Aminoaciltransferaza
Aminoaciltransferaze (EC 2.3.2) su aciltransferazni enzimi koji deluju na amino grupu.[1] Na primer, aminoacil tRNK sintetaze napadaju aminokiseline tako što ih esterifikuju sa korespondirajućom tRNK. Za aktivaciju aminokiselina sa aminoacil-tRNK synthetazom neophodna je hidroliza ATP do AMP plus PPi. Aminoacil-tRNK molekul je blisko srodan sa faktorima elongacije, poput EF-Tu.[2]
Peptidil transferaze su takođe tip aminoaciltransferaza.[3][4] One katalizuju formiranje peptidnih veza, kao i hidrolitički korak koji dovodi do odvajanja novo sintetisanih proteina od tRNK.
- ↑ Donald Voet, Judith G. Voet (2005). Biochemistry (3 izd.). Wiley. ISBN 978-0-471-19350-0.
- ↑ Berg J, Tymoczko JL, Stryer L (2006). Biochemistry (6th ed. izd.). San Francisco: W. H. Freeman. ISBN 0-7167-8724-5.
- ↑ 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.
- 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.
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- Berg J, Tymoczko JL, Stryer L (2006). Biochemistry (6th ed. izd.). San Francisco: W. H. Freeman. ISBN 0-7167-8724-5.