Pektatna lijaza
(Preusmjereno sa stranice PGA lijaza)
Pektatna lijaza (EC 4.2.2.2, poligalakturonska transeliminaza, pektinsko kiselinska transeliminaza, poligalakturonatna lijaza, endopektinska metiltranseliminaza, pektatna transeliminaza, endogalakturonatna transeliminaua, pektinsko kiselinska lijaza, alfa-1,4-D-endopoligalakturonsko kiselinska lijaza, PGA lijaza, PPase-N, endo-alfa-1,4-poligalakturonsko kiselinska lijaza, poligalakturonsko kiselinska lijaza, pektinska trans-eliminaza, poligalakturonsko kiselinska trans-eliminaza) je enzim sa sistematskim imenom (1->4)-alfa-D-galakturonan lijaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
Pektatna lijaza | |||||||||
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Identifikatori | |||||||||
EC broj | 4.2.2.2 | ||||||||
CAS broj | 9015-75-2 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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- Eliminativno razlaganje (1->4)-alfa-D-galakturonana kojim se formiraju oligosaharidi sa 4-dezoksi-alfa-D-galakt-4-enuronozil grupama na njihovim neredukujućim krajevima
Enzim je reaktivniji na pektatu, u odnosu na pektin.
Reference
uredi- ↑ Albersheim, P. and Killias, U. (1962). „Studies relating to the purification and properties of pectin transeliminase”. Arch. Biochem. Biophys. 97: 107-115. PMID 13860094.
- ↑ Edstrom, R.D. and Phaff, H.J. (1964). „Purification and certain properties of pectin trans-eliminase from Aspergillus fonsecaeus”. J. Biol. Chem. 239: 2403-2408. PMID 14235514.
- ↑ Edstrom, R.D. and Phaff, H.J. (1964). „Eliminative cleavage of pectin and of oligogalacturonide methyl esters by pectin trans-eliminase”. J. Biol. Chem. 239: 2409-2415. PMID 14235515.
- ↑ Nagel, C.W. and Vaughn, R.H. (1961). „The degradation of oligogalacturonides by the polygalacturonase of Bacillus polymyxa”. Arch. Biochem. Biophys. 94: 328-328. PMID 13727438.
- ↑ Nasuno, S. and Starr, M.P. (1967). „Polygalacturonic acid trans-eliminase of Xanthomonas campestris”. Biochem. J. 104: 178-185. PMID 6035509.
- ↑ Mayans, O., Scott, M., Connerton, I., Gravesen, T., Benen, J., Visser, J., Pickersgill, R. and Jenkins, J. (1997). „Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases”. Structure 5: 677-689. PMID 9195887.
Literatura
uredi- 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.