Biochem. J. 70: 559—570. PMID 13607409.

[4] Fairbairn, D. (1948). „The preparation and properties of a lysophospholipase from Penicillium notatum”. J. Biol. Chem. 173: 705—714.

[5] Shapiro, B. (1953). „Purification and properties of a lysolecithinase from pancreas”. Biochem. J. 53: 663—666. PMID 13032127.

[6] van den Bosch, H., Aarsman, A.J., De Jong, J.G.N. and van Deenen, L.L.M. (1973). „Studies on lysophospholipases. I. Purification and some properties of a lysophospholipase from beef pancreas”. Biochim. Biophys. Acta. 296: 94—104. PMID 4693514.

[7] van den Bosch, H., Vianen, G.M. and van Heusden, G.P.H. (1981). „Lysophospholipase-transacylase from rat lung”. Methods Enzymol. 71: 513—521. PMID 7278668.

[8] van Tienhoven, M., Atkins, J., Li, Y. and Glynn, P. (2002). „Human neuropathy target esterase catalyzes hydrolysis of membrane lipids”. J. Biol. Chem. 277: 20942—20948. PMID 11927584.

[9] Quistad, G.B., Barlow, C., Winrow, C.J., Sparks, S.E. and Casida, J.E. (2003). „Evidence that mouse brain neuropathy target esterase is a lysophospholipase”. Proc. Natl. Acad. Sci. USA. 100: 7983—7987. PMID 12805562.

[10] Lush, M.J., Li, Y., Read, D.J., Willis, A.C. and 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: 1—4. PMID 9576844.

[11] Winrow, C.J., Hemming, M.L., Allen, D.M., Quistad, G.B., Casida, J.E. and Barlow, C. (2003). „Loss of neuropathy target esterase in mice links organophosphate exposure to hyperactivity”. Nat. Genet. 33: 477—485. PMID 12640454.

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