Lipoproteinska lipaza

Lipoproteinska lipaza
Identifikatori
EC broj	3.1.1.34
CAS broj	2594722
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Lipoproteinska lipaza (EC 3.1.1.34, digliceridna lipaza, diacilglicerolna lipaza, postheparinska esteraza, digliceridna lipaza, postheparinska lipaza, diacilglicerolna hidrolaza) je enzim sa sistematskim imenom triacilglicero-protein acilhidrolaza.^[1]^[2]^[3]^[4]^[5] Ovaj enzim katalizuje sledeću hemijsku reakciju

triacilglicerol + H₂O

\rightleftharpoons

diacilglicerol + karboksilat

Ovaj enzim hidrolizuje triacilglicerole u hilomikronima i lipoproteinima niske gustine. On takođe hidrolizuje diacilglicerol.

Reference

↑ Egelrud, T. and Olivecrona, T. (1973). „Purified bovine milk (lipoprotein) lipase: activity against lipid substrates in the absence of exogenous serum factors”. Biochim. Biophys. Acta 306: 115-127. PMID 4703566.
↑ Fielding, C.J. (1970). „Human lipoprotein lipase. I. Purification and substrate specificity”. Biochim. Biophys. Acta 206: 109-117. PMID 5441398.
↑ Greten, H., Levy, R.I., Fales, H. and Fredrickson, D.S. (1970). „Hydrolysis of diglyceride and glyceryl monoester diethers with lipoprotein lipase”. Biochim. Biophys. Acta 210: 39-45. PMID 5466051.
↑ Morley, N. and Kuksis, A. (1972). „Positional specificity of lipoprotein lipase”. J. Biol. Chem. 247: 6389-6393. PMID 5076762.
↑ Nilsson-Ehle, P., Belfrage, P. and Borgström, B. (1971). „Purified human lipoprotein lipase: positional specificity”. Biochim. Biophys. Acta 248: 114-120. PMID 5168777.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Spoljašnje veze

MeSH Lipoprotein+lipase

[1] Egelrud, T. and Olivecrona, T. (1973). „Purified bovine milk (lipoprotein) lipase: activity against lipid substrates in the absence of exogenous serum factors”. Biochim. Biophys. Acta 306: 115-127. PMID 4703566.

[2] Fielding, C.J. (1970). „Human lipoprotein lipase. I. Purification and substrate specificity”. Biochim. Biophys. Acta 206: 109-117. PMID 5441398.

[3] Greten, H., Levy, R.I., Fales, H. and Fredrickson, D.S. (1970). „Hydrolysis of diglyceride and glyceryl monoester diethers with lipoprotein lipase”. Biochim. Biophys. Acta 210: 39-45. PMID 5466051.

[4] Morley, N. and Kuksis, A. (1972). „Positional specificity of lipoprotein lipase”. J. Biol. Chem. 247: 6389-6393. PMID 5076762.

[5] Nilsson-Ehle, P., Belfrage, P. and Borgström, B. (1971). „Purified human lipoprotein lipase: positional specificity”. Biochim. Biophys. Acta 248: 114-120. PMID 5168777.

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