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O-fosfo-L-seril-tRNKSec:L-selenocisteinil-tRNK sintaza
Identifikatori
EC broj	2.9.1.2
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

O-fosfo-L-seril-tRNKSec:L-selenocisteinil-tRNK sintaza (EC 2.9.1.2, MMPSepSecS, SepSecS, SLA/LP, O-fosfoseril-tRNK:selenocisteinil-tRNK sintaza, O-fosfo-L-seril-tRNK:L-selenocisteinil-tRNK sintaza) je enzim sa sistematskim imenom selenofosfat:O-fosfo-L-seril-tRNKSec selenijum transferaza.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

O-fosfo-L-seril-tRNKSec + selenofosfat

\rightleftharpoons

L-selenocisteinil-tRNKSec + fosfat

Ovaj enzim je piridoksal-fosfatni protein.

Reference

↑ Palioura, S., Sherrer, R.L., Steitz, T.A., Soll, D. and Simonovic, M. (2009). „The human SepSecS-tRNA^Sec complex reveals the mechanism of selenocysteine formation”. Science 325: 321-325. PMID 19608919.
↑ Araiso, Y., Palioura, S., Ishitani, R., Sherrer, R.L., O'Donoghue, P., Yuan, J., Oshikane, H., Domae, N., Defranco, J., Soll, D. and Nureki, O. (2008). „Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation”. Nucleic Acids Res. 36: 1187-1199. PMID 18158303.
↑ Aeby, E., Palioura, S., Pusnik, M., Marazzi, J., Lieberman, A., Ullu, E., Soll, D. and Schneider, A. (2009). „The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes”. Proc. Natl. Acad. Sci. USA 106: 5088-5092. PMID 19279205.
↑ Yuan, J., Palioura, S., Salazar, J.C., Su, D., O'Donoghue, P., Hohn, M.J., Cardoso, A.M., Whitman, W.B. and Soll, D. (2006). „RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea”. Proc. Natl. Acad. Sci. USA 103: 18923-18927. PMID 17142313.

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.

Vanjske veze

MeSH O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA+synthase

[1] Palioura, S., Sherrer, R.L., Steitz, T.A., Soll, D. and Simonovic, M. (2009). „The human SepSecS-tRNA^Sec complex reveals the mechanism of selenocysteine formation”. Science 325: 321-325. PMID 19608919.

[2] Araiso, Y., Palioura, S., Ishitani, R., Sherrer, R.L., O'Donoghue, P., Yuan, J., Oshikane, H., Domae, N., Defranco, J., Soll, D. and Nureki, O. (2008). „Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation”. Nucleic Acids Res. 36: 1187-1199. PMID 18158303.

[3] Aeby, E., Palioura, S., Pusnik, M., Marazzi, J., Lieberman, A., Ullu, E., Soll, D. and Schneider, A. (2009). „The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes”. Proc. Natl. Acad. Sci. USA 106: 5088-5092. PMID 19279205.

[4] Yuan, J., Palioura, S., Salazar, J.C., Su, D., O'Donoghue, P., Hohn, M.J., Cardoso, A.M., Whitman, W.B. and Soll, D. (2006). „RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea”. Proc. Natl. Acad. Sci. USA 103: 18923-18927. PMID 17142313.

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