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Peptidiltransferaza
Identifikatori
EC broj	2.3.2.12
CAS broj	9059-29-4
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

Peptidiltransferaza (EC 2.3.2.12, transpeptidaza, ribosomalna peptidiltransferaza) je enzim sa sistematskim imenom peptidil-tRNK:aminoacil-tRNK N-peptidiltransferaza.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

peptidil-tRNK1 + aminoacil-tRNK2

\rightleftharpoons

tRNK1 + peptidil(aminoacil-tRNK2)

Ovaj enzim je ribozim. Dve neekvivantne ribonukleoproteinske podjednice deluju na neusaglažen način pri peptidnoj elongaciji.

Reference

↑ Rychlik, I. (1966). „Release of lysine peptides by puromycin from polylysyl-transfer ribonucleic acid in the presence of ribosomes”. Biochim. Biophys. Acta 114: 425-427. PMID 5329275.
↑ Rychlik, I., Cerná, J., Chládek, S., Zemlicka, J. and Haladová, Z. (1969). „Substrate specificity of ribosomal peptidyl transferase: 2′(3′)-O-aminoacyl nucleosides as acceptors of the peptide chain on the amino acid site”. J. Mol. Biol. 43: 13-24. PMID 4897787.
↑ Traut, R.R. and Monro, R.E. (1964). „The puromycin reaction and its relation to protein synthesis”. J. Mol. Biol. 10: 63-72.
↑ Voorhees, R.M., Weixlbaumer, A., Loakes, D., Kelley, A.C. and Ramakrishnan, V. (2009). „Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome”. Nat. Struct. Mol. Biol. 16: 528-533. PMID 19363482.

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 Peptidyltransferase

[1] Rychlik, I. (1966). „Release of lysine peptides by puromycin from polylysyl-transfer ribonucleic acid in the presence of ribosomes”. Biochim. Biophys. Acta 114: 425-427. PMID 5329275.

[2] Rychlik, I., Cerná, J., Chládek, S., Zemlicka, J. and Haladová, Z. (1969). „Substrate specificity of ribosomal peptidyl transferase: 2′(3′)-O-aminoacyl nucleosides as acceptors of the peptide chain on the amino acid site”. J. Mol. Biol. 43: 13-24. PMID 4897787.

[3] Traut, R.R. and Monro, R.E. (1964). „The puromycin reaction and its relation to protein synthesis”. J. Mol. Biol. 10: 63-72.

[4] Voorhees, R.M., Weixlbaumer, A., Loakes, D., Kelley, A.C. and Ramakrishnan, V. (2009). „Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome”. Nat. Struct. Mol. Biol. 16: 528-533. PMID 19363482.

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