ATP citratna lijaza
| ATP citratna lijaza | |
|---|---|
| |
| Kristalna struktura skraćene ljudske ATP-citratne lijaze.[1] | |
| Identifikatori | |
| Simbol | ACLY |
| Entrez | 47 |
| Hugo | 115 |
| OMIM | 108728 |
| RefSek | NM_001096 |
| UniProt | P53396 |
| Drugi podaci | |
| EC broj | 2.3.3.8 |
| Lokus | Hrom. 17 q21.2 |
ATP citratna lijaza je enzim koji posreduje jedan važan korak u biosintezi masnih kiselina.[2] ATP citratna lijaza je veza između metabolizma ugljenih hidrata (kojim se oslobađa energija) i produkcije masnih kiselina.[1]
ATP citratna lijaza je primarni enzim odgovoran za sintezu citosolnog acetil-KoA u mnogim tkivima. Ovaj enzim je tetramer identičnih podjedinica. Produkat, acetil-KoA, se koristi u nekoliko biosintetičkih puteva, uključujući lipogenezu i holesterogenezu.[3] Aktivira ga insulin.[4] ATP-citratna lijaza je takođe odgovorna za katalizu konverzije citrata i KoA u acetil-KoA i oksaloacetat, uz ATP hidrolizu.[1]
U prisustvu ATP-a i koenzima A, citratna lijaza katalizuje odvajanje citrata čime nastaju acetil KoA, oksaloacetat, ADP, i ortofosfat:
- citrat + ATP + KoA + H2O oksaloacetat + Acetil-KoA + ADP + Pi.
Ovaj enzim je ranije bio klasifikovan kao EC 4.1.3.8.[5]
Ovaj enzim se nalazi u citosolu biljki[6] i životinja.
- ↑ 1,0 1,1 1,2 PDB 3MWE; Sun T, Hayakawa K, Bateman KS, Fraser ME (August 2010). „Identification of the citrate-binding site of human ATP-citrate lyase using X-ray crystallography”. J. Biol. Chem. 285 (35): 27418–27428. DOI:10.1074/jbc.M109.078667. PMC 2930740. PMID 20558738.
- ↑ Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS (March 1992). „Cloning and expression of a human ATP-citrate lyase cDNA”. Eur. J. Biochem. 204 (2): 491–499. DOI:10.1111/j.1432-1033.1992.tb16659.x. PMID 1371749. Arhivirano iz originala na datum 2013-01-18. Pristupljeno 2014-01-25.
- ↑ „Entrez Gene: ATP citrate lyase”.
- ↑ Guay C, Madiraju SR, Aumais A, Joly E, Prentki M (December 2007). „A role for ATP-citrate lyase, malic enzyme, and pyruvate/citrate cycling in glucose-induced insulin secretion”. J. Biol. Chem. 282 (49): 35657–35665. DOI:10.1074/jbc.M707294200. PMID 17928289.
- ↑ MeSH ATP+Citrate+Lyase
- ↑ Fatland BL, Ke J, Anderson MD, Mentzen WI, Cui LW, Allred CC, Johnston JL, Nikolau BJ, Wurtele ES (October 2002). „Molecular characterization of a heteromeric ATP-citrate lyase that generates cytosolic acetyl-coenzyme A in Arabidopsis”. Plant Physiol. 130 (2): 740–756. DOI:10.1104/pp.008110. PMC 166603. PMID 12376641.
- 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.
- Lovell SC, Davis IW, Arendall WB, de Bakker PI, Word JM, Prisant MG, Richardson JS, Richardson DC (February 2003). „Structure validation by Calpha geometry: phi,psi and Cbeta deviation”. Proteins 50 (3): 437–450. DOI:10.1002/prot.10286. PMID 12557186.